ArticleApplied and environmental microbiology2012
Characterization of an endo-processive-type xyloglucanase having a β-1,4-glucan-binding module and an endo-type xyloglucanase from Streptomyces avermitilis.
Article in Applied and environmental microbiology, 2012. 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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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- An acidophilic GH12 xyloglucanase fromFrontiers in nutrition · 2026Article
- Characterization of glycoside hydrolases involved in xyloglucan degradation in the thermophilic bacterium Thermotoga maritima.Scientific reports · 2025Article
- Prospection of Fungal Lignocellulolytic Enzymes Produced from Jatoba (Microorganisms · 2021Article
- Configuration of active site segments in lytic polysaccharide monooxygenases steers oxidative xyloglucan degradation.Biotechnology for biofuels · 2020Article
- Adaptation of Syntenic Xyloglucan Utilization Loci of Human GutApplied and environmental microbiology · 2019Article
- Substrate specificity, regiospecificity, and processivity in glycoside hydrolase family 74.The Journal of biological chemistry · 2019Article
- GH30 Glucuronoxylan-Specific Xylanase from Streptomyces turgidiscabies C56.Applied and environmental microbiology · 2018Article
- Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase fromJournal of applied glycoscience · 2018Article
- In vitro and in vivo characterization of threeBiotechnology for biofuels · 2018Article
- Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv. campestris.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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Authors and funding
7 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We cloned two glycoside hydrolase family 74 genes, the sav_1856 gene and the sav_2574 gene, from Streptomyces avermitilis NBRC14893 and characterized the resultant recombinant proteins. The sav_1856 gene product (SaGH74A) consisted of a catalytic domain and a family 2 carbohydrate-binding module at the C terminus, while the sav_2574 gene product (SaGH74B) consisted of only a catalytic domain. SaGH74A and SaGH74B were expressed successfully and had molecular masses of 92 and 78 kDa, respectively. Both recombinant proteins were xyloglucanases. SaGH74A had optimal activity at 60°C and pH 5.5, while SaGH74B had optimal activity at 55°C and pH 6.0. SaGH74A was stable over a broad pH range (pH 4.5 to 9.0), whereas SaGH74B was stable over a relatively narrow pH range (pH 6.0 to 6.5). Analysis of the hydrolysis products of tamarind xyloglucan and xyloglucan-derived oligosaccharides indicated that SaGH74A was endo-processive, while SaGH74B was a typical endo-enzyme. The C terminus of SaGH74A, which was annotated as a carbohydrate-binding module, bound to β-1,4-linked glucan-containing soluble polysaccharides such as hydroxyethyl cellulose, barley glucan, and xyloglucan.
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