Partial Characterization of Acid Phosphatase from Ginger (Zingiber Officinale) Rhizomes
Journal Title: GJRA-Global Journal For Research Analysis - Year 2015, Vol 4, Issue 5
Abstract
Acid phosphatase has been isolated and purified from ginger rhizome following conventional methods of protein purification with a molecular weight of 46kDa as judged by SDS-PAGE. The enzyme was found to be more stable around pH 5-9 and it was less stable at acidic pH (3-4) and the alkaline pH (10-11). The enzyme was completely inactive when exposed to 900C for 30min. The Km value of acid phosphatase was found to be 0.083M calculated from Line weaver- Burk plot and showed broad substrate specificity. Of the metals tested, only Zn2+ at 10mM concentration inhibited the enzyme to an extent of 60% and the rest of the metals tested were ineffective either in activating or inhibiting the enzyme. The activity of the enzyme was unaffected when it was exposed to 0.1% urea and guanidine hydrochloride. It was, however, inactivated to an extent of 50% when exposed to SDS (0.1%).
Authors and Affiliations
Amrutha Mani Prabha Jaladi, Muni Kumar Dokka, Siva Prasad Davuluri
Keywords
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