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Modification of the transglucosylation properties of α-glucosidases from Aspergillus oryzae and Aspergillus sojae via a single critical amino acid replacement.
Bioscience, Biotechnology, and Biochemistry ( IF 1.4 ) Pub Date : 2021-06-24 , DOI: 10.1093/bbb/zbab091
Atsushi Kawano 1 , Yuji Matsumoto 1 , Atsushi Terada 1 , Takashi Tonozuka 2 , Sawaki Tada 3 , Ken-Ichi Kusumoto 3 , Nozomu Yasutake 1
Affiliation  

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.

中文翻译:

通过单一的关键氨基酸置换修饰来自米曲霉和酱油曲霉的 α-葡糖苷酶的转葡糖基化特性。

我们通过突变第 450 位的氨基酸残基构建了来自米曲霉 (AoryAgdS) 和酱油曲霉 (AsojAgdL) 的 α-葡萄糖苷酶的酶变体。 AoryAgdS_H450R 获得了产生大量 α-1,6- 转葡萄糖基化产物的能力, AsojAgdL_R450H 改变为产生比 α-1,6-产物更多的 α-1,3- 和 α-1,4- 转葡萄糖基化产物。第 450 个氨基酸残基对于这些 α-葡糖苷酶的转葡糖基化至关重要。
更新日期:2021-06-24
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