Hydrophobic interaction between beta-sheet B1 and B2 in xylanase XYNB influencing the enzyme thermostability / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 414-419, 2005.
Article
in Chinese
| WPRIM
| ID: wpr-305259
ABSTRACT
A homology modeling of xylanase XYNB from Streptomyces olivaceoviridis A1 was made by Swiss-Model. The hydrophobic Interaction between beta-sheet B1 and B2 in the tertiary structure model of XYNB was compared with other thermophilic xylanase. A T11Y mutation was introduced in XYNB by site-dirrected mutagenesis to improve the thermostability of the enzyme. The XYNB and mutant xylanase (XYNB') expressed in Pichia pastoris were purified and their enzymatic properties were determined. The result revealed that the thermostability of XYNB' was obviously higher than that of XYNB. The optimal temperature of XYNB' for its activity was 60 degrees C, similar to XYNB. But, compare to XYNB, the optimal pH value, the Km value and the specific activity of XYNB' had also been changed. The research results suggested that the aromatic interaction between beta-sheet B1 and B2 in xylanase should increase enzyme thermostability. The mutant xylanase XYNB' is a good material for further research in the relationship between structure and function of xylanase.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pichia
/
Protein Conformation
/
Streptomyces
/
Bacterial Proteins
/
Enzyme Stability
/
Recombinant Proteins
/
Chemistry
/
Mutagenesis, Site-Directed
/
Beta-Glucosidase
/
Protein Structure, Tertiary
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2005
Type:
Article
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