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三种属于糖苷水解酶家族13且不具有转糖基化活性的真菌异麦芽糖酶的特性分析。

Characterization of Three Fungal Isomaltases Belonging to Glycoside Hydrolase Family 13 That Do not Show Transglycosylation Activity.

作者信息

Eisawa Hiroki, Ogawa Shun, Yamazaki Nobuhiro, Maekawa Kohki, Yamaguchi Takahiro, Sato Shota, Shiota Kazuma, Yoshida Takashi

机构信息

1 Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University.

2 Enzymes and Pharmaceuticals Laboratory, Godo Shusei Co., Ltd.

出版信息

J Appl Glycosci (1999). 2017 Feb 20;64(1):9-13. doi: 10.5458/jag.jag.JAG-2016_009. eCollection 2017.

Abstract

α-1,6-Glucosidase (isomaltase) belongs to glycoside hydrolase (GH) families 13 and 31. Genes encoding 3 isomaltases belonging to GH family 13 were cloned from filamentous fungi, (), (),and (), and expressed in . The enzymes hydrolyzed isomaltose and α-glucosides preferentially at a neutral pH, but did not recognize maltose, trehalose, and dextran. The activity of AgdC and Agl1 was inhibited in the presence of 1 % glucose, while Foagl1 was more tolerant to glucose than the other two enzymes were. The three fungal isomaltases did not show transglycosylation when isomaltose was used as the substrate and a similar result was observed for AgdC and Agl1 when -nitrophenyl-α-glucoside was used as the substrate.

摘要

α-1,6-葡萄糖苷酶(异麦芽糖酶)属于糖苷水解酶(GH)家族13和31。从丝状真菌中克隆出编码属于GH家族13的3种异麦芽糖酶的基因,()、()和(),并在()中表达。这些酶在中性pH下优先水解异麦芽糖和α-糖苷,但不识别麦芽糖、海藻糖和葡聚糖。在1%葡萄糖存在的情况下,AgdC和Agl1的活性受到抑制,而Foagl1比其他两种酶对葡萄糖更具耐受性。当以异麦芽糖为底物时,这三种真菌异麦芽糖酶未显示出转糖基化作用,当以对硝基苯基-α-葡萄糖苷为底物时,AgdC和Agl1也观察到类似结果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f39/8056888/04bf9f821099/JAG-64-009-g01.jpg

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