To grow and produce crops under almost any condition, plants need to make good use of all nutrients available to them. While they are masters at absorbing some nutrients from the air and soil, they are struggling with others.

One such problematic element is nitrogen. Even though nitrogen makes up about 80% of the atmosphere, it is mainly present as dinitrogen gas N₂.

This means two nitrogen atoms are tightly bound to one another via three strong and energy-rich bonds. In this form, plants can neither take up the nitrogen nor use any of the nitrogen atoms to make other molecules from them.

Yet, they need nitrogen since it is part of every DNA molecule, protein, the energy provider ATP and many vitamins. Hence, plants need a way to acquire that element in a simple way that does not cost them too much energy.

Enter bacteria.

Diazotrophic bacteria fix nitrogen

The so-called diazotrophs have developed a highly efficient enzyme complex to capture, or fix, dinitrogen from the atmosphere and break up its energy-rich bonds. This complex is the nitrogenase, and all diazotrophs use one of three types of nitrogenase.

The most efficient nitrogenase contains a molybdenum ion at its core, while other nitrogenases use vanadium or iron. These metals are extremely rare in the environment. Hence, depending on which one is available, bacteria regulate which of the three nitrogenases to produce.

After capturing a dinitrogen molecule, the nitrogenase enzyme transfers energy in the form of protons and electrons to it. This eventually breaks up the bond between the two nitrogen atoms and produces two ammonium ions NH₃⁺.

Bacteria then use the ammonium ions for their own growth and share the surplus with their friends and partners. In Nature, several symbiotic relationships exist between bacteria and other organisms which are based around the nitrogen-fixating superpower of bacteria.

Soil bacteria share fixed nitrogen with plants

The best known nitrogen-fixing organisms are soil bacteria from the families Bradyrhizobium, Frankia, Bacillus, Clostridium, Burkholderia and Pseudomonas. These either live freely in the soil or form symbiotic relationships with plants.

Especially important are symbiotic rhizobia like Bradyrhizobium and Frankia. Plants attract these soil bacteria to their roots by sending out special molecules, which the bacteria respond to via their quorum sensing receptors. Within the root network of legume plants, the bacteria then build little nodules in which they live protected from the surrounding.

Within the nodules, bacteria fix and convert nitrogen with their enzyme complexes, which requires a lot of energy. Gladly, the host plant provides this energy in the form of sugars and organic acids that it produces with photosynthesis. The plant then transports these molecules into the root nodules, where the bacteria break them up, extract their electrons and thus gain the necessary energy.

After breaking up the nitrogen using these very electrons, the bacteria transport the produced ammonium from the nodules into the plant. With the ammonium, the plant makes DNA, proteins and vitamins; everything that it needs to grow and produce crops and fruiting bodies. Hence, rhizobia bacteria are highly important for the health of plants as well as crop production and yield.

Marine bacteria can fix nitrogen

Soil bacteria are not the only nitrogen-fixing organisms; marine bacteria are also important for global nutrient cycles. For example, cyanobacteria form long filamentous multicellular organisms, with some cells specialised in nitrogen fixation.

Often, cyanobacteria are closely associated with other marine bacteria with which they share nitrogen. So far, scientists do not fully understand these types of interactions but are sure that nitrogen-fixing organisms are crucial for the marine food web and the survival of many species under water.

When temperatures are high enough and nitrogen concentrations are optimal, you can pretty much see the nitrogen-fixation process. A green blanket on the water surface is a sign for cyanobacteria that power both photosynthesis and nitrogen fixation with the carbon dioxide and nitrogen from the air. This so-called algae bloom is mainly due to cyanobacteria like Aphanizomenon, Dolichospermum, Anabaena and Synechococcus bacteria.

Soil bacteria as biofertilisers for sustainable food production

Since some soil bacteria are so efficient in fixing nitrogen and providing it to the plant, they have also become valuable in agriculture. Some so-called biofertilisers consist of bacteria that are added to soil or plants to build symbiotic relationships with them, helping them grow better and produce bigger crops.

Hence, biofertilisers containing bacteria are an efficient and sustainable way to produce more food and in higher quality. With this, farmers will rely less on synthetic fertilisers while maintaining high crop yields. Additionally, using nitrogen-fixing bacteria as biofertilisers helps protect the health of the soil and the environment.

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Whatever it was, chances are high that part of your food was fermented by microbes. As exceptionally healthy and tasty as fermented foods are, these would not exist if it weren’t for microbes and their fermentation superpowers.

Yet, microbial fermentation is a lot more than processing food and giving it a new taste or aroma. Indeed, depending on who you ask, microbial fermentation means slightly different concepts.

For once, fermentation is a metabolic pathway in some microbes and organisms. It is an energy-saving way to degrade and metabolise substrates and produce complex and energy-rich fermentation products.

Secondly, microbial fermentation describes the process of preserving food based on the fermentation pathway. For this, we let microbes break apart and ferment food in a controlled manner, eventually producing well-known fermented foods, like yoghurt, beer and chocolate.

Lastly, the industrial process of growing microbes in big cultures is often called microbial fermentation. The goal of this process is for microbes to produce a specific product – and often they do so through the fermentation pathway.

As you can see, the different definitions for microbial fermentation are grounded on the same principle: microbes degrading substrates and making fermentation products from them. Here, we will look closer at the biochemistry of microbial fermentation and explore some examples of where this microbial superpower naturally occurs and how we make use of it.

The biochemistry of microbial fermentation

From the view of a biochemist, fermentation is first of all a metabolic pathway to conserve energy. Most organisms gain energy from opening chemical bonds of molecules. This releases the energy-rich electrons that are bound within the bond. They then save these electrons in other molecules or fuel cellular machineries.

Most microbes have one preferred substrate for their metabolism. For many, this is glucose, the same sugar that our cells preferably burn and degrade. By degrading glucose, they (and us) produce several intermediary products, the most important one being pyruvate. This degradation process sets free several electrons, which microbes save in a molecule called ATP. ATP is the main fuel for microbial growth machines, swimming motors or transporters.

Sometimes microbes find themselves in environments with an excess of their preferred substrate. In this case, setting free all the energy would produce a lot of heat, damaging or even burning the cell. Hence, as an alternative, energy-conserving pathway, they switch to fermentation metabolism.

During this pathway, they degrade the substrate only partly, thus not extracting all available electrons from it. Instead, they use one of the intermediary products and bind it to another molecule in an energy-neutral reaction. This conserves the electrons and energy within the fermentation product.

