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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Site-directed mutagenesis of two fungal xylanases, PcXylA from Penicillium canescens and TrXyl3 from Trichoderma reesei, belonging to family 10 of glycoside hydrolases, was carried out in order to improve the enzyme thermostability. The most successful L18F mutant of PcXylA demonstrated an increase in the melting temperature by 4oC in comparison with the wild-type enzyme. As a result of insertion of five extra amino acid residues into the peptide loop forming the enzyme active site cleft, both xylanases acquired a resistance to XIP-type proteinaceous inhibitors, which reduce the enzyme efficiency in some biotechnological applications.