The use of plant-based nutrients is growing in the food industry, for example by incorporating plant-based protein sources into products. Peptides – small breakdown products of the protein of two or more amino acids – in these nutrients can have a profound effect on the taste. Using ultra-high performance liquid chromatography – mass spectrometry (UHPLC-MS), Boudewijn Hollebrands, analytical chemistry scientist, at Unilever investigates the influence of peptides on the taste experience. FHI spoke to him.
By: Dimitri Reijerman
According to Hollebrands, the UHLPC-MS method he uses is the combination of a modern separation technique linked to mass spectrometry for the detection of peptides. He applies this to food research at Unilever. He says: “We look at various products based on vegetable proteins in this way. In addition to the proteins, we also looked at the peptides in those products. Peptides have a major influence on the taste. With plant-based products you have multiple components that ultimately give a product flavor. Peptides can taste sweet, salty, sour, umami or bitter. You especially don't want to taste the bitter effects in a product and that is the focus of my research.”
Developing more plant-based food products is a complex undertaking, Hollebrands explains: “At Unilever, we have the ambition to increase our turnover for plant-based products fivefold, to €1 billion in 2025 to 2027. You can use many different types of protein sources for this. Of course, everyone knows soy. But there are also many unknown vegetable protein sources. If you want to use it, you will also have to deal with new taste effects, including flavors that you would not want. Part of this is due to the peptides in those protein sources. Relatively little research has been done into the taste experience and the link with the analytical data surrounding peptides.”
With his research design and the application of UHPLC-MS, Hollebrands hopes to accelerate research into peptides and taste: “The traditional way is that you have a protein, together with peptides. You will fractionate these and by tasting you will discover the taste that you do not want or that you do want. You then continue with the purification steps so that you can ultimately accurately characterize the peptides with mass spectrometry. What we want to achieve is that using a peptide analysis, which produces a lot of data, in combination with 'taste models' you can more quickly arrive at an answer to the question of which peptides influence the taste.”
He continues: “You can quickly determine the structure of peptides using mass spectrometry. Moreover, this structure is important for the interaction with taste receptors. A lot of information is already available about how peptides interact with taste receptors. This way, after determining the properties of peptides, you can predict how they will react with your taste receptors.”
His research into these flavor molecules has just started: “I started at the beginning of last year in collaboration with Wageningen University & Research. We have now been working for a year and we are still in the early stages. Mass spectrometry also provides more and more data. The biggest challenge nowadays lies mainly in setting up research methods. That takes time, but ultimately working out all the research data is the biggest job. I hope that we can ultimately build more knowledge about the relationship between peptides and taste.”
During his lecture during the Life Science Online Theme Days he also wants to give his audience more text and explanation about peptides in food: “Initially I want to tell people more about peptides and their influence on the taste. I also want to show that you can solve complex problems by doing analyzes in a smart way and linking them to computer models. Furthermore, the development of artificial taste receptors is very interesting for my research. This could allow you to replace a test panel in the future.”
Boudewijn Hollebrands' online lecture is scheduled for Thursday, April 22 at 9:00 am. Registration is free and can be done via this form.
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