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Information × Registration Number 0225U000286, (0123U100041) , R & D reports Title Study of hydrolytic enzyme systems of the digestive glands of the mollusk Rapana venosa, promising for the creation of biologically active compounds popup.stage_title Синтез естерів 2-(4-ізобутилфеніл)-пропіонової кислоти (ібупрофену), вивчення фізико-хімічних властивостей. Розробка умов та здійснення енантіоселективного гідролізу естерів 3-гідрокси-1,4-бенздіазепін-2-ону – перспективних сполук анксіолітичної і снодійної дії - та ібупрофену - нестероїдного протизапального засобу (НПЗЗ), який чинить спрямовану дію проти болю, жару, та запалення - за допомогою карбоксилестерази молюска Rapana venosa (рН, температура, термін проведення реакції гідролізу, співвідношення реагентів та ін.). Head Dekina Svitlana S., Доктор біологічних наук Registration Date 08-01-2025 Organization Physico-Chemical Institute O. Bogatsky National Academy of Sciences of Ukraine popup.description1 The purpose of this work is to study the hydrolytic enzyme systems of the digestive glands of the Rapana venosa mollusk, which contain carboxylesterase and collagenase, to obtain homogeneous and complex preparations of enzymes, to study their biochemical and physicochemical properties, the effect of inhibitors, the features of enantioselective hydrolysis of esters of nitrogen-containing heterocycles and ibuprofen to create biologically - active substances and preparations promising for use in medicine. popup.description2  Research object: The cytosolic carboxylesterase of the hepatopancreas of Rapana venosa. The aim of the work is to develop conditions and perform enantioselective hydrolysis of esters of 3-hydroxy-1,4-benzodiazepin-2-one—promising compounds with anxiolytic and sedative activity—and ibuprofen, a non-steroidal anti-inflammatory drug (NSAID) with targeted effects against pain, fever, and inflammation, using the carboxylesterase from the mollusk Rapana venosa. Conditions studied include pH, temperature, reaction duration, reagent ratio, and other factors. A method for isolating a highly stable carboxylesterase from the cytosolic fraction of the hepatopancreas of Rapana venosa was developed. The enzyme's molecular weight (57.2 kDa), subunit structure, biochemical, and physicochemical properties were determined. The classification of the isolated enzyme as part of the carboxylesterase family was confirmed by complete inhibition of its esterase activity using di-(p-nitrophenyl)-phosphate. It was shown that the enzyme retains high esterase activity (over 50%) even after two weeks of use in the incubation medium. Certain features of the substrate specificity of the carboxylesterase from the cytosolic fraction of the hepatopancreas of Rapana venosa were studied to understand its catalytic properties. The regioselectivity of the enzyme towards 1- and 2-naphthyl acetate was determined, revealing that the specific esterase activity of the enzyme for 2-naphthyl acetate is 3.6 times higher than for 1-naphthyl acetate. The hydrolytic activity of the enzyme was also tested on a series of substrates, including esters of ibuprofen and 3-hydroxy-1,4-benzodiazepin-2-one. High enantioselectivity of Rapana venosa carboxylesterase towards esters of 3-hydroxy-1,4-benzodiazepin-2-one was demonstrated. Product Description popup.authors Illiushko Nataliia О. Dekina Svitlana S. Toptikov Valentyn A. Shesterenko Yevheniia A. Shesterenko Yuliia A. popup.nrat_date 2025-01-08 Close