How much do you know about the difference between protein and protein peptide?

1. Re-understand protein peptides

Many people think that collagen and collagen peptide products are similar. They are all made of fish skin, pig skin, beef bone, and pig bone. The nutritional content is similar, and the functional effects are not very different. However, through multi-manufacturer and multi-product horizontal comparison, collagen peptides with a molecular weight of less than 1,000 Daltons, collagen peptides with a molecular weight of more than 2500 Daltons, and collagen products with a molecular weight of 5000 to 10,000 Daltons exhibit completely different effects. The information on the Internet is flooded with different voices. After sorting out the papers and information, we found that the protein peptide products produced by bio-enzyme technology now have smaller molecular weights and improved quality, which are absorbed and utilized by the human body. The way is also different. After more than 100 years of inexplicable efforts, people have gradually realized the way the human body absorbs protein substances, from the traditional protein digestion and absorption theory (amino acid absorption theory) to the later small molecule protein peptide and amino acid absorption theory. Based on this, people began to explore the true value of protein peptides, and this is another story.

In 1901, Cohnheim et al. [3] discovered the intestinal mucosal extract "erepsin" containing protease, which proved that the digestion products of protein in the small intestine were amino acids, and then proposed the "traditional protein digestion and absorption theory", that is, the protein must be completely hydrolyzed into Free amino acids (FAA) can be absorbed by the small intestine. This traditional theory lasted until 1953. Agar et al. [4] observed the transport of intact Gly-Gly across the epithelium in the rat intestine, proving that in addition to amino acids, the intestine can also completely absorb and transport diglycin. In 1962, Newey et al. [5] proposed that there is a second mode of absorption of protein hydrolysates, that is, dipeptides can be completely absorbed. Since then, Adibi et al., Matthews, Gardner et al. [6] all proved that small peptides can be directly absorbed. In 1983, Ganapathy et al. [7] described the existence of a small peptide transport and absorption system and Fei et al. [8] successfully cloned the small peptide vector PepT1 in 1994, which proved that oligopeptides, especially small peptides, can not be digested into free amino acids. Instead, it is directly transported into the cell by the carrier in the form of a peptide.

From the actual process, we can find that in the gastrointestinal environment, the action time and effect of a variety of proteases can indeed break down the protein in the food into amino acids, but not all of them. It is more likely that the food is digested and decomposed. , The probability and effect of protease's further contact with small molecule protein peptides will gradually weaken. Therefore, the nutrient absorption in our intestines and stomach should have coexisted with free amino acids and small molecule protein peptides. It is the best choice. As a biological organism, this method is undoubtedly the choice with the lowest energy loss and the highest material absorption efficiency. The process of direct absorption of small protein peptides into small intestinal cells also promotes the initiation of a series of information in the small intestine to a certain extent, guides small intestinal cells to accelerate absorption efficiency, and regulates the growth of intestinal microflora. As some small molecular peptides in the blood reach the body, it is different. Location produces information transmission and functional activity effects.

Small molecular protein peptides are not digestive intermediates but are nutrients and active substances that can be directly absorbed. It is not only nutrition but also an important biologically active substance needed by the human body.