Tag: Food Science

7 Myths and Misconceptions About Coffee (2024)

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Coffee is one of the most widely consumed psychoactive beverages on the planet. Nearly every country, region, and culture has its own unique way of preparing and consuming coffee. There’s nothing simple about coffee. Those beans in your kitchen are the sum total of a complex series of interactions between international corporations, roasters, shippers, marketers, wholesalers, and even the growers who put the seeds in the ground. It’s complicated.

Below we bust some of the most common coffee myths and misconceptions, to help you become a more informed consumer of this deliciously bitter elixir.

We’re seriously wired here at WIRED. Be sure to check out our guide on How to Make Better Coffee at Home, or take a look at our coffee-related buying guides to the Best Espresso Machines, the Best Coffee Subscriptions, and the Best Coffee Grinders.

Updated March 2024: Added a couple new myths, updated links and copy throughout.

1. Coffee Is Not a Bean

Coffee isn’t a bean, or a legume like many other foods we call beans. It’s a seed! Technically, it’s the endosperm (pit) of a berry. Initially, it’s wrapped in a thin red fruit that’s peeled off during the cleaning process. Then it’s a light silvery green color until it’s roasted.

That doesn’t mean you can plant your beans and grow your own coffee trees. The beans we grind up and brew are not plantable anymore, due to the roasting. Even if they were, it can take years before a coffee plant is mature enough to produce the berries that contain the coffee bean. Not to mention, Coffea arabica (the most popular cultivar) grows and thrives only in a few places in the world. It’s a demanding little plant with very particular climate needs—which brings us to our next point.

2. European Coffee Isn’t From Europe

Coffee beans don’t grow in Europe. They grow in Central and South America, East and West Africa, the Arabian Peninsula, parts of Asia, and the Pacific. So if you’re buying expensive imported coffee from Italy, France, or anywhere outside of these regions, you’re likely getting pretty bad coffee (unless you live in Italy or France, that is). That’s because the best-tasting coffee is always roasted shortly before it’s consumed.

If your coffee beans say they’re from Ethiopia, that’s where they were grown. But if the bag says they’re from somewhere in Europe, it likely means the coffee was roasted there, and that’s bad. Roasting brings out the flavors in coffee, but those flavor compounds start to break down shortly after they’re roasted. Coffee roasted outside your locale has likely sat in a shipping container or cargo plane for a long time. So when it arrives, all those flavors that make the coffee so tasty in a Parisian café have greatly degraded.

That’s why my advice is to always buy locally roasted coffee beans and grind them at home (with a burr grinder).

3. Dark Roasts Don’t Have More Caffeine

We often hear that darker coffee is “stronger,” meaning it contains more caffeine, and that’s not exactly true. When green coffee goes into a roaster, it’s literally just roasted to different levels of doneness—just like your morning toast.

Blonde roasts are among the lightest-roasted beans, and because they don’t spend as much time cooking, they actually contain more intact caffeine compounds than medium- or dark-roasted beans. Heat accelerates chemical interactions, which means it also breaks down caffeine compounds. So it stands to reason that the longer a coffee bean is roasted, the less caffeine it’s going to contain when it’s ground up and brewed.

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March 7, 2024
The scientific secrets to baking a perfectly moist chocolate cake

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Shutterstock/Jaclyn Vernace

NEXT week is my daughter’s 5th birthday party, and she has high expectations for her cake. It has to be extremely chocolatey, but it must also be a “piñata cake”, meaning that when you cut into it, sweets cascade out. It will also have to be large, to serve 30 children and their chaperones.

My big worry is that it could end up very dry. To achieve the required size and the piñata effect, I will have to bake at least three large layers, but I will also have to cut out the middle of the cake, which, as…

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March 6, 2024
Scientists Discover Key to Making Plant-Based Protein With Good Texture

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Despite the known benefits of consuming less meat and more plant-based foods, consumers often struggle at the supermarket, swayed by taste and texture preferences, even as some plant-based alternatives fall short in sustainability. New research from the University of Copenhagen introduces a promising solution: using non-toxic blue-green algae, specifically modified cyanobacteria, to produce protein-rich foods with meat-like textures, offering a sustainable and minimally processed alternative.

It’s widely recognized that reducing our consumption of meat and cheese in favor of plant-based foods is beneficial. However, when faced with the choice between traditional animal-based items and environmentally friendly alternative proteins in the supermarket’s refrigerated section, we don’t always make the eco-conscious choice. Despite the fact that many plant-based options now have good flavor, textures with the ‘right’ mouthfeel have often been lacking.

