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Phosphatases from rice bran.

Sastry, B. S. and Raghavendra Rao, M. R. (1972) Phosphatases from rice bran. Indian Journal of Biochemistry and Biophysics, 9. pp. 297-303.

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Abstract

A phosphodiesterase (orthophosphoric diesterase phosphohydrolase. EC 3.1.4.1) and a phosphomonoesterase (EC 3.1.3.1) from rice bran have been partially purified (10. and 70_fold respectively) by heat denaturation, ammonium sulphate fractionation, successive affinity chromatography on cellulose phosphate and chromatography on Sephadex G-150. The purified diesterase fraction runs as two bands and the monoesterase as one band on polyacrylamide disc gel electrophorograms at pH 8", although both enzymes run as a single band at pH 4'3. Both enzymes have a pH optimum at 5'0 with Km values of 0·56 mM and 0.84 mM for bis p- nitrophenyl phosphate and p_nitrophenyl phosphate as substrate respectively. Phosphodiesterase is activated by Co2+ and Mg2+, whereas phosphomonoesterase is not affected by these cations. Both enzymes are partially inhibited by Cu2+, Zn2+, NaF, pCMB. diisopropylftuorophosphate and inorganic phosphate. Theobromine and caffeine seem to inhibit phosphodiesterase activity at higher concentration only.

Item Type: Article
Uncontrolled Keywords: phosphodiesterase rice bran
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 16 Nutritive value > 07 Waste utilization
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 21 Dec 2016 07:50
Last Modified: 21 Dec 2016 07:50
URI: http://ir.cftri.com/id/eprint/4821

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