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- W2364399788 abstract "By using overlap extension PCR,a P137G site mutant named xylA137 was introduced in the xylose isomerase gene xylA from Thermus thermphilus.The recombinant plasmid XM204-XI137 containing P137G was expressed in Saccharomyces cerevisiae H158 to produce the H158-XI137 strain.The results of enzymatic activity show that H158-XI137 is twice of the contrast H158-XI at 30?℃. In addition,the range of optimum pH become broader,while the thermostability decreases obviously.The result indicates that the proline at the position 137 of the xylose isomerase is not only very important for the enzymatic activity,but essential for maintaining the thermostability." @default.
- W2364399788 created "2016-06-24" @default.
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- W2364399788 date "2006-01-01" @default.
- W2364399788 modified "2023-09-22" @default.
- W2364399788 title "Influences of site-directed mutagenesis on the enzymeactivity and the thermostability of the xylose isomerase from Thermus thermphilus" @default.
- W2364399788 hasPublicationYear "2006" @default.
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