Improving thermal stability of xylanase by introducing aromatic residues at the N-terminus / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1217-1224, 2014.
Article
in Chinese
| WPRIM
| ID: wpr-345603
ABSTRACT
Thermophilic and alkalophilic xylanases have great potential in the pulp bleaching industry. In order to improve the thermal stability of an alkaline family 11 xylanase Xyn11A-LC, aromatic residues were introduced into the N-terminus of the enzyme by rational design. The mutant increased the optimum temperature by 5 degrees C. The wild type had a half-time of 22 min at 65 degrees C and pH 8.0 (Tris-HCl buffer). Under the same condition, the mutant had the half-time of 106 min. CD spectroscopy revealed that the melting temperature (T(m)) values of the wild type and mutant were 55.3 degrees C and 67.9 degrees C, respectively. These results showed that the introduction of aromatic residues could enhance the thermal stability of Xyn11A-LC.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Temperature
/
Enzyme Stability
/
Protein Engineering
/
Chemistry
/
Endo-1,4-beta Xylanases
/
Hydrogen-Ion Concentration
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2014
Type:
Article
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