Gene cloning and characterization of a cold-adapted β-glucosidase belonging to glycosyl hydrolase family 1 from a psychrotolerant bacterium Micrococcusantarcticus
Cold-adapted enzymes from psychrotolerant and psychrophilic microorganisms have recently received increasing attention,owing to their relevance for both basic and applied research. Contrast to mesophilic enzymes, cold-adapted enzymes are characterized by high specific activity (kcat), reduced activation energy, low optimum temperature and low stability at low and moderate temperatures. These properties offer cold-adapted enzymes potential application in different fields such as detergents, textile and food industries, and bioremediation of polluted soils and wastewaters at low and moderate temperatures.Β-Glucoside glycosyl hydrolase (EC 3.2.1.21), usually called β-glucosidase, catalyzes the hydrolysis of short-chain oligosaccharides (2-6 degrees of polymerization), alkyl, and aryl β-glucosides. Nowadays there is considerable interest in the biotechnological application of P-glucosidases relating to plant-based foods, for instance, conversion of phytoestrogen glucosides in fruits and vegetables to aglycone moieties, detoxification of cassva, aroma enhancement, and removing bitter compounds from citrus fruit juices or unripe olives. Cold-adapted P-glucosidases from psychrophilic bacteria have received increased attention for the fact that they raise considerable interest in both basic and applied research.Micrococcus antarcticus;cold-adapted β-glucosidase; enzymatic characterization;thermolabile
Hong-Xia Fan Li-Li Miao Ying Liu Hong-Can Liu Zhi-Pei Liu
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101
国内会议
厦门
英文
15-16
2011-11-25（万方平台首次上网日期，不代表论文的发表时间）