Abstract

Contamination with ochratoxin A (OTA) is widespread in many foods and it is necessary to look for modern and specialized methods to remove OTA. The current study aimed to produce protease and lipase from Levilactobacillus brevis and Lactobacillus plantarum, respectively, which were isolated from Egyptian soft cheese, and evaluate them on enzymatic degradation of OTA in phosphate buffered saline (PBS) after treatment with doses ranging from 50 to 200U/ml for 6, 2 and 18h at 37 °C. The results showed that 60–80 % saturation ammonium sulfate gave the highest protease activity (1295.95 U/ml) and specific activity (3570.11), while lipase recorded high-value activity (15608.2 U/ml) and Specific activity (40021.1) at 40-60% ammonium sulfate. Partially purified using Sephadex G -100 showed only one peak for protease and lipase at fraction 55 and 32, respectively. The results indicated that using protease and lipase at 200 U/ml gives the highest degradation for OTA after incubation for 18h were 82.6 and 77.3%, respectively. Enzymatic degradation of OTA indicated that the efficacy of protease and lipase for degradation of OTA increases with the duration of incubation and the dose of the enzyme.

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