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Chemical studies on rice bran lipase.
| Content Provider | CSIR - Central Food Technological Research Institute (CFTRI) |
|---|---|
| Author | Sastry, B. S. Rao, M. R. Raghavendra |
| 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. |
| Starting Page | 190 |
| Ending Page | 200 |
| Page Count | 11 |
| File Format | |
| Journal | Cereal Chemistry. |
| Volume Number | 52 |
| Language | English |
| Access Restriction | Authorized |
| Subject Keyword | Enzymes Rice |
| Content Type | Text |
| Resource Type | Article |
