Isolation, fractionation, and some chemical studies on Kleinhovia hospita Linn. seed protein
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Protein was extracted from the seeds of Kleinhovia hospita Linn., which is being a nonconventional source. Extraction of K. hospita seed protein at various pH values in aqueous solution and at pH 7, different salt concentrations were done. Fractionation of protein from seeds was performed to separate albumin, globulin, prolamin, and glutelin. The amino acid compositions of total protein isolate (TPI) and the fractions were determined. A total of 15 amino acids were identified including 9 essential amino acids. Gel filtration by Sephadex G-100 revealed the presence of three components in the TPI. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of TPI and fractions showed different polypeptide bands having molecular weights ranging from 12 to 42 kDa approximately. Scanning electron microscopic study of TPI and fractions revealed the surface topology of the protein.