Furthermore, some plant-based protein alternatives are not as sustainable anyway, due to the resources consumed by their processing.

But what if it was possible to make sustainable, protein-rich foods that also have the right texture? New research from the University of Copenhagen is fueling that vision. The key? Blue-green algae. Not the infamous type known for being a poisonous broth in the sea come summertime, but non-toxic ones.

A closed photobioreactor where microalgae are cultivated in glass tubes. Credit: IGV Biotech, CC BY-SA 3.0 DEED

“Cyanobacteria, also known as blue-green algae, are living organisms that we have been able to get to produce a protein that they don’t naturally produce. The particularly exciting thing here is that the protein is formed in fibrous strands that somewhat resemble meat fibers. And, it might be possible to use these fibers in plant-based meat, cheese, or some other new type of food for which we are after a particular texture,” says Professor Poul Erik Jensen of the Department of Food Science.

In a new study, Jensen and fellow researchers from the University of Copenhagen, among other institutions, have shown that cyanobacteria can serve as host organisms for the new protein by inserting foreign genes into a cyanobacterium. Within the cyanobacterium, the protein organizes itself as tiny threads or nanofibers.

Minimal processing – maximum sustainability

Scientists around the world have zoomed in on cyanobacteria and other microalgae as potential alternative foods. In part because, like plants, they grow by means of photosynthesis, and partly because they themselves contain both a large amount of protein and healthy polyunsaturated fatty acids.

“I’m a humble guy from the country side who rarely throws his arms into the air, but being able to manipulate a living organism to produce a new kind of protein which organizes itself into threads is rarely seen to this extent – and it is very promising. Also, because it is an organism that can easily be grown sustainably, as it survives on water, atmospheric CO_2,and solar rays. This result gives cyanobacteria even greater potential as a sustainable ingredient,” says an enthusiastic Poul Erik Jensen, who heads a research group specializing in plant-based food and plant biochemistry.

Many researchers around the world are working to develop protein-rich texture enhancers for plant-based foods – e.g., in the form of peas and soybeans. However, these require a significant amount of processing, as the seeds need to be ground up and the protein extracted from them, so as to achieve high enough protein concentrations.

“If we can utilize the entire cyanobacterium in foodstuffs, and not just the protein fibers, it will minimize the amount of processing needed. In food research, we seek to avoid too much processing as it compromises the nutritional value of an ingredient and also uses an awful lot of energy,” says Jensen.

Tomorrow’s cattle

The professor emphasizes that it will be quite some time before the production of protein strands from cyanobacteria begins. First, the researchers need to figure out how to optimize the cyanobacteria’s production of protein fibers. But Jensen is optimistic:

“We need to refine these organisms to produce more protein fibres, and in doing so, ‘hijack’ the cyanobacteria to work for us. It’s a bit like dairy cows, which we’ve hijacked to produce an insane amount of milk for us. Except here, we avoid any ethical considerations regarding animal welfare. We won’t reach our goal tomorrow because of a few metabolic challenges in the organism that we must learn to tackle. But we’re already in the process and I am certain that we can succeed,” says Poul Erik Jensen, adding:

“If so, this is the ultimate way to make protein.”

Cyanobacteria such as spirulina are already grown industrially in several countries – mostly for health foods. Production typically occurs in so-called raceway ponds beneath the open sky or in photobioreactors chambers, where the organisms grow in glass tubes.

According to Jensen, Denmark is an obvious place to establish “microalgae factories” to produce processed cyanobacteria. The country has biotech companies with the right skills and an efficient agricultural sector.

“Danish agriculture could, in principle, produce cyanobacteria and other microalgae, just as they produce dairy products today. It would be possible to harvest, or milk, a proportion of the cells as fresh biomass on a daily basis. By concentrating cyanobacteria cells, you get something that looks like a pesto, but with protein strands. And with minimal processing, it could be incorporated directly into a food.”

Reference: “Self-Assembly of Nanofilaments in Cyanobacteria for Protein Co-localization” by Julie A. Z. Zedler, Alexandra M. Schirmacher, David A. Russo, Lorna Hodgson, Emil Gundersen, Annemarie Matthes, Stefanie Frank, Paul Verkade and Poul Erik Jensen, 8 December 2023, ACS Nano.
DOI: 10.1021/acsnano.3c08600

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March 4, 2024
A New Game-Changer in Lab-Grown Meat Production

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Glutenin, a wheat protein, shows promise for lab-grown meat production by supporting the cultivation of muscle and fat layers that mimic real meat’s texture and composition, offering a sustainable alternative to traditional meat as the global population increases.

