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Tryptic Mapping Based Structural Insights of Endo-1, 4-β-Xylanase from Thermomyces lanuginosus VAPS-24.

ABSTRACT: An endo-1,4-β-xylanase, XynA, from Thermomyces lanuginosus VAPS-24, was purified to homogeneity and exhibited a molecular mass of approximately 20 kDa. The protein sequence of XynA was found to be similar to those of other Thermomyces lanuginosus derived xylanases and, as a result, could be used as a model enzyme for understanding the protein structure-activity relationship and facilitating protein engineering to design enzyme variants with desirable properties. Therefore, this xylanase will be an attractive candidate for applications in the biofuel and fine chemical industries for the degradation of xylans in steam pre-treated biomass.

SUBMITTER: Mathibe BN

PROVIDER: S-EPMC7329953 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Tryptic Mapping Based Structural Insights of Endo-1, 4-β-Xylanase from Thermomyces lanuginosus VAPS-24.

Mathibe Brian N BN Malgas Samkelo S Radosavljevic Layla L Kumar Vishal V Shukla Pratyoosh P Pletschke Brett I BI

Indian journal of microbiology 20200511 3

An endo-1,4-β-xylanase, XynA, from Thermomyces lanuginosus VAPS-24, was purified to homogeneity and exhibited a molecular mass of approximately 20 kDa. The protein sequence of XynA was found to be similar to those of other Thermomyces lanuginosus derived xylanases and, as a result, could be used as a model enzyme for understanding the protein structure-activity relationship and facilitating protein engineering to design enzyme variants with desirable properties. Therefore, this xyl ...[more]

PMID: 32655201

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