From the medical point of view, extract are generally divided into plant extract (including herbal extract), animal extract. In general, the extracts we talk about can be understood as plant extract, herbal extract and animal extract. Animal extracts are extracted from animal bodies, some animal tissues or organs by mild enzymatic hydrolysis or boiling, then concentrated and dried by spray to become meat extracts. It is a new industry corresponding to plant extracts. Formerly commonly referred to as biochemical products, biochemical API. Its main categories are: amino acid, peptide, protein, enzyme and coenzyme, polysaccharide, lipid, nucleic acids and their derivatives. The biggest characteristic is that it can dissolve into water. Here we will introduce two promising animal extracts below:
Carboxypeptidases (CPs) are exopeptidases that degrade and release free amino acids one by one from the C end of the peptide chain. Commonly used are A, B, C and Y, 4 kinds of carboxypeptidase. Carboxypeptidase exists in the organism in the form of proenzyme and plays an important physiological function in the tissues and organs of animals and plants. Carboxypeptidase A and B are digestive enzymes, such as pancreatic carboxypeptidase A and B can be used to digest food. In addition, carboxypeptidase y(CPC) can act on any c-terminal residue, carboxypeptidase M(CPM) selectively participates in peptide hormone processing, carboxypeptidase D(CPD) and carboxypeptidase N(CPN) participate in peptide and protein processing, etc.
Carboxypeptidase is widely used in medicine, food and other industrial fields. In the field of medicine, since carboxypeptidase is widely involved in the biochemical reactions of the body, the detection of carboxypeptidase in the body can achieve the purpose of diagnosis and treatment of diseases. In addition, it can also be used for the degradation of undesirable substances (toxins, etc.) in the body. In the food industry, it can be used to prepare oligopeptides with high F value, remove ochratoxin from food and feed, and be used as a bitter reliever. In the field of biotechnology, carboxypeptidase can be used for the synthesis of polypeptides and the determination of polypeptide amino acid sequence. It can also be used as a model enzyme to help the research of other enzymes. The carboxypeptidase of animal origin mainly exists in the pancreas of pigs and cows, such as carboxypeptidase A/B, whose quantity is very limited and the price is very high, resulting in its limited application. Carboxypeptidase from microorganism exists in the vacuoles of yeast, aspergillus and other fungi, and has broad application prospect. Therefore, with the help of genetic engineering strategy, recombinant carboxypeptidase can be produced in large quantities with microorganism as the host, which is expected to overcome the limitations of animal and plant raw material sources encountered in the production process of carboxypeptidase, so as to further reduce the production cost, improve product quality, deepen the study of enzymatic properties and expand the application range.
Hyaluronidase is a kind of enzyme that can degrade hyaluronic acid. It is widely distributed in nature and exists in mammals, insects, leeches and bacteria. In recent years, the research on hyaluronidase has been increasing gradually, and its application in medicine, plastic surgery and other fields has attracted people's attention. Hyaluronidase was first discovered in 1928, when extracts from testicles and other tissues were discovered to act as a "diffusive factor" by promoting the penetration of other harmful venom components and enhancing their immobility in the bloodstream.
Hyaluronidase from different sources has some differences, but since its discovery, it has gradually gained people's attention and has been widely used in medicine and other fields. Based on this, the properties of hyaluronidase and other related research has become a field worthy of attention. It is widely distributed in various vertebrates (their testicles, animal venom, etc.) and invertebrates (insects, leeches, duodenal worms, etc.). It also exists in microorganisms (streptomyces, staphylococcus, clostridium, etc.). It has different substrate specificity, a wide range of pH values, different catalytic mechanisms and a variety of functions. Although much work has been done in this area, much remains to be done in the field of enzymology, particularly three-dimensional structures， site-directed mutants and enzymatic kinetics, to enhance understanding of binding sites, substrate recognition and catalytic mechanisms. Cloning more recombinases can determine the classification and association of these hyaluronidases. Further study the structure of purified hyaluronidase substrate to improve the understanding of the synergism of the enzyme. There are many unanswered questions regarding the regulation of expression, including complete gene sequences, the degree of regulatory coordination and the molecular mechanisms underlying the response to putative inducers. With the deepening of research, the characteristics of hyaluronidase from different sources have been gradually explored, which provides a new approach and theoretical basis for the prevention and treatment of hyaluronidase-related diseases.