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Information × Registration Number 0221U100908, 0120U100128 , R & D reports Title The study of enzyme systems of enantioselective hydrolysis and tyrosinase inhibitors to create new biologically active compounds popup.stage_title Head Romanovska Іrina I., Доктор біологічних наук Registration Date 11-01-2021 Organization Physico-Chemical Institute O. Bogatsky National Academy of Sciences of Ukraine popup.description2  The object of study - carboxylesterase of porcine liver and hepatopancreas Rapana venosa. The purpose of the work is to obtain enzyme systems of the digestive glands of the mollusk Rapana venosa and porcine liver containing carboxylesterase, study of their biochemical and physicochemical characteristics (protein content, esterase activity, the effect of selective inhibitor, pH and thermal dependence of activity); determination of protein-fractional composition of carboxylesterases of digestive glands of mollusk Rapana venosa and porcine liver using SDS-electrophoresis. A method for isolating carboxylesterase from porcine liver was developed and an enzyme preparation with high esterase activity (130 units / mg) was obtained. The belonging of the obtained enzyme to the family of carboxylesterases was confirmed by complete inhibition of its activity by di- (p-nitrophenyl) -phosphate and by the results of electrophoretic studies in polyacrylamide gel. The physicochemical characteristics of the obtained enzyme were studied, its pH and temperature optimums, which were 7.0 and 40 ºC, respectively, were established. High preservation of activity was observed at pH 6.0-8.0 and temperatures of 40-50 ºC. Carboxylesterase was first obtained from the hepatopancreas of Rapana venosa and its molecular weight was set at 25.5 kDa. The belonging of the enzyme to the family of carboxylesterases was confirmed using di- (p-nitrophenyl) -phosphate. The physicochemical characteristics of carboxylesterase from Rapana venosa hepatopancreas were studied for the first time, it was shown that the pH-optimum of esterase activity was pH 5.5, the thermo-optimum of activity was 45 ° C. Product Description popup.authors Dekina Svitlana S. Mikhaylova Tetiana V. Ryzhak Oleksandra А. Romanovska Iryna І. Shesterenko Yevheniya A. Shesterenko Yuliya А. popup.nrat_date 2021-01-11 Close
R & D report
Head: Romanovska Іrina I.. The study of enzyme systems of enantioselective hydrolysis and tyrosinase inhibitors to create new biologically active compounds. (popup.stage: ). Physico-Chemical Institute O. Bogatsky National Academy of Sciences of Ukraine. № 0221U100908
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Updated: 2026-03-25