What makes fermentation so fascinating: Many species have unique fermentation pathways. Depending on their genes, they branch off the fermentation pathway at any intermediate and produce different molecules.

For example, from pyruvate, some microbes produce ethanol, which we use for beer or wine production, and others produce lactic acid, like for yoghurt production. Other microbes ferment substrates like citrate or succinate and produce complex molecules like caffeine or colourful biopigments.

By conserving the high-energy electrons in the fermentation products, microbes produce fewer ATP molecules. Hence, they have less energy available at that moment. But if they need energy later, they can break down the fermentation product to extract the electrons. Often though, their energy levels are so high, that they even export the product to get rid of it.

Fermentation is thus a way for microbes to process molecules and conserve energy. Gladly, we learned to make use of this pathway as microbes help us convert energy-rich substrates into beneficial products.

Microbial fermentation for food preservation

One source of energy-rich substrates are carbohydrate and fibre-rich foods, which is why these are some preferred environments for microbes. By fermenting fruits, vegetables, milk and grains, microbes can grow and spread on seemingly any plant-based substrate.

Gladly, we learned to grow microbes and ferment food in controlled environments, making food fermentation one of the oldest human technologies. Throughout history, many cultures have optimised different fermentation processes and created all kinds of products.

Food fermentation can include adding so-called starter microbes to the food or using those microbes that naturally live in the foodstuff. These microbes break apart the carbohydrate component of the foodstuff to fuel their fermentation pathways.

The resulting fermentation products can be beneficial vitamins, antioxidants or molecules that change the aroma, taste, texture or stability of the foodstuff. The degradation and modification of the food itself and the accumulation of fermentation products, over time, make our well-loved cheeses, coffee, bread, chocolate, beer, wine, kombucha, yoghurt or kimchi.

For example, thanks to microbes, cheese and yoghurt taste and smell differently than the original milk. Coffee and chocolate get their complex and unique aromas only thanks to the microbial fermentation of coffee and cocoa beans.

During fermentation, many bacteria produce strong acids from the original substrate. Thus, the resulting food becomes acidic and sour, which prevents other microbes from growing and spoiling the food. That’s why food fermentation became an efficient way to conserve food. Many vegetables, like cabbages, pickles or olives, are thus preserved into sauerkraut or kimchi, sour pickles and olives, and the like. Also making kombucha, kefir or cheese are ways to preserve the original tea or milk.

When fermenting cereals, yeasts mainly produce carbon dioxide or ethanol. Carbon dioxide, for example, in sourdough bread makes the bread rise. In the beer-brewing and wine-making processes, yeast produces ethanol as well as several beneficial and aromatic molecules that give beers and wines their tasteful and diverse aromas.

About the microbes involved in food processing

Each fermented food has a unique community of microbes that changes with the fermentation process over time. With the rise of one microbial species, the pH of the food might change or a certain substrate becomes available, which might kill one species or feed and thus help another one grow.

In many vegetable-based fermentation products, lactic acid bacteria, such as Leuconostoc, Lactobacillus and Weissella, are the primary microbes. They produce acids which prevent food-spoiling microbes from growing. The acids also give the resulting kimchi and sauerkraut their sour and acidic tastes. On the contrary, in alkaline-fermented foods of Asia and Africa and in bean-fermented foods, such as tempeh, miso or natto, Bacillus bacteria are usually responsible for the fermentation process.

In milk fermentation, bacterial cultures are of two types: Lactococcus, Lactobacillus, Leuconostoc and Streptococcus bacteria that acidify the milk. This denatures the milk and produces yoghurt-type products, such as yoghurt, buttermilk and kefir.

As a second step during the cheese-making process, Brevibacterium, Propionibacterium, Debaryomyces, Geotrichum and Penicillium are added. These bacteria and fungi produce more complex molecules and give the ripening cheese its unique flavour, texture and aroma.

For cereal fermentation, yeasts are the most widely used microorganisms, producing beer, sourdough bread, sake and whiskey. For bread-making, the principal yeast is Saccharomyces cerevisiae. Other Saccharomyces species, as well as Torulaspora, Hanseniaspora and Pichia are responsible for fermenting most cereal-based drinks.

How the human body benefits from fermentation

As we’ve learned above, many fermented foods are full of microbes – as long as the food was not heated or pasteurized. Hence, when eating fermented foods, you also take in the microbes in and on the food. And these are ready to settle in your body, feed off your food and do some more fermentation.

After arriving in your gastrointestinal tract, the microbes start digesting part of your food too. They degrade the plant cell structures of vegetables, fruits, cereals, seeds and nuts as well as non-digestible fibres. This releases sugars which gut microbes ferment to short-chain fatty acids and gases, like methane. These fermentation products have beneficial effects on your digestion, mental and gut health as well as your immune system.

Hence, by eating fermented foods you gain beneficial microbes – some of them are the so-called probiotics. And by eating plant-based foods you give your gut microbes the appropriate food to ferment, which is what makes some of them prebiotics.

But this is not the only place where microbial fermentation takes place in your body. For example, Lactobacillus bacteria are the key players within the vaginal microbiome and their fermentation activities influence the health of women.

Within the vaginal tract, host cells provide Lactobacillus with glycogen. From this, the bacterium sets free glucose and ferments it to produce lactic acid and hydrogen peroxide. These molecules decrease the pH creating an acidic environment within the vagina. This acidity kills some pathogenic microorganisms directly and prevents others from growing. Hence, by feeding residential Lactobacillus bacteria, the body helps them grow and in return they protect it.

Microbial fermentation as a pillar of industrial production

The more we learn about microbes, bacteria and their fermentation pathways, the better we can use their metabolic superpowers for our own good. Especially the biotechnology and food industry are making great use of microbial fermentation.

We now grow microbes in big batches and harvest fermentation products, like bioethanol, lactic acid or vitamin B12. In many cases, microbes grow on plant-based products or even ferment waste into usable and, thus, green products. As you can guess, food fermentation based on appropriate starter cultures is taking place on large scales to produce many of our beloved foods.

As such, microbial fermentation is an essential part of our lives. Not only as a fundamental process in cellular metabolism and thus human health, microbial fermentation has become a key pillar in food production and preservation as well as industrial production.

As a sustainable tool to produce plant-based foodstuffs, pharmaceuticals and fuels, microbial fermentation may even play a crucial role in our journey towards a greener and more resilient future. Just another reason to be grateful to microbes and their fascinating superpowers.

