Partial Purification and Characterization of Lipases from Thermophilic Rhizopus Rhizopodiformis
Abu Bakar Salleh, and Razak C.N.A., and Samad M.Y.A., and Ampon K., and Yunus W.M.Z.W., and Basri M., (1996) Partial Purification and Characterization of Lipases from Thermophilic Rhizopus Rhizopodiformis. Sains Malaysiana , 25 (4). pp. 131-141. ISSN 01266039 Full text not available from this repository. Official URL: http://pkukmweb.ukm.my/~jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html AffiliationsUniversiti Pertanian Malaysia, Faculty of Science and Environmental Studies["lib/metafield:join_corp_creators" not defined]Universiti Pertanian Malaysia, Faculty of Science and Environmental Studies["lib/metafield:join_corp_creators" not defined]Universiti Pertanian Malaysia, Faculty of Science and Environmental Studies["lib/metafield:join_corp_creators" not defined]Universiti Pertanian Malaysia, Faculty of Science and Environmental Studies["lib/metafield:join_corp_creators" not defined]Universiti Pertanian Malaysia, Faculty of Science and Environmental Studies["lib/metafield:join_corp_creators" not defined]Universiti Pertanian Malaysia, Faculty of Science and Environmental Studies AbstractLipase 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.
Lipase daripada satu stren Rhizopus rhizopodifonnis yang baru dipencilkan telah diseparatulen dan diciri. Melalui fraksi asiton, enzim telah ditulen lebih kurang 2.8 ganda, dengan pengutipan 62.5% dan aktiviti spesifik 3.2 U/mg. Dengan penurasan gel melalui Sephadex G-l00, enzim ditulenkan lagi hingga 9.7 ganda dengan aktiviti spesifik mencapai 11.1 U/mg. Dengan elektroforesis gel poliakritamida, 5 jalur protein didapati selepas fraksi asetone, sementara 2 jalur protein dilihati selepas penurasan gel Sephadex G-10. Enzim ini mempunyai pH optimum pada pH 6.0 dan suhu optimumnya ialah 45°C Enzim ini paling stabit pada pH 7.0 dan suhu 50°C Enzim mempunyai kepilihan pada trigliserida rantai pendek dan dapat menghidrolisiskan beberapa ester metit. Lipase ini spesifik pada posisi 1,3. | Item Type: | Journal |
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| Additional Information: | This note was added by the search_and_modify.pl script. |
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| Keywords: | Rhizopus rhizopodifonnis, Lipase, enzymes |
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| Subjects: | Q Science, Computer Science |
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| ID Code: | 3245 |
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