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The degree and rate of inactivation of gamma-glutamyltransferase in raw cow's milk by heating at 50, 60, 70, and 80 degrees C for 1, 2, 3, 5, 10, 15, 20, 25, and 30 min were measured to evaluate the suitability of this enzyme as a marker for the pasteurization of milk. The enzymes alkaline phosphatase and lactate dehydrogenase were also measured under similar conditions for comparison. The patterns of heat inactivation of gamma-glutamyltransferase and alkaline phosphatase were similar, with only a minimal inactivation of the enzymes at 50 degrees C. The rate of inactivation increased as a result of increasing temperatures and time. A complete inactivation of both enzymes was seen at 70 degrees C after 10 min and at 80 degrees C after 1 min. Lactate dehydrogenase showed a higher heat resistance with almost complete inactivation at 70 degrees C for 30 min, and compete inactivation at 80 degrees C for 3 min. No activities of these enzymes were found in commercially pasteurized or heat-treated milk. The levels of gamma-glutamyltransferase in raw milk were between 8 and 10% higher than those of alkaline phosphatase and lactate dehydrogenase, making it more sensitive and accurate as a testing marker. It seems that gamma-glutamyltransferase may serve as a good pasteurization marker. Furthermore, the simplicity of testing and the availability of commercial kits for testing by both wet and dry chemistry make it an attractive choice, especially because dry chemistry procedures overcome the difficulties originating from the turbidity of milk, which interferes with spectrophotometric procedures.
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