What do you know about proteases?
Protease is a general term for a class of enzymes that hydrolyze protein peptide chains. According to its degradation of peptides is divided into two categories: endopeptidase and telopeptidase. The former can cut off the large molecular weight peptide chain from the middle to form smaller molecular weight prions and peptones; the latter can be divided into carboxypeptidases and aminopeptidases, which hydrolyze the peptide chain to generate amino acids one by one from the free carboxyl terminus or free amino terminus of the peptide respectively.
Classification
A general term for a class of enzymes that hydrolyze peptide bonds in proteins. According to the way they hydrolyze peptides, they can be divided into two categories: endopeptidases and exopeptidases. Endopeptidases cut off the internal part of protein molecules to form small molecular weight moonshine and peptones. Exopeptidases hydrolyze peptide bonds one by one from the free amino or carboxyl terminals of protein molecules to free amino acids, the former being aminopeptidases and the latter being carboxypeptidases. According to their active center and optimum pH, proteases can be further classified into serine proteases, mercapto proteases, metalloproteases and aspartic proteases. According to the optimum pH of their reaction, they are divided into acidic proteases, neutral proteases and alkaline proteases. The proteases used in industrial production are mainly endopeptidases.
Proteases are widely found in animal organs, plant stems and leaves, fruits and microorganisms. Microbial proteases, are produced mainly by molds and bacteria and to a lesser extent by yeast and actinomycetes.
Enzymes that catalyze the hydrolysis of proteins. There are many types, the important ones being pepsin, trypsin, histone, papain, and Bacillus subtilis protease. Protease on the role of the reaction substrate has strict selectivity, a protease can only act on a certain peptide bond in the protein molecule, such as trypsin catalyzed hydrolysis of alkaline amino acids formed by the peptide bond. Protease is widely distributed, mainly in the digestive tract of humans and animals, and abundant in plants and microorganisms. Due to the limited resources of plants and animals, the industrial production of protease preparations are mainly prepared by fermentation using microorganisms such as Bacillus subtilis and Aspergillus pernicius.
Role of trypsin
Trypsin works by hydrolyzing proteins between cells thereby dissociating the cells. Different tissues or cells respond differently to the action of trypsin. The activity of trypsin in dispersing cells is also related to its concentration, temperature and time of action. Trypsin solution has the strongest ability to act when the pH is 8.0 and the temperature is 37℃. When using trypsin, the concentration, temperature and time should be well controlled to avoid excessive digestion and cell damage. Because Ca2+, Mg2+ and serum, protein can reduce the activity of pancreatic enzyme, so the preparation of pancreatic enzyme solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks liquid. When terminating digestion, the action of trypsin on cells can be terminated with serum culture solution or trypsin inhibitor.
1. Weighing trypsin: according to the concentration of trypsin solution of 0.25%, use an electronic balance to accurately weigh the powder dissolved in a small beaker of double-distilled water (if double-distilled water needs to be adjusted to pH 7.2 or so) or PBS (D-hanks) solution. Stir well and leave overnight at 4 °C. 2.
2. Sterilization by syringe filtration: The prepared trypsin solution should be sterilized by filtration with a syringe filter (0.22 µm microporous membrane) in an ultra-clean bench. The solution should be sterilized by filtration with a syringe filter (0.22 micron microporous filter membrane) in an ultra-clean bench.
Trypsin catalyzes the hydrolysis of specific peptide bonds in proteins. The catalytic process is energy-free and does not inactivate the enzyme, nor does it change shape or hydrolyze itself. The binding of the substrate to the active center of the enzyme is reversible, and this binding makes the specific peptide bonds of proteins activated by bending and deformation, and more susceptible to attack by water molecules, which form the amino and carboxyl groups, respectively, and break them, yielding a small molecule peptide or amino acid. Different proteases can act on peptide bonds consisting of different amino acid linkages, so trypsin does not act on all peptide bonds.
Protease content
Hair removal and softening in the leather industry have made great use of proteases, which saves time and improves labor hygiene. Protease can also be used for silk degumming, meat tenderization, wine clarification. Clinically used for medicinal purposes, such as pepsin treatment of dyspepsia, acid protease treatment of bronchitis, scrupulous protease treatment of vasculitis, as well as the use of pancreatic protease, pancreatic lactic coagulation protease purification of purified surgical septic wounds and thoracic cavity plasma membrane adhesion treatment. Enzyme-added laundry detergent is a new product in detergents, containing alkaline protease, which can remove blood stains and protein stains on clothes, but when using it, be careful not to contact the skin, so as not to damage the proteins on the surface of the skin, which can cause rashes, eczema and other allergic phenomena.
Enzymes that catalyze protein hydrolysis. There are many types, the important ones are pepsin, trypsin, histone, papain and Bacillus subtilis protease. Protease has strict selectivity for the reaction substrate, a protease can only act on a certain peptide bond in the protein molecule, such as trypsin catalyzes the hydrolysis of peptide bonds formed by alkaline amino acids. Proteases are widely distributed, mainly in the digestive tract of humans and animals, and are abundant in plants and microorganisms. Due to the limited resources of plants and animals, the industrial production of protease preparations are mainly prepared by fermentation using microorganisms such as Bacillus subtilis and Aspergillus oryzae.
Widely used
Protease is one of the most important industrial enzymes that catalyzes the hydrolysis of proteins and peptides, and is widely found in animal organs, plant stems and leaves, fruits and microorganisms. Proteases are used extensively in cheese production, meat tenderization and modification of plant proteins. In addition, pepsin, pancreatic rennet, carboxypeptidase and aminopeptidase are proteases in the human digestive tract, in whose action the proteins ingested by the human body are hydrolyzed into small molecule peptides and amino acids.
The proteases currently used in the baking industry are mold proteases, bacterial proteases and plant proteases. The application of proteases in bread production alters gluten properties in a form that is different from the action of forces and the chemical reaction of reducing agents in bread modification. Instead of breaking disulfide bonds, the action of proteases is to disconnect the three-dimensional mesh structure that forms gluten. The role of proteases in bread production is mainly manifested in the dough fermentation process. Due to the action of proteases, the proteins in the flour are degraded into peptides and amino acids to supply the yeast with carbon sources and promote fermentation.
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| Compound Glucoamylase | 9032-08-0 |
| Pullulanase | 9075-68-7 |
| Xylanase | 37278-89-0 |
| Cellulase | 9012-54-8 |
| Naringinase | 9068-31-9 |
| β-Amylase | 9000-91-3 |
| Glucose oxidase | 9001-37-0 |
| alpha-Amylase | 9000-90-2 |
| Pectinase | 9032-75-1 |
| Peroxidase | 9003-99-0 |
| Lipase | 9001-62-1 |
| Catalase | 9001-05-2 |
| TANNASE | 9025-71-2 |
| Elastase | 39445-21-1 |
| Urease | 9002-13-5 |
| DEXTRANASE | 9025-70-1 |
| L-Lactic dehydrogenase | 9001-60-9 |
| Dehydrogenase malate | 9001-64-3 |
| Cholesterol oxidase | 9028-76-6 |