TITLE

Site-Directed Mutagenesis and Thermostability of Xylanase XYNB from Aspergillus niger 400264

AUTHOR(S)
Jie Xie; Lingling Song; XinRan Li; XiuLi Yi; Hui Xu; Jing Li; Dairong Qiao; Yi Cao
PUB. DATE
January 2011
SOURCE
Current Microbiology;Jan2011, Vol. 62 Issue 1, p242
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Xylanase is one of the most important hemicellulases in industry. However, its low thermostability limits its applications. In this study, one thermostable xylanase-producing strain 400264 was obtained from screening 11 Aspergillus niger strains (producing thermotolerant xylanase), and the optimum temperature of crude xylanase extracted from it was 55°C. Original activity of the crude xylanase is 64% at 60°C and 55% at 85°C with an incubation time of 30 min, respectively. After the expression of recombinant xylanase gene (xynA/xynB), the XYNB (xylanase B) showed higher thermostability than XYNA (xylanase A). Recombinant enzyme XYNB retained 94% of its activity for 10 min at 85°C, while XYNA with no activity left. Site-directed mutagenesis was performed to replace Ala33 of XYNB by Ser33 resulting 19% decrease in enzyme activity after incubating at 85°C for 30 min. It suggested that the Ala33 residue may have a certain effect on the thermophilic adaptation of xylanase.
ACCESSION #
56525143

 

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