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- Title
Expression and characterisation of a pH and salt tolerant, thermostable and xylose tolerant recombinant GH43 β-xylosidase from Thermobifida halotolerans YIM 90462<sup>T</sup> for promoting hemicellulose degradation.
- Authors
Yin, Yi-Rui; Xian, Wen-Dong; Han, Ming-Xian; Zhou, En-Min; Liu, Lan; Alkhalifah, Dalal Hussien M.; Hozzein, Wael N.; Xiao, Min; Li, Wen-Jun
- Abstract
A gene encoding a β-xylosidase (designated as Thxyl43A) was cloned from strain Thermobifida halotolerans YIM 90462T. The open reading frame of this gene encodes 550 amino acid residues. The gene was over-expressed in Escherichia coli and the recombinant protein was purified. The monomeric Thxyl43A protein presented a molecular mass of 61.5 kDa. When p-nitrophenyl-β-d-xylopyranoside was used as the substrate, recombinant Thxyl43A exhibited optimal activity at 55 °C and pH 4.0 to 7.0, being thermostable by maintaining 47% of its activity after 30 h incubation at 55 °C. The recombinant enzyme retained more than 80% residual activity after incubation at pH range of 4.0 to 12.0 for 24 h, respectively, which indicated notable thermostability and pH stability of Thxyl43A. Moreover, Thxyl43A displayed high catalytic activity (> 60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose. These properties suggest that Thxyl43A has potential for promoting hemicellulose degradation and other industrial applications.
- Subjects
GENE expression in bacteria; XYLOSIDASES; HEMICELLULOSE; ESCHERICHIA coli; RECOMBINANT proteins; HYDROGEN-ion concentration
- Publication
Antonie van Leeuwenhoek, 2019, Vol 112, Issue 3, p339
- ISSN
0003-6072
- Publication type
Article
- DOI
10.1007/s10482-018-1161-2