ArticleInternational journal of molecular sciences2018
Improving Hydrolysis Characteristics of Xylanases by Site-Directed Mutagenesis in Binding-Site Subsites from Streptomyces L10608.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Investigating the effect of substrate binding on the catalytic activity of xylanase.Applied microbiology and biotechnology · 2023Article
- Bioengineered Enzymes and Precision Fermentation in the Food Industry.International journal of molecular sciences · 2023Review
- The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region.International journal of molecular sciences · 2022Article
- Glutamic acid assisted hydrolysis strategy for preparing prebiotic xylooligosaccharides.Frontiers in nutrition · 2022Article
- Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries.Biotechnology for biofuels · 2021Article
- In silico screening and experimental analysis of family GH11 xylanases for applications under conditions of alkaline pH and high temperature.Biotechnology for biofuels · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
The preparation of oligosaccharides via xylan hydrolysis is an effective way to add value to hemicellulosic material of agricultural waste. The bacterial strain Streptomyces L10608, isolated from soil, contains genes encoding xylanases of glucoside hydrolase family 10/11 (GH10/11), and these have been cloned to catalyze the production of xylooligosaccharide (XOS). To improve the XOS proportion of hydrolysates produced by xylanase, four amino acid residues were substituted by site-directed mutagenesis, and the mutant genes were overexpressed in
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