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

Brian N Mathibe; Samkelo Malgas; Layla Radosavljevic; Vishal Kumar; Pratyoosh Shukla; Brett I Pletschke

doi:10.1007/s12088-020-00879-2

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

Indian J Microbiol. 2020 Sep;60(3):392-395. doi: 10.1007/s12088-020-00879-2. Epub 2020 May 11.

Authors

Brian N Mathibe¹, Samkelo Malgas¹, Layla Radosavljevic¹, Vishal Kumar², Pratyoosh Shukla², Brett I Pletschke¹

Affiliations

¹ Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape 6140 South Africa.
² Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana 124001 India.

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.

Keywords: Endo-1,4-β-xylanase; Protein sequence; Thermomyces lanuginosus; Tryptic mapping; Xylanase structure.