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What Is the Enzymatic Hydrolysis Mechanism of Protease in Food Industry?



Enzyme has the characteristics of high efficiency, safety, and green pollution-free, and is widely used in food industry, such as the meat soup used in restaurants, the mushroom soup used in hot pot restaurants, and the mushroom powder. Among them, the use of enzyme preparations, especially proteases, is the most extensive.


Characteristics and classification of protease


According to their sources


Proteases can be extracted from animals, plants, and microorganisms. There are many types of proteases in organisms. According to their sources, they can be divided into animal proteases, plant proteases, and microbial proteases. For example, papain from plants, alkaline protease from microbes, and trypsin from animal pancreas.


According to their modes of action


They can be divided into endopeptidases and exopeptidases. Neutral protease and alkaline protease belong to endopeptidases, while flavor enzymes belong to exopeptidases. Of course, there are also two kinds, such as acidic protease, endopeptidase, and exopeptidase. The difference between the two is mainly reflected in the hydrolysis ability. Usually, endopeptidase hydrolysis is more thorough, but the flavor and taste are not as good, while exopeptidase hydrolysis ability is generally poor, mainly manifested in more residues after hydrolysis, but the taste and flavor are better. Usually, the two are used in combination.


According to their optimal pH


They can be divided into acidic proteases, alkaline proteases, and neutral proteases. They can also be classified according to the different chemical properties of their active centers, such as serine proteases (the active center of the enzyme contains serine residues), thiol proteases (the active center of the enzyme contains thiol groups), metal proteases (the active center of the enzyme contains metal ions) and acidic proteases (the active center of the enzyme contains carboxyl groups).


The Mechanism of Protease Hydrolysis


In the process of food processing, important protease applications include protein hydrolysis, transpeptidation, and cross-linking reactions. Under the catalytic action of protease in food industry, the peptide chains in protein molecules are broken, and peptide molecules or free amino acids with shorter peptide bonds are generated. However, the catalytic reaction of ordinary proteases cannot accurately reflect the actual reaction process of proteases catalyzing protein hydrolysis. According to the theory of enzyme-catalyzed reactions, it is known that an intermediate between the enzyme and the substrate is formed during the reaction in the reactor. That is, before the peptide bond in the protein molecule is broken, the enzyme changes the reaction pathway through interactions with the substrate, but does not change the initial and final states of the reaction, thus reducing the activation energy of the hydrolysis reaction and enabling the reaction to proceed at a faster rate under mild conditions.


In the process of protease hydrolysis, protein molecules are the substrates for enzyme catalytic reactions, and the generated peptide molecules themselves can also become substrates for enzyme catalytic reactions, so the reaction generally proceeds continuously. In addition, since the amount of water in the reaction system is generally large, the trend of the reaction is to generate peptide fragments of different sizes. However, when the amount of the substrate or other amino acids is large in the reaction, the attack of the water molecule on the enzyme-peptide fragment in the final step of the reaction is not predominant, but rather the enzyme-peptide fragment is attacked by other peptide fragments or amino acids in the system, and protein synthesis reaction occurs. The newly generated peptide molecule and the original peptide molecule are significantly different in structure and properties.



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