A novel thermostable xylanase GH10 from Malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology
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A novel thermostable xylanase GH10 from Malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology
BACKGROUND The search for novel thermostable xylanases for industrial use has intensified in recent years, and thermophilic fungi are a promising source of useful enzymes. The present work reports the heterologous expression and biochemical characterization of a novel thermostable xylanase (GH10) from the thermophilic fungus Malbranchea pulchella, the influence of glycosylation on its stability...
متن کاملStudies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
An alkalitolerant fungus, Aspergillus fumigatus strain MA28 produced significant amounts of cellulase-free xylanase when grown on a variety of agro-wastes. Wheat bran as the sole carbon source supported higher xylanase production (8,450 U/L) than xylan (7,500 U/L). Soybean meal was observed to be the best nitrogen source for xylanase production (9,000 U/L). Optimum medium pH for xylanase produc...
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Aspergillus flavus is a common saprophyte and opportunistic pathogen that produces numerous secondary metabolites. The primary objectives of the A. flavus genomics program are to reduce and eliminate aflatoxin contamination in food and feed and to discover genetic factors that contribute to plant and animal pathogenicity. A. flavus expressed sequence tags (ESTs) and whole-genome sequencing have...
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Background Trichoderma reesei is considered a candidate fungal enzyme producer for the economic saccharification of cellulosic biomass. However, performance of the saccharifying enzymes produced by T. reesei is insufficient. Therefore, many attempts have been made to improve its performance by heterologous protein expression. In this study, to increase the conversion efficiency of alkaline-pret...
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ژورنال
عنوان ژورنال: Biotechnology for Biofuels
سال: 2014
ISSN: 1754-6834
DOI: 10.1186/1754-6834-7-115