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| Progress on transglutaminase-catalyzed enzymatic glycosylation in protein/polypeptide modification |
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| KeyWord:transglutaminase glycosylation glycopeptide functional property |
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| Abstract: |
| In order to expand the application scope of proteins, proteins are often modified, and the enzymatic glycosylation reaction catalyzed by transglutaminase (TGase) has been applied in the modification of various proteins/polypeptides. In order to provide a reference for the wide application of enzymatic glycosylation of protein/polypeptide, the source of TGase, types of reaction and substrate catalyzed by TGase were briefly described, and the evaluation methods of the glycosylation degree of glycosylated protein/polypeptide and changes of main functional properties of modified product were highlighted. At present, TGase is mainly derived from microorganisms, and it can catalyze three types of reaction, including substrate cross-linking, acyl transfer (enzymatic glycosylation) and deamidation. In TGase-catalyzed enzymatic glycosylation reactions, RP-HPLC, ortho-phthalaldehyde (OPA) and 3,5-dinitrosalicylic acid methods are commonly used to evaluate the degree of glycosylation. Functional properties of product such as solubility, emulsification, and thermal stability of substrates can be improved to varying degrees through enzymatic glycosylation. The enzymatic glycosylation reaction catalyzed by TGase still has problems such as complex reaction system and low glycosylation efficiency, and further research is needed to solve it. |
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