Purification and characterization of lipase from Rhizopus chinensis cells.
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.
Yasuda
M
M
Department of Chemical Engineering, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
Ogino
H
H
Kiguchi
T
T
Kotani
T
T
Takakura
S
S
Ishibashi
T
T
Nakashima
T
T
Fukuda
H
H
Ishikawa
H
H