As the global population grows, lab-grown meat, which consists of animal muscle and fat cells cultivated in lab settings, presents a promising solution to meet the rising demand for protein. Additionally, affordable plant proteins could serve as a foundation for these cell cultures. Recent findings published in ACS Biomaterials Science & Engineering demonstrate that the non-allergenic wheat protein glutenin successfully grew striated muscle layers and flat fat layers, which could be combined to produce meat-like textures.

Development of Plant-based Scaffolds for Cultured Meat

Cultured cells need a base or scaffold to adhere to produce lab-grown meat. Plant proteins are appealing candidates for the scaffolds because they are edible, abundant, and inexpensive. Previous researchers showed that a plant-based film made of glutenin was a successful base to cultivate cow skeletal muscle cells.

But for this technique to produce a promising meat-like alternative, the muscle cells need to form aligned fibers, similar to the texture in real tissues. Additionally, fat needs to be included in the 3D structure to replicate the composition of traditional meat products. To take advantage of using glutenin, a protein in gluten that people with celiac disease or a gluten sensitivity don’t typically react to, Ya Yao, John Yuen, Jr., Chunmei Li, David Kaplan, and colleagues wanted to develop plant-based films with it to grow textured muscle cells and fatty layers.

Experimental Results and Future Directions

The researchers isolated glutenin from wheat gluten and formed flat and ridge-patterned films. Then they deposited mouse cells that develop into skeletal muscle onto the protein bases and incubated the cell-covered films for two weeks. Cells grew and proliferated on both flat and ridged films. As expected, compared to cells grown on control films made of gelatin, the performance of the glutenin-based films was inferior but sufficient. The researchers say further work needs to be done to improve how cells attach to the plant-based film to get closer to the growth on the animal-derived biomaterial. During the second week of the culture, the cells on the patterned film formed long parallel bundles, recreating the fiber structure of animal muscles.

By putting ridges in a plant protein base, cultured muscle cells grew in a pattern that mimics the alignment of muscle fibers in animals. Credit: Adapted from ACS Biomaterials Science & Engineering 2024, DOI: 10.1021/acsbiomaterials.3c01500

In another test, mouse cells that produce fat tissues were deposited onto flat glutenin films. During the incubation period, as cells proliferated and differentiated, they produced visible lipid and collagen deposits.

The cultured meat and fat layers attached to the edible glutenin films could be stacked to form a 3D meat-like alternative protein. Because the glutenin material base supported the growth of both textured animal muscle and fat layers, the researchers say it could be used in an approach for more realistic cultivated meat products.

Reference: “Cultivated Meat from Aligned Muscle Layers and Adipose Layers Formed from Glutenin Films” by Ya Yao, John S. K. Yuen, Jr., Ryan Sylvia, Colin Fennelly, Luca Cera, Kevin Lin Zhang, Chunmei Li and David L. Kaplan, 16 January 2024, ACS Biomaterials Science & Engineering.
DOI: 10.1021/acsbiomaterials.3c01500

The authors acknowledge funding from MilliporeSigma and the U.S. Department of Agriculture. Some authors are employees of MilliporeSigma, Inc.

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February 26, 2024
A New Startup Wants to Turn the Sugar You Eat Into Fiber

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What the body does need is fiber, a nutrient found in vegetables, whole grains, and legumes that helps regulate the bowel and lower blood cholesterol and glucose levels. Only about 5 percent of Americans get the recommended amount of daily fiber, which is about 30 grams a day.

The enzyme Zya is developing comes from a family called inulosucrases, and is naturally made by a strain of bacteria found in the human microbiome that’s capable of converting sugar to fiber in the gut environment. This enzyme acts on sugar before it can be broken down and absorbed by the body. It works by rearranging sugar molecules into inulin fiber, a type of soluble fiber found in plants such as chicory root that fosters the growth of beneficial gut bacteria.

In the human gut, the enzyme isn’t expressed in amounts to be useful. In addition to scaling up its production, Zya has modified the enzyme to improve its stability and performance in the GI tract.

In lab experiments, researchers added the enzyme to table sugar in models of the human gut, and also tested real food products with the enzyme in these systems. They found that the enzyme could convert up to 30 percent of the sugar present into fiber. They also mixed the enzyme with food and fed it to pigs, which have digestive tracts similar to humans.

