Bioprocess for the production of recombinant HAP phytase of the thermophilic mold Sporotrichum thermophile and its structural and biochemical characteristics
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文摘
A ∼41-fold improvement in rStPhy production has been achieved under constitutive GAP promoter as compared to that of wild strain S. thermophile. Analysis of surface properties of rStPhy revealed the critical factors that determine thermostability of the protein. The catalytically important amino acids (Arg74, His75, Arg78, His368 and Asp369) were identified by docking and site directed mutagenesis studies.

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