title: Purification and characterization of lipase from Rhizopus chinensis cells.
abstract: Lipase from Rhizopus chinensis cells was purified and characterized. The molecular mass of purified lipase was 28.4 kDa and the optimal temperature and pH for its activity were 37 degrees C and 5.5, respectively. Purified lipase exhibited high hydrolytic activity against fatty acid methyl esters such as methyl caprylate, methyl laurate, and methyl palmitate. Freeze-dried lipase catalyzed the transesterification between olive oil and methyl laurate in n-hexane.
authors.affiliation: Department of Chemical Engineering, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Yasuda
authors.forename: H
authors.initials: H
authors.lastname: Ogino
authors.forename: T
authors.initials: T
authors.lastname: Kiguchi
authors.forename: T
authors.initials: T
authors.lastname: Kotani
authors.forename: S
authors.initials: S
authors.lastname: Takakura
authors.forename: T
authors.initials: T
authors.lastname: Ishibashi
authors.forename: T
authors.initials: T
authors.lastname: Nakashima
authors.forename: H
authors.initials: H
authors.lastname: Fukuda
authors.forename: H
authors.initials: H
authors.lastname: Ishikawa