Peptide Nutrition And Health Function

Numerous studies have shown that foodborne peptides have multiple nutritional and health benefits. Some active peptide segments exist in an inactive state within the protein amino acid sequence, but are released through enzymatic hydrolysis in vivo or in vitro (such as during gastrointestinal digestion and food processing), thus they may have multiple physiological activities. In addition, although the content of active peptides in organisms is very small, their physiological activity is significant.

Promote amino acid absorption and protein synthesis
In foodborne peptides, the transport system of oligopeptides (usually composed of 2-6 amino acids) has the characteristics of fast speed, low energy consumption, and low saturation, and is absorbed faster than the corresponding free amino acids. Due to the independent absorption mechanism between oligopeptides and free amino acids, which do not interfere with each other, it helps to alleviate the absorption inhibition caused by free amino acids competing for common absorption sites, thereby promoting the absorption of peptide form amino acids and increasing the efficiency of protein synthesis. For example, when lysine and arginine exist in free form, they compete for absorption sites, while when lysine exists in peptide form, arginine has no effect on its absorption. In addition, oligopeptides in the circulation can also directly participate in the synthesis of tissue proteins. Studies have shown that when using peptides as nitrogen sources, overall protein deposition is higher than in corresponding amino acid or intact protein diets.

Promote the absorption of mineral elements
Many studies have reported that foodborne peptides have the effect of promoting the absorption and utilization of mineral elements. Foodborne peptides can increase water solubility by forming chelates with metal elements, thereby promoting the absorption of mineral elements. For example, the phosphorylated serine residues contained in casein phosphopeptide hydrolysate can bind with Ca2+and Fe2+, thereby enhancing its solubility. Meister et al. isolated casein phosphopeptides from bovine casein, whose serine hydroxyl groups are almost entirely phosphorylated. These phosphopeptides concentrate a large amount of negative charges, which can prevent further protein hydrolysis, and can combine with free metal ions such as calcium, iron, copper, and zinc to form soluble salts, increasing their concentration in the intestinal lumen and promoting the passive transport of these ions.

Enhance immune function
Foodborne peptides have immune activity and can enhance the body's immunity, playing an important regulatory role in the immune system. In 1984, Parker et al. isolated an immunologically active peptide (Val Gln Pro Ile Pro Tyr) from casein hydrolysate, which can activate the phagocytic activity of mouse peritoneal macrophages on Mianyang red blood cells. In 1992, Coste et al. isolated a 17 peptide (Tyr Gln Gln Glu Val Leu Gly Val Arg Gly Phe Pro Ile Ile Val) from bovine casein digestion products, which stimulated the proliferation of pre sensitized rat lymph node cells and non sensitized rat spleen lymphocytes. In 2003, Tsuruki et al. isolated a 13 peptide from β - soy globulin, Met-Ile-Thr-Leu-Ala-Ile-Pro-Val-Asn-Lys-Pro-Gly-Arg, Named Soymetide, it proves to have strong immunomodulatory effects.

Antioxidant effect
Due to the potential health hazards of artificially synthesized antioxidants, natural and safe antioxidants have become a major research hotspot. Foodborne peptides have the characteristics of small molecular weight and easy absorption, which can achieve anti-aging effects by inhibiting the peroxidation of biomolecules and clearing free radical products in the body. Many peptide substances with antioxidant activity have been extracted from different protein sources, such as soy peptides, corn peptides, fish protein peptides, pig hemoglobin peptides, wheat germ protein peptides, royal jelly protein peptides, whey protein peptides, potato protein peptides, etc