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Characterization of membrane-bound lipase from a thermophilic Rhizopus oryzae isolated from palm oil mill effluent


Citation

Abdul Razak, Che Nyonya and Musani, Rosiah and Basri, Mahiran and Salleh, Abu Bakar (1999) Characterization of membrane-bound lipase from a thermophilic Rhizopus oryzae isolated from palm oil mill effluent. Journal of the American Oil Chemists' Society, 76 (2). pp. 171-174. ISSN 0003-021X; ESSN: 1558-9331

Abstract / Synopsis

The characteristics of the membrane-bound lipase from a thermophilic Rhizopus oryzae were studied. The pH and temperature optima for lipase activity were at 7.0 and 37°C, respectively. The enzyme was stable and acidic conditions, retaining more than 80% of its initial activity at pH 4.0 after 30 min incubation. It was stable up to 50°C with 70% of initial activity retained after 3 h incubation. The enzyme is 1,3 specific and exhibits substrate preference. Monoacid triglyceride substrates were hydrolyzed better than methyl esters, polyoxysorbitan and sorbitan substrates.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
DOI Number: https://doi.org/10.1007/s11746-999-0214-0
Publisher: AOCS Press
Keywords: Characterization; Lipase; Membrane-bound lipase; Rhizopus oryzae
Depositing User: Nabilah Mustapa
Date Deposited: 02 Feb 2016 12:05
Last Modified: 02 Feb 2016 12:05
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1007/s11746-999-0214-0
URI: http://psasir.upm.edu.my/id/eprint/22569
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