The rise and rise of bioactive proteins

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  • Published: Jun 1, 2016
  • Author: Ryan De Vooght-Johnson
  • Channels: Laboratory Informatics / Chemometrics & Informatics
thumbnail image: The rise and rise of bioactive proteins

Proteins that do more than just nourish

The inextricable connection between diet and health is being increasingly recognised worldwide, driven by the rise of obesity-related diseases such as diabetes and heart disease, and a growing body of research linking poor diet to diseases such as cancer. Consumers and governments are thus becoming more and more aware of the importance of food to human wellbeing, fuelling research to investigate the connection.

The inextricable connection between diet and health is being increasingly recognised worldwide, driven by the rise of obesity-related diseases such as diabetes and heart disease, and a growing body of research linking poor diet to diseases such as cancer. Consumers and governments are thus becoming more and more aware of the importance of food to human wellbeing, fuelling research to investigate the connection.

Extensive research is being conducted in ‘foodomics’ – the study of food and nutrition using high-throughput technologies. So-called ‘bioactive peptides’, sourced from both plant and animal proteins, have been of particular interest within these studies. Beyond their fundamental energy-providing role, a range of evidence shows that these proteins have health-promoting properties, including acting as antioxidants, lowering cholesterol and blood pressure and tackling inflammation.

Peptides are small proteins created by digestive enzymes in the gut, which cut proteins into smaller pieces. Digestion of the proteins in food generates a complex mix of peptides of different lengths and containing different amino acids, some of which may be bioactive. These bioactive peptides may attach to receptors while in the intestine or after being absorbed from the digestive tract. Some even make it into the bloodstream, where they can have beneficial effects throughout the body.

In the past, these proteins have been investigated using high-performance liquid chromatography and amino acid sequencing. To accurately and comprehensively characterise all of the peptides produced by digestion, more efficient analytical techniques are needed. This is where mass spectrometry (MS) comes in. Separation methods in combination with mass spectrometry is the current gold standard for characterising proteins in food.

From the slaughterhouse to the pharmacy?

In a study newly published in Electrophoresis, a team of French researchers applied these techniques to an often-neglected part of the food production chain: blood.

Blood is an unavoidable by-product of the meat industry. It is usually disposed of as waste or sold cheaply as an animal food or fertiliser (only 30% of the blood produced by slaughterhouses is sold for use in the food industry – the rest is discarded), but it is actually a valuable source of protein and contains several compounds that may have commercial value. Efforts are ongoing to find uses for the proteins in blood, especially those that are bioactive.

These researchers focused on the compounds inside cattle haemoglobin – the most abundant protein in blood and a promising source of bioactive peptides. They digested the haemoglobin in vitro using a protocol that mimics real digestion, with fluids designed to reproduce the conditions of the mouth, stomach and intestine. Next, they created a ‘peptide map’ using first low-resolution and then high-resolution liquid chromatography alongside tandem MS.

Improving MS

The low-resolution technique identified 75 different peptides, while the high-resolution approach identified over 10 times more – a total of 971 peptides – highlighting the importance of choosing the right analytical technique. Several of these proteins are already known to be bioactive and several more are being investigated as such.

These findings could fuel the growing market for ‘nutraceuticals’ or ‘functional foods’ for promoting good health and reducing disease risk, although there will undoubtedly be negative consumer perceptions to overcome first.

The food peptidomics approach described here, which uses state-of-the-art separation methods and high-resolution mass spectrometry, could also be a promising approach for assessing the health benefits of proteins in other samples. However, there is still room for improvement and the researchers discuss limitations, including misidentification of very small proteins, the grouping together of structurally similar peptides and difficulties with quantification.

Related Links

Electrophoresis, 2016. Caron et al., Food peptidomics of in vitro gastrointestinal digestions of partially purified bovine hemoglobin: low-resolution versus high-resolution LC-MS/MS analyses.

Bioactive proteins and peptides in food

Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery

Slaughterhouse Blood: An Emerging Source of Bioactive Compounds

Article by Ryan De Vooght-Johnson

The views represented in this article are solely those of the author and do not necessarily represent those of John Wiley and Sons, Ltd.

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