| Title : Purification and characterization of lipase from Rhizopus chinensis cells - Yasuda_1999_J.Biosci.Bioeng_88_571 |
| Author(s) : Yasuda M , Ogino H , Kiguchi T , Kotani T , Takakura S , Ishibashi T , Nakashima T , Fukuda H , Ishikawa H |
| Ref : J Biosci Bioeng , 88 :571 , 1999 |
|
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. |
| PubMedSearch : Yasuda_1999_J.Biosci.Bioeng_88_571 |
| PubMedID: 16232664 |
Yasuda M, Ogino H, Kiguchi T, Kotani T, Takakura S, Ishibashi T, Nakashima T, Fukuda H, Ishikawa H (1999)
Purification and characterization of lipase from Rhizopus chinensis cells
J Biosci Bioeng
88 :571
Yasuda M, Ogino H, Kiguchi T, Kotani T, Takakura S, Ishibashi T, Nakashima T, Fukuda H, Ishikawa H (1999)
J Biosci Bioeng
88 :571