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Applied and Environmental Microbiology, March 2002, p. 1250-1256, Vol. 68, No. 3
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.3.1250-1256.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Novel {alpha}-Glucosidase from Aspergillus nidulans with Strong Transglycosylation Activity

Naoki Kato, Sachie Suyama, Masao Shirokane, Masashi Kato, Tetsuo Kobayashi,* and Norihiro Tsukagoshi

Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan

Received 29 October 2001/ Accepted 19 December 2001

Aspergillus nidulans possessed an {alpha}-glucosidase with strong transglycosylation activity. The enzyme, designated {alpha}-glucosidase B (AgdB), was purified and characterized. AgdB was a heterodimeric protein comprising 74- and 55-kDa subunits and catalyzed hydrolysis of maltose along with formation of isomaltose and panose. Approximately 50% of maltose was converted to isomaltose, panose, and other minor transglycosylation products by AgdB, even at low maltose concentrations. The agdB gene was cloned and sequenced. The gene comprised 3,055 bp, interrupted by three short introns, and encoded a polypeptide of 955 amino acids. The deduced amino acid sequence contained the chemically determined N-terminal and internal amino acid sequences of the 74- and 55-kDa subunits. This implies that AgdB is synthesized as a single polypeptide precursor. AgdB showed low but overall sequence homology to {alpha}-glucosidases of glycosyl hydrolase family 31. However, AgdB was phylogenetically distinct from any other {alpha}-glucosidases. We propose here that AgdB is a novel {alpha}-glucosidase with unusually strong transglycosylation activity.


* Corresponding author. Mailing address: Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan. Phone: 81-52-7894086. Fax: 81-52-7894087. E-mail: koba{at}agr.nagoya-u.ac.jp.


Applied and Environmental Microbiology, March 2002, p. 1250-1256, Vol. 68, No. 3
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.3.1250-1256.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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