Ontology highlight
ABSTRACT:
SUBMITTER: Mathibe BN
PROVIDER: S-EPMC7329953 | biostudies-literature | 2020 Sep
REPOSITORIES: biostudies-literature
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 <i>Thermomyces lanuginosus</i> 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 <i>Thermomyces lanuginosus</i> 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]