Zhu Xiaochong, Tang Shuangyan
CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Beijing 100101, China.
Sheng Wu Gong Cheng Xue Bao. 2021 Aug 25;37(8):2623-2632. doi: 10.13345/j.cjb.200565.
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.
α-L-鼠李糖苷酶是一种非常重要的工业酶，广泛分布于多种生物体中。不同来源的α-L-鼠李糖苷酶表现出功能多样性。例如，细菌来源的α-L-鼠李糖苷酶的最适pH接近中性或碱性，而真菌来源的α-L-鼠李糖苷酶的最适pH在酸性范围内。此外，不同来源的α-L-鼠李糖苷酶的酶学性质在最适温度、热稳定性和底物特异性方面存在差异，这决定了这些酶的不同应用。因此，通过分析其酶学性质来阐明不同来源的α-L-鼠李糖苷酶催化机制和底物特异性的异同至关重要。此外，探索和了解糖苷配基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也很重要。这些知识有助于发现具有工业意义的α-L-鼠李糖苷酶并促进其工业应用。
