Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
ISSN-L : 1344-7882
Regular Paper
Characterization of Three Fungal Isomaltases Belonging to Glycoside Hydrolase Family 13 That Do not Show Transglycosylation Activity
Isomaltases from Filamentous Fungi
Hiroki Eisawa, Shun Ogawa, Nobuhiro Yamazaki, Kohki Maekawa, Takahiro Yamaguchi, Shota Sato, Kazuma Shiota, Takashi Yoshida
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Keywords: α-glucosidase, isomaltase, Aspergillus, Fusarium, fungi
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2017 Volume 64 Issue 1 Pages 9-13

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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, Aspergillus oryzae (agl1), A. niger (agdC), and Fusarium oxysporum (foagl1), and expressed in Escherichia coli. 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 p-nitrophenyl-α-glucoside was used as the substrate.

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© 2017 by The Japanese Society of Applied Glycoscience
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