Eisawa Hiroki, Ogawa Shun, Yamazaki Nobuhiro, Maekawa Kohki, Yamaguchi Takahiro, Sato Shota, Shiota Kazuma, Yoshida Takashi
1 Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University.
2 Enzymes and Pharmaceuticals Laboratory, Godo Shusei Co., Ltd.
J Appl Glycosci (1999). 2017 Feb 20;64(1):9-13. doi: 10.5458/jag.jag.JAG-2016_009. eCollection 2017.
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.
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。