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Purification and Characterization of a Lipase from Aspergillus oryzae

1995; Oxford University Press; Volume: 59; Issue: 7 Linguagem: Inglês

10.1271/bbb.59.1199

1347-6947

Jinichi Toida, K Kondoh, Mikio Fukuzawa, Kunio Ohnishi, Junichi Sekiguchi,

Biofuel production and bioconversion

A lipase from Aspergillus oryzae was purified by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interaction chromatography, and anion exchange chromatography. The purified enzyme was a monomeric protein with a molecular mass of 41 kDa estimated by SDS-PAGE and 39 kDa by gel filtration. The optimum pH at 30°C and optimum temperature at pH 7.0 were 7.0 and 30°C, respectively. The enzyme was stable over a pH range of 6-9 at 25°C for 18 h, and up to 30°C at pH 7.0 for 3 h. Ag+, Fe3+, Hg2+, Cu2+, and Zn2+ inhibited the enzyme activity severely. The enzyme was a lipase that hydrolyzed monoacylglycerols and diacylglycerols, but did not hydrolyze triacylglycerols. The N-terminal amino acid sequence of the enzyme was highly homologous with that of the mono- and diacylglycerol lipase from Penicillium camembertii U-150.