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. 1991 Apr;57(4):987–992. doi: 10.1128/aem.57.4.987-992.1991

Production, Purification, and Characterization of β-(1-4)-Endoxylanase of Streptomyces roseiscleroticus

Anthony C Grabski 1,†, Thomas W Jeffries 1,*
PMCID: PMC182834  PMID: 16348475

Abstract

Twelve species of Streptomyces that formerly belonged to the genus Chainia were screened for the production of xylanase and cellulase. One species, Streptomyces roseiscleroticus (Chainia rosea) NRRL B-11019, produced up to 16.2 IU of xylanase per ml in 48 h. A xylanase from S. roseiscleroticus was purified and characterized. The enzyme was a debranching β-(1-4)-endoxylanase showing high activity on xylan but essentially no activity against acid-swollen (Walseth) cellulose. It had a very low apparent molecular weight of 5,500 by native gel filtration, but its denatured molecular weight was 22,600 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It had an isoelectric point of 9.5. The pH and temperature optima for hydrolysis of arabinoxylan were 6.5 to 7.0 and 60°C, respectively, and more than 75% of the optimum enzyme activity was retained at pH 8.0. The xylanase had a Km of 7.9 mg/ml and an apparent Vmax of 305 μmol · min-1 · mg of protein-1. The hydrolysis rate was linear for xylan concentrations of less than 4 mg/ml, but significant inhibition was observed at xylan concentrations of more than 10 mg/ml. The predominant products of arabinoxylan hydrolysis included arabinose, xylobiose, and xylotriose.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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