ArticleMarine drugs2013
Gene cloning, expression and characterization of a novel xylanase from the marine bacterium, Glaciecola mesophila KMM241.
Article in Marine drugs, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 43 citations in OpenAlex.
- Xylan Degradation in the Halotolerant BacteriumJournal of agricultural and food chemistry · 2025Article
- Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations.Food science & nutrition · 2025Review
- Characterization of thermophilic xylanases from Tengchong Qiaoquan hot spring for lignocellulose bioprocessing and prebiotic production.Frontiers in microbiology · 2025Article
- Identification of a novel glycoside hydrolase family 8 xylanase from Deinococcus geothermalis and its application at low temperatures.Archives of microbiology · 2024Article
- Marine Polysaccharides: Occurrence, Enzymatic Degradation and Utilization.Chembiochem : a European journal of chemical biology · 2021Review
- A New Group of Modular Xylanases in Glycoside Hydrolase Family 8 from Marine Bacteria.Applied and environmental microbiology · 2018Article
- Characterization of a novel cold-active xylanase from Luteimonas species.World journal of microbiology & biotechnology · 2018Article
- Effects of substrate binding site residue substitutions of xynA from Bacillus amyloliquefaciens on substrate specificity.BMC biotechnology · 2018Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Carbohydrate-active enzymes identified by metagenomic analysis of deep-sea sediment bacteria.Extremophiles : life under extreme conditions · 2014Article
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Authors and funding
12 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Marine xylanases are rather less studied compared to terrestrial xylanases. In this study, a new xylanase gene, xynB, was cloned from the marine bacterium, Glaciecola mesophila KMM241, and expressed in Escherichia coli. xynB encodes a multi-domain xylanase XynB of glycoside hydrolase (GH) family 8. The recombinant XynB comprises an N-terminal domain (NTD) with unknown function and a catalytic domain, which is structurally novel among the characterized xylanases of GH family 8. XynB has the highest identity (38%) to rXyn8 among the characterized xylanases. The recombinant XynB showed maximal activity at pH 6-7 and 35 °C. It is thermolabile and salt-tolerant. XynB is an endo-xylanase that demands at least five sugar moieties for effective cleavage and to hydrolyze xylohexaose and xylopentaose into xylotetraose, xylotriose and xylobiose. NTD was expressed in Escherichia coli to analyze its function. The recombinant NTD exhibited a high binding ability to insoluble xylan and avicel and little binding ability to chitosan and chitin. Since the NTD shows no obvious homology to any known carbohydrate-binding module (CBM) sequence in public databases, XynB may contain a new type of CBM.
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