Abstract
Bioactive peptides have been identified in a range of foods, including plant, milk and muscle, e.g., beef, chicken, pork and fish muscle proteins. Bioactive peptides from food proteins offer major potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an outline of the bioactive peptides identified in the muscle protein of meat to date, with a focus on muscle protein from domestic animals and fish. The majority of research on bioactives from meat sources has focused on angiotensin-1-converting enzyme (ACE) inhibitory and antioxidant peptides.
Highlights
Food proteins have long been recognized for their nutritional and functional properties
Nutrients 2011, 3 on the liberation of bioactive peptides which are encrypted within food proteins, with a view to utilizing such peptides as functional food ingredients aimed at health maintenance
Katsuobushi Oligopeptide LKPNM, which is found in blood pressure-lowering capsules, is derived from dried bonito and converted to the active form by digestive enzymes following ingestion [133]
Summary
Food proteins have long been recognized for their nutritional and functional properties. Within the parent protein sequence, the peptides are inactive and must be released to exert an effect These bioactive peptides are usually 2–20 amino acid residues in length, some have been reported to be >20 amino acid residues. The first food-derived bioactive peptide was identified in 1950 when Mellander reported that casein phosphorylated peptides enhanced vitamin D-independent bone calcification in rachitic infants [11]. Interest in this field has increased considerably in the last two decades, with the majority of research focusing on the identification of bioactive peptides from milk proteins [12,13]. For example C12®, a casein derived peptide supplied by DMV International, claims to reduce blood pressure
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