Purification and characterization of lipase from Rhizopus chinensis cells

Authors
Yasuda, M Ogino, H Kiguchi, T Kotani, T Takakura, S Ishibashi, T Nakashima, T Fukuda, H Ishikawa, H
Citation
M. Yasuda et al., Purification and characterization of lipase from Rhizopus chinensis cells, J BIOSCI BI, 88(5), 1999, pp. 571-573
Citations number
10
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723 → ACNP
Volume
88
Issue
5
Year of publication
1999
Pages
571 - 573
Database
ISI
SICI code
1389-1723(199911)88:5<571:PACOLF>2.0.ZU;2-Y
Abstract
Lipase from Rhizopus chinensis cells was purified and characterized. The mo lecular mass of purified lipase was 28.4 kDa and the optimal temperature an d pH for its activity were 37 degrees C and 5.5, respectively. Purified lip ase exhibited high hydrolytic activity against fatty acid methyl esters suc h as methyl caprylate, methyl laurate, and methyl palmitate. Freeze-dried L ipase catalyzed the transesterification between olive oil and methyl laurat e in n-hexane.