ArticleWorld journal of microbiology & biotechnology2013
Molecular and biochemical characterization of a new alkaline active multidomain xylanase from alkaline wastewater sludge.
Article in World journal of microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Gene cloning, expression, and characterization of two endo-xylanases fromFrontiers in microbiology · 2023Article
- Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase fromMarine drugs · 2020Article
- The extracellular endo-β-1,4-xylanase with multidomain from the extreme thermophileBiotechnology for biofuels · 2019Article
- Molecular and Biochemical Characterization of a Bimodular Xylanase FromFrontiers in microbiology · 2019Article
- DEPTOR at the Nexus of Cancer, Metabolism, and Immunity.Physiological reviews · 2018Review
- The thermophilic biomass-degrading fungus Thielavia terrestris Co3Bag1 produces a hyperthermophilic and thermostable β-1,4-xylanase with exo- and endo-activity.Extremophiles : life under extreme conditions · 2017Article
- Microbial community structure and dynamics in thermophilic composting viewed through metagenomics and metatranscriptomics.Scientific reports · 2016Article
- Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.The Journal of biological chemistry · 2016Article
- A Novel Multi-domain High Molecular, Salt-Stable Alkaline Xylanase fromFrontiers in microbiology · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A xylanase gene, xyn-b39, coding for a multidomain glycoside hydrolase (GH) family 10 protein was cloned from the genomic DNA of the alkaline wastewater sludge of a paper mill. Its deduced amino acid sequence of 1,481 residues included two carbohydrate-binding modules (CBM) of family CBM_4_9, one catalytic domain of GH 10, one family 9 CBM and three S-layer homology (SLH) domains. xyn-b39 was expressed heterologously in Escherichia coli, and the recombinant enzyme was purified and characterized. Xyn-b39 exhibited maximum activity at pH 7.0 and 60 °C, and remained highly active under alkaline conditions (more than 80 % activity at pH 9.0 and 40 % activity at pH 10.0). The enzyme was thermostable at 55 °C, retaining more than 90 % of the initial activity after 2 h pre-incubation. Xyn-b39 had wide substrate specificity and hydrolyzed soluble substrates (birchwood xylan, beechwood xylan, oat spelt xylan, wheat arabinoxylan) and insoluble substrates (oat spelt xylan and wheat arabinoxylan). Hydrolysis product analysis indicated that Xyn-b39 was an endo-type xylanase. The K (m) and V (max) values of Xyn-b39 for birchwood xylan were 1.01 mg/mL and 73.53 U/min/mg, respectively. At the charge of 10 U/g reed pulp for 1 h, Xyn-b39 significantly reduced the Kappa number (P < 0.05) with low consumption of chlorine dioxide alone.
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