Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
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...
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Penerbit Universiti Kebangsaan Malaysia
1996
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Online Access: | http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf http://psasir.upm.edu.my/id/eprint/22573/ http://www.ukm.my/jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html |
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my.upm.eprints.225732016-02-02T04:03:43Z http://psasir.upm.edu.my/id/eprint/22573/ Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis Salleh, Abu Bakar Abdul Razak, Che Nyonya Abd Samad, Mohd Yusoff Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Basri, Mahiran 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. Penerbit Universiti Kebangsaan Malaysia 1996 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf 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 http://www.ukm.my/jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html |
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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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Salleh, Abu Bakar Abdul Razak, Che Nyonya Abd Samad, Mohd Yusoff Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Basri, Mahiran |
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Salleh, Abu Bakar Abdul Razak, Che Nyonya Abd Samad, Mohd Yusoff Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Basri, Mahiran Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
author_facet |
Salleh, Abu Bakar Abdul Razak, Che Nyonya Abd Samad, Mohd Yusoff Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Basri, Mahiran |
author_sort |
Salleh, Abu Bakar |
title |
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
title_short |
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
title_full |
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
title_fullStr |
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
title_full_unstemmed |
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis |
title_sort |
partial purification and characterization of lipases from thermophilic rhizopus rhizopodiformis |
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Penerbit Universiti Kebangsaan Malaysia |
publishDate |
1996 |
url |
http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf http://psasir.upm.edu.my/id/eprint/22573/ http://www.ukm.my/jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html |
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13.18916 |