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

So, they talked of cocci and bacilli based on the spheres and rods that they saw under the microscope.

And they classified microbes and bacteria based on these shapes.

It came only with later, modern technologies that scientists learned that there was more to bacteria than their shapes. Even though bacteria looked similar, they had different superpowers.

Yet, some of these bacterial superpowers are indeed influenced by their cell shapes.

So, what is it about bacterial shapes? Why do bacteria look differently? And how do the different shapes of bacteria help them survive and thrive?

What gives bacteria their shapes?

To protect themselves from the environment, bacteria as well as all other organisms have cell envelopes. These keep the cellular machines and internal parts together so that a bacterium can function within this envelope.

And this envelope also gives bacteria their shape.

Both Gram-positive and Gram-negative bacteria have a layer of so-called peptidoglycan within their envelope. This peptidoglycan layer is made of sugars that are linked together by very strong bonds. This is why the peptidoglycan layer is pretty rigid and stiff and has a specific shape in each bacterium.

Either on the inside or on the outside, the peptidoglycan layer is linked to the cellular membranes. Together, these make up the bacterial envelope with a specific cell shape.

What different shapes do bacteria have?

Microbiologists have different ways to classify known bacterial shapes. Here, I will introduce you to the bacterial shapes according to what makes the most sense to me.

Rod-shaped bacteria

As the name suggests, these bacteria have a rod or cylindrical shape. Examples of rod-shaped bacteria are Escherichia coli and Bacillus subtilis.

Scientists are also convinced that rod-shaped bacteria are the evolutionary ancestors of all other bacterial shapes.

The shape comes from proteins that form long cables within the bacterial cell. These span out the whole bacterium from one end to the other.

Rod-shaped bacteria grow by two modes that we talk about in Why bacteria divide into two and grow with the help of a strong ring: First, they extend their cell size by growing the peptidoglycan, the cable proteins and the membrane.

Second, the cable proteins determine the middle of the cell, where the bacterium produces a special ring. Eventually, this ring narrows so that the bacterium divides and two bacterial cells form.

Spherical bacteria

The spherical bacteria – or so-called cocci – include many pathogenic bacteria like Staphylococcus aureus, Streptococcus pneumoniae and Neisseria gonorrhoeae.

Microbiologists think that spherical bacteria were once rod-shaped as well. However, spherical bacteria do not have these long cable proteins that extend their cell bodies. Thus, they stay spherical and grow by dividing their spherical cells right in the middle.

However, sometimes the two daughter cells do not completely divide and they stay attached to each other. This is why some spherical bacteria live as so-called diplococci.

Curved bacteria

Curved bacteria have the shape of a comma or banana and are sometimes also slightly twisted. Examples of curved or banana-shaped bacteria are Caulobacter crescentus and Vibrio cholerae.

These curved bacteria usually live in watery environments where there are flows. Here, the curved shape helps the bacteria to align with the flow while staying attached to a surface.

In the case of Caulobacter crescentus, one end of the bacterium is glued to a surface with a strong super glue. When this bacterium divides in the middle, one daughter cell remains attached to the surface, while the other one can swim away and find a new location to settle down.

Spiral bacteria

Spiral bacteria are a mix of rods and curves which give them a helical twist. Hence, these bacteria have a corkscrew shape.

Many pathogenic bacteria use their corkscrew shape to swim through gel-like solutions. This includes Helicobacter pylori and Campylobacter jejuni.

Since spiral – or helical – bacteria are also thinner, they can reach locations that are too narrow for other bacteria to reach. They also use their flagella to push themselves forward and “wriggle” through narrow pores.

Star-shaped bacteria

Some bacteria look even fancier than others: They are real stars – yes, bacteria with a star shape.

While we don’t know much yet about star-shaped bacteria, they belong to the so-called Stella species or are Methylomirabilis oxyfera. These usually grow in freshwater, soil and sewage.

The star shape comes from six little arms that extend out of the bacterial cell. These push and grow to the outside giving these bacteria a shiny star shape.

Why do bacteria have different shapes?

Now that we have seen the different shapes of bacteria, you might ask yourself, why do bacteria have these different shapes? How do they help them?

As always in biology, it comes down to how a property helps a bacterium survive in a certain location. Often, the cell shape gives a bacterium advantages over other bacteria and it is easier for them to settle down and face harsh environments.

For example, spherical cells have the lowest surface-to-volume ratio. This means they have a large envelope surface through which they can take up a lot of nutrients. All this while their cell volume is relatively small. So they don’t actually need that many nutrients. This helps cocci to grow in locations where there are little amounts of nutrients.

On the other hand, rod-shaped bacteria often have flagella. And thanks to their shapes, they are efficient swimmers. This allows them to swim to new places in cases of danger or the lack of nutrients.

Bacterial cell shapes help face harsh environments

Also, straight rod cells can pack into biofilms more efficiently and build organised structures. This helps them colonise different locations and resist dangerous environments.

Many rod-shaped bacteria also form longer filamentous organisms. These stronger and larger structures protect bacteria from being eaten by other organisms. Another advantage of these multicellular organisms is that they allow more cells to attach to surfaces and colonise hosts.

Lastly, both curved and helical bacteria use their shapes to get better around their environments. Curved bacteria grow in watery environments but also in our guts. Here, their shapes help them align with the flow of water or our gut content while they stay attached to a surface or the gut wall. This keeps them at their preferred location and protects them from being flushed away.

Spiral bacteria use a fascinating helical movement to screw through gel-like or viscous fluids. This for example helps pathogens swim through the mucus of our stomach and guts and colonise us and make us sick.

Bacteria and their shapes

Here, we looked at the different shapes that bacteria have and how these help them survive. Bacteria always face harsh and new environments and conditions and only survive if they have the right tools or means.

So, by adapting their shapes, bacteria often have advantages over other bacteria. Plus, they look cool and fabulous!

The post Looking fabulous: Why bacteria need to stay in shape too appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Also, bacteria want to grow and flourish and reproduce. But they are only single cells so that their way of reproduction is unique. They reproduce asexually meaning you only need one parent bacterium to make two daughter bacteria.

When you think about it, bacterial cell division seems very easy: Start with one bacterium, divide it in the middle and you end up with two.

