α-L-鼠李糖苷酶特性简述及影响酶活的因素

Enzymatic properties of α-L-rhamnosidase and the factors affecting its activity: a review

摘要:

α-L-鼠李糖苷酶是一个非常重要的工业酶，广泛分布于各种生物中。不同来源的α-L-鼠李糖苷酶具有多样性。细菌来源的α-L-鼠李糖苷酶的最适pH接近中性或偏碱性，而真菌来源的α-L-鼠李糖苷酶的最适pH在酸性范围。除此之外，不同来源的α-L-鼠李糖苷酶在最适温度、热稳定性和底物特异性等方面也不尽相同，酶学性质的差异，决定了其在工业应用时所具有的优势和限制。因此，分析不同来源的α-L-鼠李糖苷酶的酶学性质、阐明其在催化机制和底物特异性等方面的异同点、探究底物的糖苷配体和金属阳离子对酶活性的影响以及L-鼠李糖和葡萄糖对酶的竞争性抑制作用，可以为工业生产中准确选择α-L-鼠李糖苷酶提供参考，进一步推动该酶的工业化应用进程。

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.