Characterization of recombinant yeast exo-β-1,3-glucanase (Exg 1p) expressed in Escherichia coli cells

Article abstract of DOI:10.1271/bbb.65.1310

Yeast exo-β-1,3-glucanase gene (EXG1) was expressed in Escherichia coli and the recombinant enzyme (Exg1p) was characterized. The recombinant Exglp had an apparent molecular mass of 45 kDa by SDS-PAGE and the enzyme has a broad specificity for β1,3-linkages as well as β-1,6-linkages, and also for other ss-glucosidic linked substrates, such as cellobiose and pNPG. Kinetic analyses indicate that the enzyme prefers small substrates such as laminaribiose, gentiobiose, and pNPG rather than polysaccharide substrates, such as laminaran or pustulan. With a high concentration of laminaribiose, the enzyme catalyzed transglucosidation forming laminarioligosaccharides. The enzyme was strongly inhibited with high concentrations of laminaran.

Full text of DOI:10.1271/bbb.65.1310

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Characterization of Recombinant Yeast Exo-β-1,3-
Glucanase (Exg 1p) Expressed in Escherichia coli
Cells
Kanako SUZUKIa, Tomio YABEa, Yutaka MARUYAMAa, Keietsu ABEa & Tasuku NAKAJIMAa
a Divison of Applied Life Science, Graduate School of Agricultural Science, Tohoku
University
Published online: 22 May 2014.
To cite this article: Kanako SUZUKI, Tomio YABE, Yutaka MARUYAMA, Keietsu ABE & Tasuku NAKAJIMA (2001)
Characterization of Recombinant Yeast Exo-β-1,3-Glucanase (Exg 1p) Expressed in Escherichia coli Cells, Bioscience,
Biotechnology, and Biochemistry, 65:6, 1310-1314, DOI: 10.1271/bbb.65.1310
To link to this article: http://dx.doi.org/10.1271/bbb.65.1310
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Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.