Premium
Studies on plant gums: Characterisation of neem ( Azadirachta indica ) gum protease as a glycoprotein
Author(s) -
Nayak B. Ramakrishna,
Pattabiraman Thillaisthanam N.
Publication year - 1982
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740330311
Subject(s) - protease , chemistry , chromatography , affinity chromatography , sephadex , monosaccharide , sepharose , biochemistry , arabinose , galactose , polyacrylamide gel electrophoresis , gel permeation chromatography , xylose , fermentation , organic chemistry , enzyme , polymer
A protease has been purified from neem gum by chromatography of the partially demetallised gum on TEAE‐cellulose and by affinity chromatography on concanavalin A‐Sepharose 4B. The protease was found to be homogeneous by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis and by chromatography on Sephadex G‐200 in the presence of 6M urea. The protease contained covalently bound carbohydrate to the extent of 19%. The monosaccharide units mannose, glucosamine, arabinose, galactose, fucose, xylose and glucose in an approximate molar ratio of 4:3:3:2:2:1:1, constituted the carbohydrate portion of the protease. The linkage between the carbohydrate and protein segments in the protease was found to be an N ‐glycosidic bond involving glucosamine.