期刊
FOOD CHEMISTRY
卷 128, 期 3, 页码 725-730出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2011.03.096
关键词
Horseradish cv. Balady; Peroxidase; Purification; Phenolic compounds
资金
- King Abdulaziz University [3-114/430]
An anionic peroxidase POIII, molecular weight 56 kDa, was purified from the roots of horseradish cv. Balady. The enzyme exhibited high activity towards o-phenylenediamine and guaiacol, while o-dianisi-dine had moderate peroxidase activity. Pyrogallol and p-aminoantipyrine had low affinity toward POIII. POIII was found to have a temperature optimum at 40 degrees C; the enzyme activity remained stable up to 40 degrees C and retained 87%, 51% and 29% of its activity at 50, 60 and 70 degrees C, respectively. The enzyme exhibited more than 50% of activity in the pH range between 4.0 and 8.0 with its pH optimum at 5.5. Several metal cations had partial inhibitory effects toward POIII. Fe3+ enhanced the activity of the enzyme by 160% at 5 mM. All the metal chelators caused partial inhibitory effects toward POIII, except for EDTA at 1 mM, which had no effect on the enzyme. Crown Copyright (C) 2011 Published by Elsevier Ltd. All rights reserved.
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