However, the mechanism of cell division is pretty complex and involves at least three tasks:

• the bacterium needs to decide WHERE to divide
• get all the needed machinery to the division site
• produce new cell envelope material to separate the two new daughter cells

How a bacterium starts cell division

As you can imagine, for most bacteria it makes the most sense to divide straight in the middle. Like this, they end up with two daughter cells of the same size.

This means a bacterium needs to find its middle and mark it. While it is not completely clear yet to researchers how bacteria find the exact middle, they know it involves a so-called Z-protein.

This Z-protein can bind two things: itself and the inside of the bacterial cell envelope. But it only binds the cell envelope where it is straight and not bent. And this is only the case in the middle of the bacterial cell envelope.

Hence, the Z-proteins bind themselves in a long chain linked to the straight cell envelope. Eventually, they form a ring on the inside of a bacterial cell. And this so-called Z-ring stays in the middle of the bacterium.

Also, the Z-ring is only stable when bacteria have enough nutrients and do not encounter any stress situations. This reassures that bacteria only divide when they have all the needed supplies.

How bacteria divide and produce two daughter cells

Once this Z-ring is stable, it recruits helper machineries to this now defined division site.

The Z-ring is a sign of an upcoming cell division. Now, the bacterium knows it needs to activate machineries to produce more cell envelope material and become longer. And to increase their cell envelopes, bacteria use ferries, tunnels and bridges to transport lipids into the cell envelope.

Like this, the bacterium becomes longer and can start the actual cell division. At the same time, the Z-ring becomes tighter and the cell envelope gets its natural bend again.

Now, two processes happen at the same time: Bacteria cut open their peptidoglycan envelope to separate the two daughter cells and also produce envelope material to close both cells.

After this happened, we have two daughter cells coming from the same parent. They both share the same cell envelope and genome. This is why we consider them identical twins.

But do all bacteria produce identical twins upon cell division?

Do bacteria always divide in the middle and produce identical daughter cells?

Yes, most bacteria are symmetrical. And when they divide right in the middle, they produce two identical daughter cells.

Researchers could even watch bacteria during this process thanks to amazing microscopy techniques. You can see the single stages of bacterial cell division and how bacteria produce the cell envelope in the image below.

Yet, the bacterium Caulobacter crescentus has two different cell ends. It can stick to a surface with its sticky stalk on one end and have flagella on the other.

This bacterium also starts cell division in the middle like what we discussed above. However, the new daughter cells are now different: one is still glued to the surface and the other one has flagella and can swim away.

Also, the bacterium Helicobacter pylori with its helical shape can never really find its perfect middle. Hence, the Z-ring forms somewhere inside the bacterium and its daughter cells always have different sizes.

And then there are funny bacteria that decided they don’t even need to divide in the middle. Bacteria like Gemmatimonas aurantiaca grow “budding” daughter cells out of their own parent cells. However, researchers don’t understand yet why this bacterium chooses to divide in this asymmetric way.

Another way of asymmetric cell division happens in the bacterium Bacillus subtilis when it produces spores. During the sporulation process, the spore daughter cell grows within the mother cell. In the end, the mother cell bursts to release the spore into the environment. In this case, only one daughter cell comes out of the division process.

Why and how we want to prevent bacteria from dividing

Since cell division is an essential mechanism for bacteria, nature also found ways to inhibit it. Many antibiotics or toxins inhibit the production of cell envelope material or of the Z-ring. Like this, bacteria cannot divide anymore; they cannot grow and die.

However, we also know that some bacteria can find ways around the toxicities of antibiotics or toxins and become resistant to them. Hence, by better understanding how the whole mechanism works, researchers can hopefully find new ways to interfere with bacterial growth and find new weapons in the fight against antimicrobial resistance.

The post Why bacteria divide into two and grow with the help of a strong ring appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

And with an increasing global population, it will be important to find ways to increase the world’s food supply in sustainable ways.

Adding microbial communities, called biofertilizers, to soil can increase crop yield and plant health all without adding any toxic chemicals.

Lucky for us that microbes once again can help save our planet by addressing our global food crisis.

A global challenge

While the global population grows to almost 8 billion people, the land for agriculture remains limited. One way to meet this growing challenge is to increase the quantity of food produced on the same amount of land.

In the past, farmers added expensive chemical fertilizers to their crops. These meant to increase important soil nutrients – specifically nitrogen and phosphorus – and help the plants produce more food.

Unfortunately, these chemicals enter and pollute nearby water systems, harming our health as well as the health of our planet. Plus, producing these chemical fertilizers releases greenhouse gases that add to climate change.

One sustainable method to increase crop production is to add microbial communities to agricultural plants; so-called microbial biofertilizers.

Microbes as biofertilizers

These biofertilizers are soil microorganisms that provide nutrients, stimulate growth, and improve plant health. Also, biofertilizers are more sustainable, less toxic, and cheaper than traditional fertilizers.

Here, we will look at what biofertilizers actually do and how these microbes work for the plants.

Helping plants get nutrients

All living organisms need nitrogen, but not all nitrogen found in the soil is in a useable form. In fact, nitrogen is a major limiting nutrient for plants because most nitrogen in the soil is in a form that plants cannot use.

Hence, microorganisms first need to “fix” the nitrogen and then convert it into a usable form. For this, bacteria make an enzyme called nitrogenase that converts nitrogen from atmospheric nitrogen (N₂) to ammonia (NH₃). Now, plants can absorb this nitrogen form and use it for energy and growth.

Some plants have evolved to work with bacteria to make it easier for them to absorb the fixed nitrogen. For example, the roots of certain legume plants include special root nodules. In these live nitrogen-fixing bacteria called Rhizobia. When chickpea seeds were grown together with these bacteria, their yield increased 250%. Also, adding Bradyrhizobium species to mung bean plants promoted plant growth and yield and plants had a higher tolerance to insecticides.

Cyanobacteria also help plants fix nitrogen. When wheat plants grew together with cyanobacteria species Calothrix ghosei, Hapalosiphon intricatus, and Nostoc species, they grew higher and had more grain. Additionally, co-cultivation with Nostoc or Anabaena species resulted in increased root length and wheat plant nitrogen levels. Cyanobacteria are important nitrogen-fixing bacteria in aquatic environments too, especially for rice production.

Helping plants grow

Besides nitrogen, soil bacteria can provide plants with many nutrients, vitamins, and plant hormones. These are called phytohormones. Phytohormones promote plant growth by acting as signaling molecules to regulate plant metabolism and stress response.

