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Purification and characterization of lipase from Rhizopus chinensis cells

M Yasuda¹, H Ogino, T Kiguchi

¹Department of Chemical Engineering, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.

Journal of Bioscience and Bioengineering

|October 20, 2005

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.

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