Alpha-D-Mannosidase from Capsicum Annuum

Priya Sethu, K. M. and Prabha, T. N. (1997) Alpha-D-Mannosidase from Capsicum Annuum. Phytochemistry, 44 (5). pp. 383-387.

PDF Phytochemistry_44(5)383-387_1997.pdf Restricted to Registered users only Download (471kB)

Abstract

Alpha-D-Mannosidase (EC 3.2.1.24), a glycosidase showing a consistent increase in activity with the progress in softening in Capsicum annuum, was purified to electrophoretic homogeneity by fractionation with ammonium sulphate followed by gel filtration on Sephadex G-100, ion-exchange chromatography on DEAE Sephadex A-50 and HPLC gel filtration on GF 250. The purified enzyme had a native and a SDS M, of 43 000 and 23 000, respectively. The optimal pH was 5.7 and the optimal temperature was 50”. The enzyme was thermally stable up to 60” for 15 min. The K, for p-nitrophenyl alpha-D-mannopyranoside was 0.7 mM. The enzyme activity was inhibited nearly 95% by Fe’+ and Cu” at 0.1 mM. The preparation was free of other glycosidases. Antibodies were raised against the purified enzyme for further studies on the physiological function of a-D-mannosidase in fruit systems. This is the first report on purification to homogeneity and characterization of alpha-D-mannosidase from fruit systems.

Item Type:	Article
Uncontrolled Keywords:	Capsicum annuum; Solanaceae; bell-pepper; enzyme purification; characterization; glycosidase; alpha-mannosidase
Subjects:	600 Technology > 08 Food technology > 23 Vegetables 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions:	Plant Cell Biotechnology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	24 Sep 2007 10:39
Last Modified:	28 Dec 2011 09:30
URI:	http://ir.cftri.res.in/id/eprint/1422

Actions (login required)

View Item