When Rhizobia bacteria grew together with the mustard plant Brassica juncea and produced phytohormones, the plants grew better. Also, in corn (maize), inoculation with Azospirillum brasilense resulted in increased plant growth correlated with elevated phytohormone levels.

Over 80% of Rhizobia bacteria produce the major phytohormone indole-3-acetic acid (IAA). This phytohormone regulates plant growth, cell differentiation, and stress response. Thus, when bacteria secrete indole-3-acetic acid, it promotes root growth. This helps plants take up nutrients better.

In addition to a single bacterial species, communities of microbes help plants stay healthy and grow. Archaea, bacteria and fungi all associate with the roots of plants and synergistically provide nutrients to the plant. Researchers are studying these communities to understand important microbial interactions. The aim is to design microbial communities specific to each crop that promote higher crop production in the future. Just think, one day you could order a biofertilizer optimized for your unique climate, soil, and plant!

Fighting plant enemies

Not only do microbes provide their hosts with nutrients to promote growth, they also protect their hosts from deadly pathogens. Especially fungal pathogens are known enemies that threaten plants.

For example, Pseudomonas and Bacillus strains release toxic chemicals such as hydrogen cyanide to inhibit fungi that infect coffee plants. Other Bacillus strains produce antifungal molecules and simultaneously increase corn (maize) seedling growth. The bacterium Ochrobactrum anthropi TRS‐2 can fight fungi, and application of this bacterium on tea plants decreased brown root rot caused by the fungi Phellinus noxius.

Some bacteria even produce biofilms on the roots of plants as a barrier against invading fungal pathogens!

Agricultural crops are also prone to infection by nematodes, commonly called roundworms. Nematophagous bacteria can deter nematode growth by sending out toxins, and competing for nutrients. For example, Pasteuria penetransbacteria infects nematodes, while Pseudomonas strains can produce antibiotics against nematodes that infect potato plants. No matter the pathogen, soil bacteria have evolved ways to promote and protect their host plant.

Microbial biofertilizers assist our global challenge

As the world’s population increases, we will need sustainable and inexpensive ways to increase agricultural production. Just as microbes add nutrients and flavors to our meals, bacteria can nourish our crops as well. Plus, biofertilizers are a greener, healthier, and less expensive alternative to traditional chemical fertilizers.

So, next time you go out into your garden, think about adding some biofertilizers like compost or manure instead of chemicals to help your fruits and vegetables grow.

Along with bacteria, we can help save the planet!

Take away messages from this week’s article:

• The increasing human population is creating a global food crisis 
• Microbes can act as biofertilizers by providing important nutrients and helping promote plant growth
• Microbial biofertilizers are a sustainable and inexpensive way to increase global food production

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

What’s your New Year’s resolution?

Are you trying to eat healthier by eating microbially fermented foods full of nutrients?

Or do you want to be more friendly to the environment by using green bio-plastics?

Keeping this planet green and healthy is a great New Year’s resolution. And one that microbes can help us with.

For example, microbes can degrade and remove the toxic pollution that we have produced. They do that in a process called microbial bioremediation.

Just another way microbes help save the planet.

Our pollution problem

Oil spills, chemical leaks, industrial discharge. We hear about these types of toxic pollution all too often. Increased urbanization, industrialization, and utilization of natural resources pollute and contaminate the environment, which is unhealthy to humans and the planet.

Unfortunately, it is much easier to spill oil or leak a chemical than it is to clean it up. Especially, if the pollution compound is toxic. Cleaning up these types of pollution is costly and may be harmful to the environment.

Why microbial bioremediation?

How lucky are we that microbes can make cleaning up these messes easier? Our microbial friends can degrade and detoxify environmental pollution. This process is called microbial bioremediation.

Microbes absorb or eat toxic pollutants. They then break them down into harmless compounds. This process is a more cost-effective and environmentally friendly method to clean up toxic pollution.

Cleaning up after oil spills

We use petroleum oil in multiple ways, from powering our cars and homes to manufacturing plastics and medicines. Most petroleum oil is found deep in the ground and it takes much energy and expense to pump the oil to the surface.

Unfortunately, sometimes we spill some of that oil. The 2010 Deepwater Horizon oil spill in the Gulf of Mexico is the largest known oil spill and it released 4.9 million barrels of oil into the ocean! What an environmental disaster!

Petroleum oil is a type of fossil fuel full of different organic compounds called hydrocarbons. They contain hydrogen (“hydro”) and carbon molecules. For us humans, ingesting these compounds would be deadly.

So, when that oil disaster happened in 2010, microbiologists and their microbial friends came to the rescue. Luckily, some microbes have special enzymes that recognize and degrade hydrocarbons into smaller compounds. They then use these smaller compounds to grow and reproduce.

Microbes eating hydrocarbons

Many bacteria can degrade petroleum oil. For example, a special Pseudomonas aeruginosa strain can break down oil droplets and grow on petroleum oil with nothing else to eat.

Additional Pseudomonas strains as well as Bacillus subtilis strains are capable of eating hydrocarbons too.

Researchers have also found communities of bacteria working together to degrade and remove petroleum oil. And they are now developing ways to implement these bacterial communities for cleaning up oil spills from contaminated soil and water.

Fungi are also used for bioremediation, called mycoremediation (“myco” refers to fungus). Researchers discovered 16 different fungi species that degrade hydrocarbons in crude oil.

The superhero fungi Trichoderma viridae, Aspergillus flavus and Varicosporium elodeae have the highest rates of degradation. And the Exophiala xenobiotica fungus degrades a hydrocarbon compound found in car gasoline.

Scientists are working to use these microbes in larger bioremediation projects as greener and cheaper ways to clean up oil spills.

Detoxifying heavy metal contamination

Oil spills are not the only toxic pollution generated by us humans. Through many industrial processes, we release heavy metals such as copper, lead, and mercury. Once in the environment, heavy metals can enter the food supply and accumulate in our bodies. Unfortunately, these can lead to health issues and sometimes even cancer.

Removing heavy metals from contaminated water and soils is costly, time-consuming, and ineffective at low concentrations of the contaminate. Good thing microbes can make this process faster and more efficient.

They help remove heavy metals through a process called biosorption. Microbial cell walls are made up of proteins and sugars with a slightly negative charge. Metals have a positive charge.

Thus, microbes can attract and bind these toxic metals. This means microbes act like magnets and pull out the toxic metals from the environment.

