Journal
COMPTES RENDUS BIOLOGIES
Volume 332, Issue 5, Pages 426-432Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.crvi.2009.01.002
Keywords
Carthamus tinctorius L.; alpha-Amylase; Purification; Germination
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alpha-Amylase (alpha-1-4 D-glucan glucanohydrolase EC 3.2.1.1) crude extract was obtained from safflower (Carthamus tinctorius L.) cotyledons excised from 5-day-old dark grown seedlings. The enzyme was purified by precipitating the crude extract with ammonium sulphate at 20-60% saturation, and then by subjecting this fraction to affinity chromatography on a beta-cyclodextrin-Sepharose 613 column. The active fraction was dialysed and concentrated. An overall purification of about 131 folds with an activity yield of 81.25% was achieved. The molecular mass of purified enzyme determined by SDS-PAGE was 35 kD. When the purified alpha-amylase was subjected to gel electrophoresis followed by negative staining, only one band of active protein was detected. Its maximal activity was in the pH 6.0 and at a temperature of 55 degrees C. This enzyme was activated by Ca2+ and inhibited by Fe2+. To cite this article: M. Ben Elarbi et al., C. R. Biologies 332 (2009). (C) 2009 Academie des sciences. Published by Elsevier Masson SAS. All rights reserved.
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