Purification And Characterization Of Protease From Artocarpus Integer Leaf
The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning w...
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| Format: | Thesis |
| Language: | English |
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2012
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| Online Access: | http://eprints.usm.my/44895/ http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf |
| _version_ | 1848880183683055616 |
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| author | Zulfigar,, Siti Balqis |
| author_facet | Zulfigar,, Siti Balqis |
| author_sort | Zulfigar,, Siti Balqis |
| building | USM Institutional Repository |
| collection | Online Access |
| description | The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning with 6 % (v/v) Triton X-114, 44 % (w/v) ammonium sulphate precipitation and gel filtration chromatography yielded a preparation with a 12-fold increase in enzyme purity and a final specific activity of 76.67 U/mg. The purified protease was maximally active at 40ºC and at pH 10.0. |
| first_indexed | 2025-11-15T17:59:05Z |
| format | Thesis |
| id | usm-44895 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T17:59:05Z |
| publishDate | 2012 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | usm-448952019-07-05T08:15:58Z http://eprints.usm.my/44895/ Purification And Characterization Of Protease From Artocarpus Integer Leaf Zulfigar,, Siti Balqis T1-995 Technology(General) The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning with 6 % (v/v) Triton X-114, 44 % (w/v) ammonium sulphate precipitation and gel filtration chromatography yielded a preparation with a 12-fold increase in enzyme purity and a final specific activity of 76.67 U/mg. The purified protease was maximally active at 40ºC and at pH 10.0. 2012-07 Thesis NonPeerReviewed application/pdf en http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf Zulfigar,, Siti Balqis (2012) Purification And Characterization Of Protease From Artocarpus Integer Leaf. Masters thesis, Universiti Sains Malaysia. |
| spellingShingle | T1-995 Technology(General) Zulfigar,, Siti Balqis Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title | Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title_full | Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title_fullStr | Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title_full_unstemmed | Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title_short | Purification And Characterization Of Protease From Artocarpus Integer Leaf |
| title_sort | purification and characterization of protease from artocarpus integer leaf |
| topic | T1-995 Technology(General) |
| url | http://eprints.usm.my/44895/ http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf |