Enzymatic properties of α-L-rhamnosidase and the factors affecting its activity: a review / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 2623-2632, 2021.
Artigo
em Chinês
| WPRIM
| ID: wpr-887828
ABSTRACT
α-L-rhamnosidase is a very important industrial enzyme that is widely distributed in a variety of organisms. α-L-rhamnosidase of different origins show functional diversity. For example, the optimal pH of α-L-rhamnosidase from bacteria is close to neutral or alkaline, while the optimal pH of α-L-rhamnosidase from fungi is in the acidic range. Furthermore, the enzymatic properties of α-L-rhamnosidases of different origins differ in terms of the optimal temperature, the thermal stability, and the substrate specificity, which determine the different applications of these enzymes. In this connection, it is crucial to elucidate the similarities and differences in the catalytic mechanism and substrate specificity of α-L-rhamnosidase of different origins through analyzing its enzymatic properties. Moreover, it is important to explore and understand the effects of aglycon and metal cations on enzyme activity and the competitive inhibition of L-rhamnose and glucose on enzymes. These knowledge can help discover α-L-rhamnosidase of industrial significance and promote its industrial application.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Ramnose
/
Especificidade por Substrato
/
Temperatura
/
Glicosídeo Hidrolases
/
Concentração de Íons de Hidrogênio
Idioma:
Chinês
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2021
Tipo de documento:
Artigo
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