作者: Mohamed Ali Borgi , Moez Rhimi , Samir Bejar
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摘要: The Ala103 to Gly mutation, introduced within the glucose isomerase from Streptomyces sp. SK (SKGI) decreased its catalytic efficiency (k(cat)/K(m)) toward D-glucose 7.1 3 mM(-1) min(-1). reverse counterpart replacement Gly103Ala into of olivochromogenes (SOGI) considerably improved be 6.7 instead 3.2 This later mutation also increased half-life time enzyme 70 95 min at 80 degrees C and mainly modified pH profile. These results provide evidence that residue plays an essential role in kinetic physicochemical properties isomerases species.