Purification and characterization of membrane-bound peroxidases from Metroxylon sagu
Two membrane-bound peroxidases, mPOD-I and mPOD-II, have been isolated and purified from Metroxylon sagu, using a combination of temperature-induced phase partitioning, DEAE-Toyopearl 650M, CM-Toyopearl 650 M and gel filtration. The mPOD-I and mPOD-II had molecular mass of 51.2 and 43.8 kDa, respect...
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Format: | Article |
Language: | English |
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Elsevier
2004
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Online Access: | http://psasir.upm.edu.my/id/eprint/24179/1/Purification%20and%20characterization%20of%20membrane.pdf |
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author | Onsa, Galila Hassan Saari, Nazamid Selamat, Jinap Bakar, Jamilah |
author_facet | Onsa, Galila Hassan Saari, Nazamid Selamat, Jinap Bakar, Jamilah |
author_sort | Onsa, Galila Hassan |
collection | UPM |
description | Two membrane-bound peroxidases, mPOD-I and mPOD-II, have been isolated and purified from Metroxylon sagu, using a combination of temperature-induced phase partitioning, DEAE-Toyopearl 650M, CM-Toyopearl 650 M and gel filtration. The mPOD-I and mPOD-II had molecular mass of 51.2 and 43.8 kDa, respectively, as determined by SDS–PAGE. Both enzymes showed high efficiency of interaction with the substrates. The isoenzymes were highly inhibited by ascorbic acid, metabisulfite, l-cysteine and p-coumaric acid. The inhibition mode of action and inhibition rate constant (Ki) values for these inhibitors were determined. Their activities were highly enhanced by Al3+, Ca2+ and Fe3+ but they were moderately inhibited by Zn2+. |
first_indexed | 2024-03-06T07:59:05Z |
format | Article |
id | upm.eprints-24179 |
institution | Universiti Putra Malaysia |
language | English |
last_indexed | 2024-03-06T07:59:05Z |
publishDate | 2004 |
publisher | Elsevier |
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spelling | upm.eprints-241792016-12-23T08:45:06Z http://psasir.upm.edu.my/id/eprint/24179/ Purification and characterization of membrane-bound peroxidases from Metroxylon sagu Onsa, Galila Hassan Saari, Nazamid Selamat, Jinap Bakar, Jamilah Two membrane-bound peroxidases, mPOD-I and mPOD-II, have been isolated and purified from Metroxylon sagu, using a combination of temperature-induced phase partitioning, DEAE-Toyopearl 650M, CM-Toyopearl 650 M and gel filtration. The mPOD-I and mPOD-II had molecular mass of 51.2 and 43.8 kDa, respectively, as determined by SDS–PAGE. Both enzymes showed high efficiency of interaction with the substrates. The isoenzymes were highly inhibited by ascorbic acid, metabisulfite, l-cysteine and p-coumaric acid. The inhibition mode of action and inhibition rate constant (Ki) values for these inhibitors were determined. Their activities were highly enhanced by Al3+, Ca2+ and Fe3+ but they were moderately inhibited by Zn2+. Elsevier 2004-05 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/24179/1/Purification%20and%20characterization%20of%20membrane.pdf Onsa, Galila Hassan and Saari, Nazamid and Selamat, Jinap and Bakar, Jamilah (2004) Purification and characterization of membrane-bound peroxidases from Metroxylon sagu. Food Chemistry, 85 (3). pp. 365-376. ISSN 0308-8146; ESSN: 1873-7072 http://www.sciencedirect.com/science/article/pii/S0308814603003637 10.1016/j.foodchem.2003.07.013 |
spellingShingle | Onsa, Galila Hassan Saari, Nazamid Selamat, Jinap Bakar, Jamilah Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title | Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title_full | Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title_fullStr | Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title_full_unstemmed | Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title_short | Purification and characterization of membrane-bound peroxidases from Metroxylon sagu |
title_sort | purification and characterization of membrane bound peroxidases from metroxylon sagu |
url | http://psasir.upm.edu.my/id/eprint/24179/1/Purification%20and%20characterization%20of%20membrane.pdf |
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