Many microbes can absorb a variety of metals. But these microbes also need to protect themselves from toxic metals. For this, they have special enzymes that transform the metals into less toxic forms inside the cell.

However, even microbes cannot survive if the concentration of toxic metals is too high. So, it is important to find microbes that can tolerate high levels of metals and detoxify them. Scientists have discovered some Aspergillus species that can survive high concentrations of copper and nickel metals.

These microbes must also be superb at decontaminating. One rockstar strain of Aspergillus flavus removed over 97% of mercury contamination. And two Pseudomonas species strains removed over 75% of copper, lead, and zinc contamination. Microbes like these will be vital for removing future heavy metal contamination.

Microbes creating a cleaner future

There are a lot of toxic materials in our world. As human activity increases, so too does the amount of toxic pollution we create on our planet. The results of oil spills and heavy metal contamination hurt our human health as well as the health of our planet.

Luckily, microbes have evolved ways to survive and detoxify these types of pollution. Our microbial friends can help remove these toxins and clean up messes created by us. By harnessing the power of microbes, bioremediation projects address our pollution problem and work to make our planet a greener and healthier place. And that’s a great New Year’s resolution!

Along with microbes, we can save the planet!

Take away messages from this week’s article:

• Toxic pollution is a major problem for the health of humans and our planet
• Microbes can detoxify environmental pollution in a process called microbial bioremediation
• Microbial bioremediation is an environmentally friendly and relatively inexpensive way to clean up toxic pollution

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

They don’t have eyes to see what is going on.

Neither do they have ears to hear a foe approaching.

And yet they seem to know exactly what is happening around them.

How is that possible?

In other articles, we already looked at different mechanisms of how bacteria sense their environment. And we learned about various ways bacteria use to know what is going on around them.

Here, we will look at another one of these mechanisms. A mechanism in which bacteria destroy proteins to understand the environment and adapt to it.

But before we can look at why bacteria destroy proteins, we first need to understand how bacteria produce proteins.

Bacteria need proteins to produce proteins

Every living cell, like a bacterial cell or a human cell, contains DNA. And the DNA contains many different sections, which are genes. These genes are the templates for ALL proteins that a cell can produce.

A cellular machine called the polymerase (bright blue in the figure below) recognizes the start of a gene (yellow), before it transcribes this gene into a string of mRNA (grey). Next, a ribosome reads the mRNA fragment and translates it into a protein (yellow).

This is how every living cell produces proteins from DNA.

Now, we will focus on the first step: when the polymerase recognizes the start of a gene.

Bacteria need proteins to regulate protein production

When you think about it, bacteria do not always need all genes and all proteins. Just as you don’t need an umbrella when it is sunny outside, but it is always good to keep it handy. Similarly, bacteria have heaps of genes on that long string of DNA and they need some of them only under certain circumstances.

For this, all living cells have regulators. These regulators make sure that the polymerase only produces mRNA from genes that are required at a specific time point.

And these regulators come in two forms: activators and repressors.

Activators activate genes

Sometimes, the polymerase cannot recognize a specific gene on its own. This is when the polymerase needs an activator (green). 

An activator is a protein that binds to a specific gene only when needed. This attracts the polymerase to this gene so that it produces mRNA from that gene. Like that, an activator ensures that bacteria only produce certain proteins when needed.

This means something else needs to activate the activator at a specific time point. And while some activators are activated by specific systems as explained in How bacteria sense their environment, sometimes protein-destroying systems are involved. More about that below.

Repressors deactivate genes

Repressors (dark blue) do exactly the opposite of activators. These proteins bind specific genes right at the start. This blocks the polymerase from binding the start of that gene and from producing mRNA.

But when the bacterium needs a specific protein, the polymerase has to recognize and bind that specific gene. At that point, the bacterium has to get rid of the repressor.

So, let’s have a look at how bacteria gain access to genes that need activators or are blocked by repressors.

Bacteria destroy proteins to understand the environment

The environment constantly changes for a bacterium. So, all the time, a bacterium needs to produce certain proteins to handle these new situations. Just as you take your umbrella when it is raining suddenly.

This is when the bacterium needs the polymerase to recognize a specific gene to make mRNA from it.

To get rid of a repressor or to activate an activator when needed, bacteria came up with a simple mechanism: protein destruction.

Yes, to produce proteins, sometimes bacteria destroy proteins.

Proteins that destroy proteins are called proteases and these work like molecular scissors. Proteases cut proteins in at least one specific location. This makes the protein fall apart and become kaput. 

When do bacteria destroy proteins?

Different bacteria developed various mechanisms when to destroy specific proteins. And researchers start to understand more and more about this way of regulation.

So, let’s have a look at a few cool examples of bacteria destroying proteins.

Radiation leads to protein destruction and survival

For example, the fascinating bacterium Deinococcus deserti has genes to cope with radiation and desiccation. However, the bacterium does not need to produce these proteins when there is no radiation or desiccation.

Under these circumstances, the repressor D (dark blue in the figure below) blocks these genes and makes sure the polymerase cannot recognize them.

But as soon as the bacterium is hit with radiation (lightning), the radiation activates the protease M (red). This protease can now bind the repressor D and destroy it. Now, that the repressor does not block the radiation genes anymore, the polymerase can recognize the genes and produce mRNA from them. Now, the ribosome produces proteins (yellow) that cope with the radiation. 

And this is how the bacterium Deinococcus deserti destroys proteins to survive. And yes, this bacterium has the superpowers to withstand radiation and desiccation like no other bacterium.

Antibiotics lead to protein destruction and resistance

In another example, Staphylococcus aureus has a similar mechanism to cope with antibiotics and become resistant. 

In the membrane of this bacterium sits the protease R (red) that is generally inactive. However, when the bacterium meets antibiotics (green molecules), the antibiotics change R. 

Now, the protease falls into the inside of the bacterium and destroys its target protein. This is the repressor I (dark blue), which sits and blocks a certain gene. After protease R destroyed repressor I, this gene is unblocked and the bacterium produces a protein (yellow) that cleaves the antibiotic. 

And this is how Staphylococcus aureus becomes resistant to antibiotics by destroying proteins.

Heat leads to protein destruction and survival

But bacteria do not only destroy repressors. They also use a similar mechanism to activate their activators. 

Generally, to keep an activator inactive, another protein is involved. This is the so-called anti-activator since it captures the activator and inhibits it from functioning. So, for the activator to become active and to bind its specific gene, the anti-activator needs to go. And this is exactly what bacteria do.

