Research Center for Fundamental Technologies, Showa Sangyo Co., Ltd., Funabashi City, Chiba, Japan.
Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Fuchu City, Tokyo, Japan.
Biosci Biotechnol Biochem. 2021 Jun 24;85(7):1706-1710. doi: 10.1093/bbb/zbab091.
We constructed enzyme variants of the α-glucosidases from Aspergillus oryzae (AoryAgdS) and Aspergillus sojae (AsojAgdL) by mutating the amino acid residue at position 450. AoryAgdS_H450R acquired the ability to produce considerable amounts of α-1,6-transglucosylation products, whereas AsojAgdL_R450H changed to produce more α-1,3- and α-1,4-transglucosylation products than α-1,6-products. The 450th amino acid residue is critical for the transglucosylation of these α-glucosidases.
我们通过突变位置 450 的氨基酸残基构建了来自米曲霉（AoryAgdS）和大豆曲霉（AsojAgdL）的α-葡萄糖苷酶的酶变体。AoryAgdS_H450R 获得了产生大量α-1,6-转葡糖苷产物的能力，而 AsojAgdL_R450H 则改变为产生更多的α-1,3-和α-1,4-转葡糖苷产物而不是α-1,6-产物。第 450 个氨基酸残基对这些α-葡萄糖苷酶的转葡糖苷作用至关重要。
