Protein is an indispensable nutrient in human life. Human beings get protein through food, which is the source of many bioactive peptides.

Some of the active peptides derived from food proteins are naturally occurring and some are the products of enzymatic hydrolysis catalyzed by protease.

Immunoactive oligopeptide. Breast milk is the first food for infants. Breast milk is the source of immunoregulatory substances. In fact, immunostimulatory peptides have been detected in casein of human and milk. Using mouse macrophages as the detection system, we can see that these peptides can stimulate macrophage phagocytosis.

Similarly, the egg protein (eggs of all kinds of birds), soybean protein, rice protein, wheat protein, corn protein, sorghum protein and millet protein, as human food protein, can also produce peptides with immune activity through appropriate enzyme and reasonable enzyme formula, and some peptides can inhibit tumor cells in addition to phagocytosis of macrophages Growth.

Antihypertensive peptide. In the physiological process of human body, the regulation of blood pressure is very important. Vasoconstriction and extracellular fluid volume are regulated by renin and Angiotension.

Renin (an enzyme) released by the cells near the glomerulus of the kidney enters the blood. A plasma AZ globulin (angiotensin) is converted into angiotensin II by the function of converting enzyme when it passes through the pulmonary circulation, which can directly strengthen the contractility of the heart muscle, improve the heart rate, and also be directly used for the smooth muscle of the blood vessel;

or through the sympathetic nerve, it can contract the blood vessels such as the viscera and the skin; it can make the blood vessel inside The results showed that the skin cells contracted, the intercellular space widened, the permeability of the wall increased, and the formation of tissue fluid increased because of the increased resistance of the capillary.

In this system, angiotension II can cause strong vasoconstriction. However, angiotension II is formed by the enzyme conversion of Angiotension I. From the point of view of nutrition and treatment, enzyme inhibitors are the key point in this process. It is generally believed that all substances that can inhibit ace have antihypertensive function. In fact, there are many ACE inhibitors in the enzymatic products of many proteins.

For example, there are several antihypertensive peptides in the trypsin hydrolysate of casein. The presence of ace in the small intestine may indicate that antihypertensive peptides released from milk can directly bind to specific receptors. α - zein and γ - zein have antihypertensive effects.

For example, most of the angiotensin inhibitors obtained by enzymolysis of α - zein are tripeptides. There are four different amino acids pro, Tyr, ala, Glu at the l-terminal. It has been reported that if the amino acid of l-terminal is pro or aromatic amino acid, then this peptide has strong inhibition effect on ACE.

It has also been found that the peptide with Glu at the l-terminal has a weaker ability to inhibit ace than the peptide with Pro, Tyr and Ala residues at the l-terminal.

A peptide that transports trace elements. These peptides are mainly derived from casein. Some scholars believe that the formation of casein phosphopeptides in the process of digestion is related to the transport of trace element peptides.

Casein phosphopeptides can form soluble complexes with calcium ions and prevent the decrease of calcium and phosphorus concentrations. Casein phosphopeptide can increase the concentration of soluble calcium in the small intestine, so it can promote the passive absorption of calcium in the small intestine. 

Besides compounding with calcium ion, it can also be compounded with other elements, such as iron, zinc, magnesium, copper and so on, which are beneficial to human health. At present, casein can also be enzymolyzed in vitro to obtain the peptide that transports trace elements.

Opioid peptides. Many kinds of food proteins will produce opioid peptides after enzymatic hydrolysis. For example, other proteins of casein milk, bovine casein, human milk protein, wheat protein and rice protein have the main function of analgesia.

The difference between it and the current analgesic is that it enters the human body through the digestive organs without any side effects. To detect whether the peptide has physiological function or activity, the guinea pig ileum detection system is generally used.

Because many bioactive peptides can regulate ileal contraction. Opioid peptides were mainly detected by this system.

The opioid peptides, which are made of wheat gluten, are the result of pepsin and microbial neutral protease in vitro. No such active peptide was detected in pepsin hydrolysate.

The β - casein morphine peptide released by casein is the result of enzymatic hydrolysis of gastrointestinal protease and microbial protease in vivo. Casein morphine peptide is mainly used as a tool for pharmacological research, as a therapeutic drug for animals and people, as well as a marker of pathological and physiological state.

Growth promoting peptide. This peptide can stimulate the growth of beneficial bacteria, especially Lactobacillus. Enzymatic hydrolysates such as insulin, casein, ribonuclease and soybean protein.

Cyclopeptide CHP. Cyclopeptide CHP, as a special peptide sequence, is listed because of its diversity of biological activities. It is partially derived from TRH (thyrotropin releasing hormone in hypothalamus), and widely distributed in human central nervous system and gastrointestinal tract. Exogenous CHP can show many biological activities, such as satiety and insulin inhibition in mice And glucagon secretion.

After oral intake, exogenous CHP can be absorbed by gastrointestinal tract and show biological activity. Many foods have CHP, such as noodles, milk free ice cream, ham, eggs, bread, tuna, whole milk, fish sauce, dried shrimp, which are determined by immunochemistry. Among them, the content of dried shrimp is the highest.

The origin of these CHP like peptides in food is not clear, but it is likely to be due to the thermal hydrolysis or enzymolysis of proteins during food processing.

There are many cyclopeptides in the cyclopeptide family, such as cyclohexin and cyclooctapeptide. Some cyclic peptides exist naturally in some plants or animals and have many physiological activities. For example, Rubia cordifolia contains a highly effective and non-toxic anti-cancer oligopeptide.

With the rapid development of protein engineering, enzyme engineering and food science and technology, a large number of bioactive peptides will be found continuously. Through the application of biotechnology, many bioactive oligopeptides can be produced, which can be used in food additives, oligopeptide end products, health care drugs, cosmetics additives, plant auxin, animal feed additives, preservatives, etc.

The 21st century will be the century of peptides. Bioactive peptides have a strong diversity of activities and physiological functions, which will attract worldwide attention.

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Chengdu Shengnuo Biotechnology Co., Ltd. has "Chengdu polypeptide drug engineering technology research center" in Chengdu, mainly engaged in polypeptide, polypeptide drug and beauty peptide research. Our zero defect has passed the FDA certification, and now it has become the first-class professional peptide drug and product development, technology transfer, technical service and peptide drug industry in the scale production and export of China's parks.