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Chemical studies on rice bran lipase.

Sastry, B. S. and Raghavendra Rao, M. R. (1976) Chemical studies on rice bran lipase. Cereal Chemistry, 52. pp. 190-200.

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Abstract

Rice bran lipase contained 16.00 plus/minus 0.15% N and was composed of about 320 amino acid residues. It also had a small quantity of lipid material (about 0.5%). The calculated mol. wt. from sodium dodecyl sulphate-polyacrylamide gel electrophoresis (and by gel filtration on Sephadex G-100) was about 40 000 plus/minus 2000. Disc gel electrophoresis in the presence or absence of 8M urea and results of experiments on mol. wt. detn. 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 sulphydryl-blocking reagents, only p-chloromercuribenzoate significantly inhibited the enzyme activity. I, H2O2, copper sulphate, and higher concn. of organofluorophosphates adversely affected lipase activity. Results of experiments on the action of N-bromosuccinimide on lipase showed that the enzyme required one or more tryptophan residues for activity.

Item Type: Article
Uncontrolled Keywords: LIPASES-; rice bran lipases, activity of; BRAN-; RICE-; activity of rice bran lipases
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 21 Cereals > 01 Rice
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Jul 2016 10:25
Last Modified: 14 Jul 2016 10:25
URI: http://ir.cftri.com/id/eprint/3428

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