For example, in the soil bacterium Bacillus subtilis, the anti-activator Y (dark blue) captures the activator S (green). Plus, Y brings S to the cellular garbage machine (purple) to destroy this protein.

However, as soon as it is getting too hot for the bacterium, Y becomes unstable. So unstable, that it cannot hold S anymore. This means S gets freed, binds its favorite genes and leads the polymerase to them. Now, the bacterium produces proteins (yellow) that help the bacterium to cope with the damage from the heat.

And this is how Bacillus subtilis destroys proteins to cope with heat.

Destroying proteins means bacteria can survive

Here we explored three different ways of how bacteria destroy proteins for their own benefit. Interestingly, the benefit always handles the incoming signal which is often a sign of stress.

Like in Deinococcus deserti, radiation activates protein destruction that leads to protein production. And these new proteins now handle the damage after the radiation attack.

Or in Staphylococcus aureus; antibiotics activate a specific protease that destroys a repressor. Now, the produced proteins are meant to destroy the harmful antibiotics.

So by closing these circles, bacteria found efficient ways of how to read their environment and adapt to it.

Interestingly, most bacteria seem to use similar mechanisms. This means, the better we understand the way most bacteria work, the better chances we have to fight the nasty ones. So we need to keep researching the good bacteria, to understand the bad guys too!

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

What is bacterial sporulation?

When a bacterium sporulates, it transforms from a rod-shaped bacterial cell (4-10 μm long) to a round, spherical spore (1-1.5 μm long).

Bacterial spores are surrounded by thick layers of cell wall material or peptidoglycan and many layers of proteins. These make the spore highly resilient and shield it from all kinds of environmental assaults, including UV radiation, desiccation and antibiotics. Within the spore, it protects the genetic material of the parent bacterium.

Now the spore is metabolically dormant. This means that the cell has stopped all activities which require energy, like growth and development.

Spores can remain stable for extremely long periods of time. In fact, researchers found Bacillus spores dating back almost 25 million years in the abdomen of extinct bees preserved in Dominican amber. Other samples date back 250 million years from salt crystals.

Why study sporulation?

To date, most studies aim to understand sporulation in the model bacterium Bacillus subtilis. Bacillus subtilis is a Gram-positive bacterium with a thick layer of peptidoglycan outside the cellular membrane.

One of the major reasons why is it relatively easy to study sporulation in Bacillus subtilis is its natural ability to take up foreign DNA and integrate it into its genome. This provides scientists with a wide range of tools for gene editing in Bacillus subtilis. And they can study the functions of different molecules in space and time during sporulation.

Some bacterial spore-formers can also be pathogenic in a human or animal host.

Examples include Bacillus anthracis (the causative agent of anthrax), Clostridium difficile (implicated in colon disease) and Clostridiumm botulinum (implicated in food poisoning). Spores of these pathogenic bacteria can secretly survive inside the host due to their ability to withstand harsh environments. But once they get access to nutrients, they germinate again and become viable bacteria. These bacteria can then release lethal toxins to cause diseases in their respective hosts.

There is some good news for the food lovers too though! Spores of a strain of Bacillus subtilis, Bacillus subtilis (natto) are used to ferment soybeans in a traditional Japanese dish called natto. The critical process in natto preparation is the germination of spores which then use nutrients from the soybeans to ferment them. The dish with its powerful smell and flavor is definitely for the bold!

How does sporulation work?

Normally, a bacterial cell divides in the middle to produce two identical daughter cells. Researchers call this process binary fission or vegetative growth.

But when a bacterium sporulates, the cell divides closer to one end of the cell, near a pole. This leads to the formation of two daughter cells of different sizes. The smaller cell is the forespore and the larger cell is the mother cell.

The two cells are separated by a wall made by the invagination of the cell membrane and the peptidoglycan. This wall is the septum.

Cell division leads to separation between spore and mother cell

Surprisingly, the wall separating the two daughter cells is almost four times thinner during sporulation than during vegetative growth (~22 nm vs ~80 nm).

Scientists have always wondered why the cell would need a thinner septum during sporulation. One reason can be that the forespore and the mother cell need to communicate with each other and exchange certain metabolites. A thinner septum can make this a lot easier because channels don’t have to go through a thick wall.

Another reason could be that the thinner septum is likely more flexible and easier to bend and stretch. Hence, the mother cell can move forward to engulf the forespore so that it is completely inside the mother cell.

Transporting DNA into the spore

When a bacterial cell divides vegetatively, it splits the bacterial DNA equally into two daughter cells.  But an interesting phenomenon occurs during sporulation.

The DNA is trapped at the septum such that the forespore has only 1/3^rd of the DNA and the remaining 2/3^rd stays in the mother cell. A transporter then pumps the rest of the DNA from the mother cell to the forespore.

Packing the whole DNA into the small volume of the forespore probably increases the turgor pressure in the forespore. Hence, the forespore inflates like air in a balloon to give it an ovoid shape.

Bringing the spore inside the mother cell

A critical process during endospore formation is when the mother cell engulfs the forespore. This means that instead of lying side by side, the forespore is now within the mother cell.

To engulf the forespore, the mother cell has to overcome two barriers:

(1) the peptidoglycan that surrounds the bacterial cell on the outside (shown by blue circles in the figure below), and

(2) the septum (also peptidoglycan) that separates the two cells (shown by green circles in the figure below).

But the septum and the bacterial cell envelope are also connected. At this so-called leading-edge the two peptidoglycan structures meet. Here, critical activity happens.

First, enzymes within the forespore (denoted by ‘1’ in the figure) make a new bond with the cell wall ahead of the leading edge. With a new bond between the two, the old bond is no longer needed. Thus, enzymes in the mother cell break this old bond (denoted by ‘2’ in the figure).

Like this, the mother cell can slowly move around the spore until it completed warps around it.

Wrapping the spore in a thick coat

Once the mother cell engulfed the forespore completely, the spore needs to mature. For this, the mother cell builds thick and protective layers around the spore to protect it from the environment.

Ultimately, the mother cell lyses and dies and releases the mature spore into the environment. Only when the environmental conditions become favourable again, spores germinate and normal vegetative growth cycle starts again. 

Bacterial sporulation – a tightly regulated process

Although the process of sporulation sounds pretty simple, it can be extremely challenging to comprehend from the point of view of the bacterial cellular machinery. More than 500 genes are active only during sporulation. And these are not active during vegetative growth.

