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Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis


Citation

Salleh, Abu Bakar and Abdul Razak, Che Nyonya and Abd Samad, Mohd Yusoff and Ampon, Kamaruzaman and Wan Yunus, Wan Md. Zin and Basri, Mahiran (1996) Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis. Sains Malaysiana, 25 (4). pp. 131-141. ISSN 0126-6039

Abstract / Synopsis

Lipase from a newly isolated strain of Rhizopus rhizopodifonnis was partially purified and characterized. By acetone fractionation, the enzyme was purified to about 2.8 fold, with 62.5% recovery and with specific activity of 3.2 U/mg. By gel filtration through Sephadex G-100, the enzyme was further purified to 9.7 fold and had a specific activity of 11.1 U/mg. By polyacrylamide gel electrophoresis, five protein bands were observed after acetone fractionation, white two protein bands were observed after the preparation was passed through Sephadex G-100. It has a pH optimum at 6.0 and a temperature optimum at 45°C. The enzyme is most stable at pH 7.0 and temperature of 50°C. The enzyme has a preference for short chain triglycerides and can also hydrolyse some methyl esters. The lipase is specific for 1,3 positions.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
Publisher: Penerbit Universiti Kebangsaan Malaysia
Keywords: Rhizopus rhizopodifonnis; Lipase; Purification; Characterization
Depositing User: Nabilah Mustapa
Date Deposited: 02 Feb 2016 12:03
Last Modified: 02 Feb 2016 12:03
URI: http://psasir.upm.edu.my/id/eprint/22573
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