Enzymes are highly selective biological molecules that speed up the rate of metabolic reaction. Living organisms usually maintain a relatively constant internal environment that keeps enzymes active, and deviation from norm would denature enzymes. This is true for most enzymes; however, calf intestinal alkaline phosphatase deviates from this norm. Our previous experiment showed that calf intestinal alkaline phosphatase was activated by trifloroethanol in carbonate buffer at pH 10 and temperatures 45�C, 65 �C. In our study, we tested the effect of Tris buffer at pH of 8 and 9, and at temperatures 25 �C, 45 �C and 65 �C on calf intestinal alkaline phosphatase. Para-Nitophenylphosphate was used as a substrate for the alkaline phosphatase in this experiment, after which the absorption and concentration of the reaction were recorded using spectrophotometer.

Effect of tris buffer on calf intestinal alkaline phosphatase

245th National Meeting (2013)

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