Also, some genes are only active in the mother cell and others only active in the forespore. And each stage of spore formation needs to be tightly regulated!

The studies of spore formation in Bacillus subtilis have undoubtedly increased our appreciation of what else bacteria are capable of.

However, there are still many unanswered questions and unknown genes during sporulation that we need to study.

Also, we need to expand these studies to understand sporulation in pathogenic spore-formers like Clostridium difficile and Bacillus anthracis so that we can develop treatments for these disease-causing organisms!

Recent sequencing analysis of the human gut microbiota also indicate that around 50-60% of bacteria in a healthy host intestine are spore-formers. But we still don’t understand the functional and physiological relevance of the majority of them.

There is definitely lots to explore and understand about this one-of-a-kind process of sporulation in bacteria!

The post Sporulation in Bacillus subtilis: A strategy for bacterial hibernation appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

If you are like me, you would make sure to always have your stock filled with this delicacy.

Especially in tough times, you need it more than ever. And you are trying to hide the chocolate from yourself. Yet, you would always find it again and indulge in its sweet-bitter taste that feels like home to you.

But did you know that chocolate, as well as other foods like beer and wine and bread, would not taste as we know it if it wasn’t for our little microbial friends?

That bacteria and microbes actually make the chocolate taste because they produce certain molecules that give it its flavour?

So, next time you enjoy your piece of chocolate, be grateful to bacteria and their superpowers for providing you with such a delicious fermentation product.

Where does chocolate come from?

It all starts with cocoa beans.

Cocoa beans are the seeds of the fruit pod of the tree Theobroma cacao that grows in tropical regions. These beans usually grow within the slimy white-creamy pulp inside the pod.

When the pods are ripe, people harvest and open them. They take out the beans and the pulp from the pod and leave them in the sun to ferment. This takes up to a week, during which the beans are regularly moved to avoid the growth of toxic fungi.

When the beans are dry, they are roasted to kill the remaining bacteria. This process is also important for the flavour of the beans. Then the beans are crushed into cocoa nibs and separated into cocoa powder and cocoa butter and processed into delicious chocolate.

Which bacteria are involved in cocoa fermentation?

When growing on the tree, the inner of the fruit pod is free of microbes. Only the surface of the pod is covered by different bacteria, yeasts and fungi. This consortium of microorganisms is the co-called COCOBIOTA.

When opening the pods, the microbes from the outside come in contact with the inner pulp where they start doing their magic. Without the microbial activity, the pulp is full of sucrose and citric acid and tastes very “sugary acidic and really good. Really unexpected.” as our graphical wizard, Noémie knows from her own experience.

Interestingly, cocoa fermentation is a naturally occurring process, so no artificial bacterial starter culture is added. Only those microbes that are present on the pod ferment the beans.

And scientists found that the superheroes of chocolate fermentation are lactic acid bacteria like Lactobacillus fermentum and Acetobacter pasteurianus and the yeasts Saccharomyces cerevisiae, Hanseniaspora thailandica, Hanseniaspora opuntiae and Pichia kudriavzevii. Also, many other microbes, that are still not well characterised, are involved in the process.

What happens during cocoa fermentation?

Since the inner pulp of the bean is so acidic, not many bacteria grow on it. However, yeasts and lactic acid bacteria love this kind of sour environment. So, they grow and metabolise the pulp.

First, yeast enzymes break down the sucrose of the pulp into the sugars glucose and fructose.

Next, different yeast strains metabolise the glucose and fructose and produce ethanol from the sugars. This is the actual fermentation process. In the next step, lactic acid bacteria make acetic acid and lactic acid from the ethanol.

Due to the metabolic activity of the microbes, the temperature of the pulp rises. Yeasts generally do not like this warmth and die.

Instead, other microbes break down the citric acid which makes the pulp less acidic. Now it is an environment that is very friendly for other bacteria so that bacteria like Bacillus, and fungi, as for example Penicillium citrinum and Aspergillus fumigatus start growing.

This consortium of microorganisms produces several compounds that diffuse into the cocoa beans. Without the bacterial activity, the raw beans “are definitely far from chocolate taste” as Noémie put it.

What chocolate-tasting molecules do bacteria produce during cocoa fermentation?

Scientists are just starting to understand the microbial network and metabolism that create the chocolate taste. You can understand the bacterial metabolism as the following phenomenon.

When bacteria live in an environment with an overload of nutrients (like within the pulp full of sugar), they switch their metabolism to high activity. In this mode, bacteria use their normal metabolism to grow and divide and be happy. On top of that, they have all that excess sugar with which they fill up the cell storage for bad times. And from these stored sugars, they produce additional fancy molecules, so-called secondary metabolites.

Imagine the sugars as your monthly salary. In normal times, you pay all your basic monthly bills, like rent, electricity etc, and probably put the rest in your savings. When you get a massive paycheck and swim in cash, you do all that as well, plus you buy some additional fancy stuff that you don’t really need to survive. This additional stuff represents those secondary metabolites.

Secondary metabolites are often super complex molecules and certain bacteria even produce unique compounds that no one else produces. For example, antibiotics are secondary metabolites as well and so are certain probiotics.

Bacteria produce the right mix for the chocolate taste

In the case of chocolate, the right composition of the secondary metabolites is important to give chocolate its unique taste.

For example, the bitter taste of chocolate comes from caffeine and theobromine. These compounds are especially important if you prefer chocolate with higher cocoa content as it contains more caffeine and less sugar.

Another group of secondary metabolites that microbes produce during cocoa fermentation is polyphenols. Polyphenols are also prebiotics so they are actually beneficial for our health. You can find other polyphenols also in some fruits, nuts, red wine and, obviously, chocolate.

In all, by producing the right mix of these secondary metabolites, bacteria and fungi change the taste of the cocoa bean into the delicious chocolate flavour that you are familiar with.

Thank bacteria for the delicious chocolate taste

And to make you feel better when enjoying your chocolate: Researchers found in animal and human studies that cocoa itself has health benefits. After eating cocoa, people showed lower rates of cardiovascular disease, diabetes and vasodilation which might even have positive impacts on learning and memory regions.

However, as always when it comes to diet, quantity is key ?

So, the next time you enjoy your chocolate, be grateful to bacteria and their chocolatey superpowers!

The post Bacteria are responsible for the delicious chocolate taste appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world