Cereal Chem 53:190 - 200.  |  VIEW ARTICLE
Chemical Studies on Rice Bran Lipase.

B. S. Shastry and M. R. Raghavendra Rao. Copyright 1976 by the American Association of Cereal Chemists, Inc. 

Rice bran lipase contained 16.00 +/- 0.15% nitrogen and was composed of about 320 amino acid residues. It also had a small quantity of lipid material (about 0.5%). The calculated molecular weight from SDS- polyacrylamide gel electrophoresis (and by gel filtration of Sephadex G-100) was about 40,000 +/- 2,000. Disc gel electrophoresis in the presence or absence of 8M urea and results of experiments on molecular- weight determination indicated that the enzyme had no subunits. The amino terminal of the enzyme protein was blocked by acetyl group and the carboxy-terminal residue was phenylalanine. Among the sulfhydryl- blocking reagents, only p-chloromercuribenzoate significantly inhibited the enzyme activity. Iodine, hydrogen peroxide, copper sulfate, and higher concentrations of organofluorophosphates adversely affected lipase activity. Results of the experiments on the action of N-bromosuccinimide on lipase showed that the enzyme required one or more tryptophan residues for activity.