UPM Institutional Repository

Purification and characterization of membrane-bound peroxidases from Metroxylon sagu


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


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+.

Download File

PDF (Abstract)
Purification and characterization of membrane.pdf

Download (183kB) | Preview

Additional Metadata

Item Type: Article
Divisions: Faculty of Food Science and Technology
DOI Number: https://doi.org/10.1016/j.foodchem.2003.07.013
Publisher: Elsevier
Keywords: Metroxylon sagu; Pith; Membrane-bound peroxidases; Purification; Characterization
Depositing User: Nur Farahin Ramli
Date Deposited: 10 Oct 2013 04:52
Last Modified: 23 Dec 2016 08:45
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1016/j.foodchem.2003.07.013
URI: http://psasir.upm.edu.my/id/eprint/24179
Statistic Details: View Download Statistic

Actions (login required)

View Item View Item