Polygalacturonase activity in starfruit
Polygalacturonase (PGase) was extracted and partially purified from ripe starfruit (Averrhoa carambola, L.). 2·3- and 7·8-fold purifications were obtained following purification by Amicon ultrafiltration and Sephadex G-100 filtration, respectively. The apparent pH optimum of PGase in the Amicon conc...
| Main Authors: | , |
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| Format: | Article |
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Elsevier
1987
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| Online Access: | http://psasir.upm.edu.my/id/eprint/114135/ |
| _version_ | 1848866414858862592 |
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| author | Ghazali, H.M. Leong, C.K. |
| author_facet | Ghazali, H.M. Leong, C.K. |
| author_sort | Ghazali, H.M. |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Polygalacturonase (PGase) was extracted and partially purified from ripe starfruit (Averrhoa carambola, L.). 2·3- and 7·8-fold purifications were obtained following purification by Amicon ultrafiltration and Sephadex G-100 filtration, respectively. The apparent pH optimum of PGase in the Amicon concentrate and gel filtrate (combined fractions 6-8) was 5·2. Viscometric and reductometric analyses, on PGase in the gel filtrate and paper chromatographic analysis on the enzyme reaction mixture, were carried out to ascertain the mode of action. The results obtained indicated that exoPGase was the only PGase enzyme present in ripe starfruit. |
| first_indexed | 2025-11-15T14:20:14Z |
| format | Article |
| id | upm-114135 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:20:14Z |
| publishDate | 1987 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1141352024-12-03T06:44:08Z http://psasir.upm.edu.my/id/eprint/114135/ Polygalacturonase activity in starfruit Ghazali, H.M. Leong, C.K. Polygalacturonase (PGase) was extracted and partially purified from ripe starfruit (Averrhoa carambola, L.). 2·3- and 7·8-fold purifications were obtained following purification by Amicon ultrafiltration and Sephadex G-100 filtration, respectively. The apparent pH optimum of PGase in the Amicon concentrate and gel filtrate (combined fractions 6-8) was 5·2. Viscometric and reductometric analyses, on PGase in the gel filtrate and paper chromatographic analysis on the enzyme reaction mixture, were carried out to ascertain the mode of action. The results obtained indicated that exoPGase was the only PGase enzyme present in ripe starfruit. Elsevier 1987 Article PeerReviewed Ghazali, H.M. and Leong, C.K. (1987) Polygalacturonase activity in starfruit. Food Chemistry, 24 (2). pp. 147-157. ISSN 0308-8146; eISSN: 0308-8146 https://linkinghub.elsevier.com/retrieve/pii/030881468790046X 10.1016/0308-8146(87)90046-x |
| spellingShingle | Ghazali, H.M. Leong, C.K. Polygalacturonase activity in starfruit |
| title | Polygalacturonase activity in starfruit |
| title_full | Polygalacturonase activity in starfruit |
| title_fullStr | Polygalacturonase activity in starfruit |
| title_full_unstemmed | Polygalacturonase activity in starfruit |
| title_short | Polygalacturonase activity in starfruit |
| title_sort | polygalacturonase activity in starfruit |
| url | http://psasir.upm.edu.my/id/eprint/114135/ http://psasir.upm.edu.my/id/eprint/114135/ http://psasir.upm.edu.my/id/eprint/114135/ |