Purification and molecular properties of papaya pectinesterase
Pectinesterase (EC 3.1.1.11) was extracted and purified from papaya (Carica papaya L. var. exotica). The procedure adopted for purification resulted in an approximate 250-fold purification (784 units/mg protein) with a 45% recovery of the pectinesterase activity. The enzyme was eluted in a single pe...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
1994
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| Online Access: | http://psasir.upm.edu.my/id/eprint/113113/1/113113.pdf |
| _version_ | 1824452324213391360 |
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| author | Fayyaz, A. Asbi, B.A. Ghazali, H.M. Che Man, Y.B. Jinap, S. |
| author_facet | Fayyaz, A. Asbi, B.A. Ghazali, H.M. Che Man, Y.B. Jinap, S. |
| author_sort | Fayyaz, A. |
| collection | UPM |
| description | Pectinesterase (EC 3.1.1.11) was extracted and purified from papaya (Carica papaya L. var. exotica). The procedure adopted for purification resulted in an approximate 250-fold purification (784 units/mg protein) with a 45% recovery of the pectinesterase activity. The enzyme was eluted in a single peak after CmdashSephadex and Sephadex G-100 chromatography. The purified enzyme had a uniform specific activity throughout the final chromatographic peak. The enzyme preparation was confirmed to be of homogeneous state by gel filtration and nondashdenaturing polyacrylamide gel electrophoresis and it has a molecular weight of approximately 32 000 Da. |
| first_indexed | 2025-02-19T02:48:43Z |
| format | Article |
| id | upm.eprints-113113 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2025-02-19T02:48:43Z |
| publishDate | 1994 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | upm.eprints-1131132025-01-22T02:06:07Z http://psasir.upm.edu.my/id/eprint/113113/ Purification and molecular properties of papaya pectinesterase Fayyaz, A. Asbi, B.A. Ghazali, H.M. Che Man, Y.B. Jinap, S. Pectinesterase (EC 3.1.1.11) was extracted and purified from papaya (Carica papaya L. var. exotica). The procedure adopted for purification resulted in an approximate 250-fold purification (784 units/mg protein) with a 45% recovery of the pectinesterase activity. The enzyme was eluted in a single peak after CmdashSephadex and Sephadex G-100 chromatography. The purified enzyme had a uniform specific activity throughout the final chromatographic peak. The enzyme preparation was confirmed to be of homogeneous state by gel filtration and nondashdenaturing polyacrylamide gel electrophoresis and it has a molecular weight of approximately 32 000 Da. Elsevier 1994 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/113113/1/113113.pdf Fayyaz, A. and Asbi, B.A. and Ghazali, H.M. and Che Man, Y.B. and Jinap, S. (1994) Purification and molecular properties of papaya pectinesterase. Food Chemistry, 49 (4). pp. 373-378. ISSN 0308-8146; eISSN: 1873-7072 https://linkinghub.elsevier.com/retrieve/pii/0308814694900078 10.1016/0308-8146(94)90007-8 |
| spellingShingle | Fayyaz, A. Asbi, B.A. Ghazali, H.M. Che Man, Y.B. Jinap, S. Purification and molecular properties of papaya pectinesterase |
| title | Purification and molecular properties of papaya pectinesterase |
| title_full | Purification and molecular properties of papaya pectinesterase |
| title_fullStr | Purification and molecular properties of papaya pectinesterase |
| title_full_unstemmed | Purification and molecular properties of papaya pectinesterase |
| title_short | Purification and molecular properties of papaya pectinesterase |
| title_sort | purification and molecular properties of papaya pectinesterase |
| url | http://psasir.upm.edu.my/id/eprint/113113/1/113113.pdf |
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