Using a small tube called a cannula, researchers took samples from the pigs’ small intestine. Sauer says they’ve observed “significant and meaningful levels of sugar-to-fiber conversion” compared to food given to the pigs that didn’t contain the enzyme, but they’re still performing tests to quantify the exact amount. The company also plans to test the enzyme in people.

So far, Zya has raised £4.1 million (a little over $5 million) in venture capital over two financing rounds: a seed round led by Astanor Ventures in 2022 followed by a further round by Better Ventures in 2023.

Sauer is hoping to launch its product, called Convero, in the US in 2026, with the goal of getting into dry food products first. He says food manufacturers are already interested in using it as an ingredient. But first, Zya will have to get the enzyme approved by the US Food and Drug Administration.

Wendelyn Jones, executive director of the Institute for the Advancement of Food and Nutrition Sciences, a public health nonprofit based in Washington, DC, says enzymes are not listed on a food product’s nutrition facts panel, so companies developing them will need to work with regulatory experts on how to label the foods that contain them and how to list them as ingredients.

“As this product moves from the laboratory to the table, the company will need to define how they want to label the product,” she says. For instance, if Zya wants to make a health claim about its enzyme, it has to provide evidence to the FDA to back up that claim.

Zya isn’t the only one pursuing this kind of technology. American food company Kraft Heinz—known for its macaroni and cheese and array of condiments—is working with the Wyss Institute at Harvard University to develop similar enzymes.

Taylor Wallace, CEO of Think Healthy Group, a food science consulting firm, sees huge potential in these kinds of enzymes. “It’s a great idea,” he says. “We’re not going to stop people from eating cookies. We can encourage them to moderate, but we’ve basically been preaching the same dietary guidelines since the early ’80s and nothing’s changed. We’ve only gotten fatter. We’ve only gotten less healthy.”

Wallace says pigs are a good place to start with testing, but results in animals don’t always translate to humans.

He doesn’t think any one product is going to be a magic bullet to the obesity problem, but he sees the Zya enzyme as one of many technologies that could nudge the population to a healthier state.

Mark Haub, a professor of food, nutrition, dietetics, and health at Kansas State University, agrees. “This could be a viable means of helping people with their food choices,” he says. “If there’s a way to let people consume what they normally do but make it healthier, that would be great.”

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February 23, 2024
Alarm over ultra-processed food shouldn't put us off plant-based diets

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The concern over factory-made fare, especially many plant-based meat substitutes, is often misplaced and lacking evidence, says biologist Jenny Chapman

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February 21, 2024
Super-thickeners made from starch reduce calories and carbs in food

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Starch is a component of flour, a thickening agent in cooking

Viktor Fischer/Alamy

Building tiny sheets and cages from starch particles turns them into super-thickeners that could reduce the calorie content of foods.

Starch is often added to foods like soups to make them richer and thicker, but doing so increases the calorie count and carbohydrate content. Now, Peilong Li at Cornell University in New York and his colleagues have found that the amount of starch in foods can be reduced without sacrificing texture by arranging starch particles into special shapes.

Starch particles thicken food because they swell up when they are heated. This means the particles jam against each other, leaving less room for liquid components of the dish to flow freely. The researchers wondered whether they could replicate this effect but cut the amount needed by hollowing out globs of starch. “But you can’t just carve a starch granule like it’s a pumpkin,” says Li.

Instead, working with starch particles extracted from amaranth grain, he and his colleagues devised a way to assemble them into three-dimensional shapes by mixing them with water and oil. The starch particles arranged themselves around oil drops, and then the researchers removed the two liquids through a combination of heating and freeze-drying. This left them with just the starchy structures, some shaped like cages with hollow centres, some shaped like sheets that would cascade on top of each other so liquids would get trapped between them.

The team discovered that these starch structures performed so well as thickening agents that they could be used to halve the amount of starch typically needed to thicken foods.

Fan Zhu at the University of Auckland in New Zealand says that using these granules as building blocks for the new class of hollow starch structures is very innovative and could make starches a big part of designing future foods. However, Zhu says that amaranth starch is expensive and can be difficult to source in large quantities, so adapting the new method to more affordable and abundant starches like those made from corn would be advantageous. “And more studies are needed on what happens when you put this kind of structure in your mouth,” he says.

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February 16, 2024
Scientists Discover Unexpected Effects of Common Food Preservative

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Foods such as yogurts, canned vegetables, and packaged breads frequently include preservatives that leverage the antimicrobial properties of substances like lantibiotics, including those similar to nisin, to ensure their longevity and safety. These additives, while essential for preventing microbial growth that can lead to spoilage, are now being studied for their broader implications on health, particularly their interactions with the human gut microbiome. Recent findings by researchers at the University of Chicago point to the dual action of these compounds, capable of targeting both detrimental pathogens and crucial beneficial bacteria within the gut, thereby raising important questions about their long-term effects on digestive health and microbial diversity.

Research on a widely used food preservative known for its ability to eliminate pathogens indicates it also impacts helpful bacteria, posing a risk to the gut microbiome’s equilibrium.

To extend the shelf life of food items, manufacturers commonly incorporate preservatives into their products. These substances are intended to eliminate microorganisms that may cause the food to deteriorate. While traditional preservatives such as sugar, salt, vinegar, and alcohol have a long history of use, contemporary food products often list more obscure additives like sodium benzoate, calcium propionate, and potassium sorbate on their labels.

Bacteria produce chemicals called bacteriocins to kill microbial competitors. These chemicals can serve as natural preservatives by killing potentially dangerous pathogens in food. Lanthipeptides, a class of bacteriocins with especially potent antimicrobial properties, are widely used by the food industry and have become known as “lantibiotics” (a scientific portmanteau of lanthipeptide and antibiotics).

Despite their widespread use, however, little is known about how these lantibiotics affect the gut microbiomes of people who consume them in food. Microbes in the gut live in a delicate balance, and commensal bacteria provide important benefits to the body by breaking down nutrients, producing metabolites, and—importantly—protecting against pathogens. If too many commensals are indiscriminately killed off by antimicrobial food preservatives, opportunistic pathogenic bacteria might take their place and wreak havoc—a result no better than eating contaminated food in the first place.

Effects on good and bad bacteria

A new study published in ACS Chemical Biology by scientists from the University of Chicago found that one of the most common classes of lantibiotics has potent effects both against pathogens and against the commensal gut bacteria that keep us healthy.

Nisin is a popular lantibiotic used in everything from beer and sausage to cheese and dipping sauces. It is produced by bacteria that live in the mammary glands of cows, but microbes in the human gut produce similar lantibiotics too. Zhenrun “Jerry” Zhang, Ph.D., a postdoctoral scholar in the lab of Eric Pamer, MD, the Donald F. Steiner Professor of Medicine and Director of the Duchossois Family Institute at UChicago, wanted to study the impact of such naturally-produced lantibiotics on commensal gut bacteria.

“Nisin is, in essence, an antibiotic that has been added to our food for a long time, but how it might impact our gut microbes is not well studied,” Zhang said. “Even though it might be very effective in preventing food contamination, it might also have a greater impact on our human gut microbes.”

He and his colleagues mined a public database of human gut bacteria genomes and identified genes for producing six different gut-derived lantibiotics that closely resemble nisin, four of which were new. Then, in collaboration with Wilfred A. van der Donk, Ph.D., the Richard E. Heckert Endowed Chair in Chemistry at the University of Illinois Urbana-Champaign, they produced versions of these lantibiotics to test their effects on both pathogens and commensal gut bacteria. The researchers found that while the different lantibiotics had varying effects, they killed pathogens and commensal bacteria alike.

“This study is one of the first to show that gut commensals are susceptible to lantibiotics, and are sometimes more sensitive than pathogens,” Zhang said. “With the levels of lantibiotics currently present in food, it’s very probable that they might impact our gut health as well.”

Harnessing the power of lantibiotics

Zhang and his team also studied the structure of peptides in the lantibiotics to better understand their activity, in the interest of learning how to use their antimicrobial properties for good. For example, in another study, the Pamer lab showed that a consortium of four microbes, including one that produces lantibiotics, help protect mice against antibiotic-resistant Enterococcus infections. They are also studying the prevalence of lantibiotic-resistant genes across different populations of people to better understand how such bacteria can colonize the gut under different conditions and diets.

“It seems that lantibiotics and lantibiotic-producing bacteria are not always good for health, so we are looking for ways to counter the potential bad influence while taking advantage of their more beneficial antimicrobial properties,” Zhang said.

