Green Feed Additive--Bioactive Peptide (2)
1.1.3 Peptides with hormone properties Hormone peptides include growth hormone-releasing peptides (GHRPs), oxytocin, and the like. They produce a variety of physiological effects by reacting themselves as hormones or regulating hormones. GHRPs are a class of newly synthesized bioactive peptides developed in the 1990s and have biological activity to release growth hormone (GH) in animals. Currently synthesized GHRPs have four forms: GHRP-6, GHRP-2, GHRP-1, and hexarelin, which all have the amino acid sequence of Ala-Trp-D-Phe-Lys-NH2. Oxytocin is synthesized and released by the supraoptic supraoptic nucleus and the pancreas nucleus. Oxytocin plays an important role in the breeding of sows. It can strongly contract the uterine smooth muscle and promote the uterus to discharge the piglets; at the same time, it can stimulate the strong contraction of myoepithelial cells. Caused milking reactions. 1.1.4 Enzyme Modulators and Inhibitors Such peptides include glutathione, incretin, and the like. Glutathione can be completely absorbed in the small intestine, and it can maintain the integrity of the erythrocyte membrane; it has the function of protecting and restoring the activity of enzymes that require sulfhydryl groups; is a coenzyme or a prosthetic group of various enzymes; participates in the absorption and transport of amino acids. Participate in the reduction of methemoglobin and promote iron absorption. 1.1.5 Immunoactive peptides There are two types of immunoactive peptides, endogenous and exogenous. Endogenous peptides shown to be immunologically active include interferons, interleukins, and β-endorphin, which are the centers of activation and regulation of the body's immune response. Studies have shown that there are not only beta-endorphin receptors on immune cells, but immunoreactive cells also have immunoreactive beta-endorphins, which can affect antibody synthesis, lymphocyte proliferation, and NK The cytotoxic effect of the cells. Exogenous immunogenic peptides are mainly derived from casein in human milk and cow's milk. Casein-derived immunogenic peptides are mainly composed of the following: (1) αs1-casokinin-6, which is derived from αs1-casinoin An immunologically active short peptide obtained from the enzymolysis product of the protein, and the amino acid composition and arrangement is comparable to the 194-199 residue sequence of αs1-casein; (2) β-casokinin-10, corresponding to The amino acid residue sequence of 193-202 of β-casein; (3) The immunologically active β-casein fragment whose amino acid arrangement sequence is respectively related to the 63-68 residue sequence of cattle β-casein and 191-193 residue. The base sequence is the same. The immunologically active peptide has many physiological functions. It can not only enhance the body's immune ability and play an important role in the immune regulation in animals, but also stimulate the proliferation of the body's lymphocytes and enhance the phagocytic ability of macrophages, and improve the body's External pathogen resistance. In addition, endorphin, enkephalin, and dynorphin in exogenous opioid peptides also have immunostimulatory effects and can stimulate lymphocyte proliferation. For example, methylephrine (M-Enk) can produce IL-1 in mouse peritoneal macrophages stimulated by lipopolysaccharide, promoting the proliferation of mouse splenic lymphocytes and the production of IL-2 and IL-6. Extracting thymosin from thymus tissue and adding it to Avid chicken feed or intramuscular injection can significantly increase chicken peripheral lymphocyte percentage and plasma T4 levels, and GH and T3 levels also have a tendency to increase. 1.1.6 Mineral binding peptides Most studies in this area have focused on the peptides obtained by enzymatic hydrolysis of casein to bind and transport divalent mineral cations (Meisel, 1997). Milk, fish, soy, and cereal proteins can be used as precursors to bind mineral active peptides. At present, several casein phosphopeptides (CPP) that bind to minerals have been isolated from the enzymatic hydrolysates of alpha and beta-casein (Maubois et al., 1989; 1991). Most of the mineral-binding peptides contain a phosphorylated serine group and a glutamyl residue at the center of the peptide, and the sites of binding to mineral elements are present on the negatively charged side chains of these amino acids. The most obvious feature is the presence of phosphate groups. group. Binding to calcium requires a serine-containing phosphate group and a free carboxyl group of glutamic acid. This binding prevents further interaction of the complex and enhances the solubility of the mineral-peptide complex. CPP is the most studied mineral element binding peptide. CPP can combine with various mineral elements to form soluble organic phosphate. It acts as a carrier for many mineral elements such as Fe2+, Mn2+, Cu2+, Se2+, and Ca2+ in vivo, which can promote Absorption of Ca2+ and other mineral elements in the small intestine. Recent studies have also shown that CPP contributes to animal Zn2+ uptake in diets containing phytate-rich phosphorus. Therefore, CPP is a good metal ion binding peptide, and the raw material casein of CPP is a natural protein, and there is no safety problem when used as a feed additive. At present, there have been many reports on mineral element-peptide complexes promoting the absorption of mineral elements and improving animal production performance.
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