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Proteins and trypsin inhibitor activity of guar ( Cyamopsis tetragonoloba L. Taub) seed
Author(s) -
Kaur Perminder,
Bhatia Iqbal S.
Publication year - 1984
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.2740350907
Subject(s) - cyamopsis , sephadex , chromatography , trypsin , chemistry , trypsin inhibitor , polyacrylamide gel electrophoresis , tris , molecular mass , polyacrylamide , guar , biochemistry , enzyme , polymer chemistry
Proteins soluble in tris‐acetate buffer (pH9.0) were fractionated by DEAE‐cellulose, DEAE‐Sephadex A‐50 and Sephadex G‐200 column chromatography. The purified proteins which contained 5–6% carbohydrate, had molecular weights of 125 900 and 22 390 amu. The high molecular weight fraction was homogeneous by polyacrylamide gel electrophoresis. Proteins extracted in phosphate buffer (0.1 M , pH7.6) when subjected to Sephadex G‐200 gel chromatography were resolved into three fractions, all of which showed considerable trypsin inhibitor activity. Germination for 3 days reduced the trypsin inhibitor activity of the seed by about 30%.
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