Reference: “Activity of Gut-Derived Nisin-like Lantibiotics against Human Gut Pathogens and Commensals” by Zhenrun J. Zhang, Chunyu Wu, Ryan Moreira, Darian Dorantes, Téa Pappas, Anitha Sundararajan, Huaiying Lin, Eric G. Pamer and Wilfred A. van der Donk, 31 January 2024, ACS Chemical Biology.
DOI: 10.1021/acschembio.3c00577

The study was supported by the GI Research Foundation, the Howard Hughes Medical Institute, the National Institutes of Health (grants R01AI095706, P01 CA023766, U01 AI124275, and R01 AI042135) and the Duchossois Family Institute at UChicago. Additional authors include Chunyu Wu, Ryan Moreira, and Darian Dorantes from the Univeristy of Illinois Urbana-Champaign, and Téa Pappas, Anitha Sundararajan, and Huaiying Lin from UChicago.

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February 6, 2024
You Can’t Buy Lab-Grown Meat Even If You Wanted To

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“The restaurant dinners we held at China Chilcano in Washington, DC last summer went extremely well,” wrote Eat Just’s director of global communications, Carrie Kabat, in an emailed statement to WIRED. “We plan to resume these dinners this year.”

Good Meat/Eat Just’s chicken had also previously been on sale in Singapore, but sales there have also been paused. “In Singapore, we are ramping up production and plan to begin serving shortly,” Kabat wrote.

The goal of these early cultivated meat sales was likely to generate buzz, gauge public reaction, and raise awareness of the industry, says Steve Molino, an investor at Clear Current Capital, a plant-based and cultivated meat venture capital firm, who has not invested in either Eat Just or Upside Foods. “It accomplished what it needed to accomplish and now it’s time to refocus,” Molino says, noting that the companies probably made a loss on the sale of their meat given the high costs of production.

Eat Just is currently embroiled in a legal dispute with a former partner over alleged unpaid invoices. In a November 2023 WIRED investigation, former employees alleged that the company was struggling financially and failed to pay vendors on time. “The reality for us now is we need to figure out a way to build large-scale facilities without spending north of half a billion dollars, because it’s simply not viable long-term,” Eat Just CEO Josh Tetrick told WIRED at the time. “There has to be a better way of doing it. And if we can’t figure out a different way of doing it, then what we’re doing won’t work.”

Although cultivated meat is no longer on sale in the US and Singapore, both Eat Just and Upside Foods told WIRED that they planned to relaunch sales in 2024. And last month, Israel-based Aleph Farms received regulatory approval from the Israeli Ministry of Health for its cultivated beef product: a mix of beef cells and plant protein. The company still requires an inspection of its pilot production facility in Rehovot and directions on labeling and marketing from Israeli regulators before it can sell its product in Israel.

“Post inspection of our production facility, Aleph Cuts will be introduced in targeted tasting experiences for consumers and relevant stakeholders,” says Aleph Farms CEO and cofounder Didier Toubia. “This phase of limited market activations allows us to gather feedback from consumers, refine our brand positioning collaboratively with them, and lay the foundation for a successful long-term launch.”

Sheila Voss, senior vice president of communications at the alternative protein nonprofit the Good Food Institute, says she expects the rollout of cultivated meat to continue in the US.

“As we saw in Singapore, the first country in the world to approve the sale of cultivated meat, the rollout to consumers migrated across fine dining restaurants, home delivery, and hawker stalls, highlighting the versatility of this product, and we expect similar introductory rollouts in the US,” she says. “We are still at the very early stages of cultivated meat’s entrance into the marketplace.”

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February 2, 2024
Flavour bridging: How to cook a bizarre but delicious Christmas dinner

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Guests enjoy a main course of turkey, peanuts and chocolate to test “flavour bridging” theory

David Stock

SOME foods are made for one another. From the comforting cuddle of mozzarella, tomato and marjoram atop a pizza to the tantalising trinity of ginger, garlic and soy sauce that make East Asian dishes sing, some combinations seem so natural that it is difficult to imagine a world without them. And yet for centuries, gourmands and academics have been confounded by why some foods harmonise so well.

In 1992, chefs Heston Blumenthal and François Benzi hit the lab to try to solve this culinary riddle. They happened upon the idea that foods that taste good together also share many volatile flavour compounds – the aroma-carrying chemicals that rise up into the back of the nose to create the perception of flavour on the tongue. Their findings were validated in 2011, with a study that analysed 56,498 recipes from different international cuisines.

Yong-Yeol Ahn at Indiana University and his colleagues used the data to construct a network model, a complex map of the relationships between all of the recipes’ ingredients and the flavour compounds they shared. This confirmed that recipes from North America and western Europe do tend to pair ingredients that share flavour compounds.

“Flavour pairing theory” made waves in the culinary world, with food manufacturers dedicating resources to applying the idea to their products and start-ups tapping into open-source data on flavour compounds to predict what the next big…

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December 12, 2023