Transxylosylation of β-Xylosidase from Aspergillus awamori K4
β-Xylosidase from Aspergillus awamori K4 was purified. The optimum pH and temperature were around pH 4 and 70°C, and the molecular weight was estimated to be 117,000 on SDS-PAGE analysis. The enzyme has broad acceptor specificity in transxylosylation. Especially, its acceptor accessibility for sorbi...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 61; no. 12; pp. 2010 - 2014 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Taylor & Francis
1997
Japan Society for Bioscience Biotechnology and Agrochemistry |
Subjects | |
Online Access | Get full text |
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Summary: | β-Xylosidase from Aspergillus awamori K4 was purified. The optimum pH and temperature were around pH 4 and 70°C, and the molecular weight was estimated to be 117,000 on SDS-PAGE analysis. The enzyme has broad acceptor specificity in transxylosylation. Especially, its acceptor accessibility for sorbitol and mannitol of sugar alcohols were higher than that for monosaccharides. Trehalose was a much more effective acceptor than maltose and lactose of other disaccharides. In the reaction with 13-14% xylooligosaccharides (consisting of 3.4% xylose, 67.9% xylobiose, and 28.7% xylotriose) and 9-13% acceptors (sorbitol, mannitol, and trehalose), the amount of transfer products for each acceptor was 7-11% in 24 h. On
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H- and
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C-NMR analysis, main transfer products with sorbitol and mannitol were 6-O-β-xylosyl sorbitol (77.3%) and l(6)-O-β-xylosyl mannitol (73.7%), respectively. Two products with trehalose were 6 (6′)-O-β-xylosyl trehalose (52.1%) and 6,6′-O-β-di-xylosyl trehalose (47.9%). |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.61.2010 |