Abstract
A lipase from a Sporidiobolus pararoseus strain was purified from culture filtrate by (NH4)2SO4 precipitation, and DEAE-Toyopearl 650M, Butyl-Toyopearl 650M, and Toyopearl HW-55 chromatography. The purified enzyme appeared as a single band with a molecular mass of 37 kDa by SDS-PAGE. The optimum temperature and pH were approximately 60°C and 6.0, respectively. The specificity toward triglyceride was similar to that of pregastric esterase Lipase PGET. Addition of the lipase during the mozzarella cheese-making process produced a strong cheese flavor. Taken together, the lipase produced by S. pararoseus is considered a potential replacement of pregastric esterase in the dairy industry.
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