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...

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Main Authors: Ghazali, H.M., Leong, C.K.
Format: Article
Published: Elsevier 1987
Online Access:http://psasir.upm.edu.my/id/eprint/114135/
https://linkinghub.elsevier.com/retrieve/pii/030881468790046X
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spelling my.upm.eprints.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
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
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.
format Article
author Ghazali, H.M.
Leong, C.K.
spellingShingle Ghazali, H.M.
Leong, C.K.
Polygalacturonase activity in starfruit
author_facet Ghazali, H.M.
Leong, C.K.
author_sort Ghazali, H.M.
title Polygalacturonase activity in starfruit
title_short Polygalacturonase activity in starfruit
title_full Polygalacturonase activity in starfruit
title_fullStr Polygalacturonase activity in starfruit
title_full_unstemmed Polygalacturonase activity in starfruit
title_sort polygalacturonase activity in starfruit
publisher Elsevier
publishDate 1987
url http://psasir.upm.edu.my/id/eprint/114135/
https://linkinghub.elsevier.com/retrieve/pii/030881468790046X
_version_ 1817844705051803648
score 13.235796