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Chemical studies on rice bran lipase.

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Relation http://ir.cftri.com/3428/
 
Title Chemical studies on rice bran lipase.
 
Creator Sastry, B. S.
Raghavendra Rao, M. R.
 
Subject 05 Enzymes
01 Rice
 
Description 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.
 
Date 1976
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/3428/1/Cereal%20Chemistry%2C%20Volume-52%28%20%281976%29%20190-200.pdf
Sastry, B. S. and Raghavendra Rao, M. R. (1976) Chemical studies on rice bran lipase. Cereal Chemistry, 52. pp. 190-200.