by Chirag Maheshwari1, Mahesh Kumar2, Muzaffar Hasan3, Nitin Kumar Garg4
1, 3 Scientist, ICAR-CIAE, Bhopal.
2 Scientist, ICAR-CAZRI, Jodhpur.
4 Assistant Professor, Rajasthan Agricultural Research Institute, Durgapura, Jaipur.
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Proteins are serving as source of energy and amino acids that contribute to growth and maintenance of the body. Along with nutritional role, proteins are responsible for various physiochemical and sensory properties of foods, and may act as functional and health-promoting ingredients. Many of the physiological and functional properties of proteins are attributed to biologically active peptides which are often encrypted in the native sequence. Native protein serve as a precursor for bioactive peptides which can be produced from the protein precursor by digestive enzymes (gastrointestinal digestion), during food processing (ripening, fermentation, cooking), storage, or by invitro hydrolysis by proteolytic enzymes. Bioactive peptides are short specific peptides that can alter body functions or conditions and may ultimately influence health positively. Bioactive peptides mainly contain 3–20 amino acid units, but in some cases the size can be larger.
Bioactive peptides Sources
Bioactive peptides may be obtained from plants, animal or marine sources. Plant peptides, having molecular weight less than 10 kDa, can essentially be divided into two categories: bioactive peptides that are produced by selective action of peptidases on larger precursor proteins and degraded peptides that result from the activity of proteolytic enzymes during protein turnover. Bioactive peptides such as hypogin (peanut), angularin (adzuki bean), lunasin (soybean and barley) have been shown to have medicinal properties.
Plant peptides also include glutathions and protease inhibitors such as mustard trypsin inhibitors. Interestingly, most of the therapeutic peptides initially discovered were sourced from animal venoms and toxins. Recently research has focused on discovery of new bioactive peptides from animal sources. Moreover, bio functionalities and isolation procedures of previously discovered bioactive peptides are well documented in the literature. Peptides from animal sources possess biological activities such as antihypertensive, antioxidant, antimicrobial and antiproliferative activity. Sources such as milk, egg and meat have been given special consideration due to their abundance in the human diet and documented biological activities.
Enzymatic digestion is one of the common methods to obtain peptides from protein hydrolysates of meat products. In addition to this, fermentation of meat products is an alternate method to generate bioactive peptides by proteolytic enzymes during microbial fermentation. The marine environment provides half of the total global biodiversity. Marine derived biologically active peptides are reported to have a range of functionalities including enzyme inhibition, mineral binding, immunomodulatory, antimicrobial, antioxidant, antithrombotic, hypocholesterolemic, and antihypertensive actions. Bioactive peptides and depsipeptides with functional properties have also been isolated from tunicates, sponges, soft corals, sea hares, nudibranchs, bryozoans, sea slugs, tunicates, sponges, mollusks and other marine organisms…
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