Global Advanced Research Journal of Agricultural Science (GARJAS) ISSN: 2315-5094
June 2016 Vol. 5(6): pp. 195-203
Copyright © 2016 Global Advanced Research Journals

 

Full Length Research Paper

Purification and Characterization of Acid Phosphatase (AcPase) from Cotyledon of Erythrina indica

Emadeldin Hassan E. Konozy

 

Biotechnology Park, Africa City of Technology, Khartoum, B. O. Box: 13332, Sudan

Email: ehkonozy@yahoo.com

Accepted 07 June, 2016

 

Abstract

Acid phosphatase (AcPase) (EC 3.1.3.2) is a ubiquitous lysosomal enzyme that hydrolyzes phosphate esters at an acid pH and therefore, plays critical role in plant development and growth. AcPase from seeds of Erythrina indica, a leguminous plant, was extracted and purified 61 folds to apparent electrophoretic homogeneity in 5 purification steps which involved; ammonium sulphate fractionation, ConA-seralose 4B, acidification to pH 5 and finally DEAE-cellulose.  The native molecular weight of the enzyme as estimated by calibrated gelfiltration was 89kDa while 38 and 42kDa were obtained for subunits under reduced denatured SDS-PAGE conditions. AcPase had a broad pH optima from 4.5 to 5.5 with a maxima centered at around pH 5. The enzyme, as well, had a wide range of temperature optima ranging from 30 ͦ C to 55 ͦ C. AcPase activity was totally inhibited with Zn++, while 80% increase in activity was noticed in the presence of Cu++. The enzyme kinetics data, km and Vmax values, for hydrolysis of p-nitrophenyl phosphate were 3.3 and 13, respectively. AcPase was present in at least three isoforms, had a glycoprotein nature with mannose as terminal putative sugar.

Keywords: Acid phosphatase, Erythrina indica, leguminousae, purification, characterization.

   


 

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