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- W2394557278 abstract "Aspergillus japonicus lipase was purified to homogeneity by Q-Sepharose and Sephadex G-100 column chromatography. The enzyme had a molecular weight of 43 KDa in SDS-PAGE. Purified A. japonicus lipase had a specific activity of 480 U/mg protein. The purification magnitude was 3.44 and the total yield was 4.53%. Purified A. japonicus lipase had an optimum pH of 7.5 while the optimum temperature was 40°C. Metal ions such as MnCl2 and CoCl2 exhibited an inhibitory effect on the enzyme. The enzyme displayed substrate specificity for ρ-nitrophenyl palmitate. The enzyme was stable in two organic solvents-methanol and acetone. An-ionic detergent, SDS inhibited its activity." @default.
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- W2394557278 date "2012-01-01" @default.
- W2394557278 modified "2023-09-26" @default.
- W2394557278 title "Purification and characterization of Aspergillus japonicus lipase from a pig fat production medium" @default.
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