Hello,
I am working on xylanolytic enzyme. During my recent study, in which I was trying to find for how long enzyme could be stable in buffer solutions (pH-5 to pH-9), I found that in some buffer solutions in which enzyme was diluted there was drop in enzyme activity over the period of incubation time (pH-5 and pH-6) but surprisingly there was increase in residual activity of enzyme after initial drop. What could be the possible reason for increase in residual activity? There are reports similar to this but without any proper explanation about this.
Off hand, I can think of two explanations:
- The enzyme was stored in an unsuitable buffer and regained activity when it was exposed to conditions more to its liking.
- Incubation destroyed some inhibitor of the enzyme, that happend to be present.
Engelbert Buxbaum Thank you very much Sir for your reply. Is there any possibility that incubation in buffer (different pH values) led to change in protein conformation which subsequently gave better catalytic properties?
Sure, that is my option #1. Ionic bonds and hydrogen bonds between polar and charged groups depend on pH and in part determine the tertiary structure of proteins. With luck, the change in structure is reversible.
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