COPURIFICATION OF A HEAT-STABLE ANTIOXIDANT WITH THE SUPEROXIDE-DISMUTASE ACTIVITY FROM DRIED PEAS

Authors
NICE DJ ROBINSON DS
Citation
Dj. Nice et Ds. Robinson, COPURIFICATION OF A HEAT-STABLE ANTIOXIDANT WITH THE SUPEROXIDE-DISMUTASE ACTIVITY FROM DRIED PEAS, Food chemistry, 48(4), 1993, pp. 353-357
Citations number
15
Categorie Soggetti
Food Science & Tenology","Nutrition & Dietetics","Chemistry Applied
Journal title
Food chemistry → ACNP
ISSN journal
03088146
Volume
48
Issue
4
Year of publication
1993
Pages
353 - 357
Database
ISI
SICI code
0308-8146(1993)48:4<353:COAHAW>2.0.ZU;2-H
Abstract
A heat-stable antioxidant component was observed to co-purify with the superoxide dismutase (SOD) activity from dried peas. The heat-stable component co-purified by size (gel filtration on Sephadex G-75) and by charge (flat-bed isoelectric focusing (IEF) and Rotofor IEF) coincide ntly with the SOD activity. Throughout the purification procedure the SOD fractions all exhibited heat-stable antioxidant activity. The auto xidation of linoleic acid in the presence of the pea SOD fraction was delayed for more than four weeks. Purified pea SOD may provide a novel protein-bound, thermostable natural oxidant.