Search academic texts

Information × Registration Number 0224U000120, 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 Head Romanovska Iryna І., Доктор біологічних наук Registration Date 02-01-2024 Organization Physico-Chemical Institute O. Bogatsky National Academy of Sciences of Ukraine popup.description2  The object of research is the cytosolic carboxylesterase from Rapana venosa hepatopancreas. The aim of the work is to develop a method of obtaining highly active carboxylesterase from hepatopancreas of the mollusk Rapana venosa with a high degree of purity to study its biochemical and physicochemical properties. The method of isolation of carboxylesterase from the cytosolic fraction of the hepatopancreas Rapana venosa was developed. This allows to obtain an enzyme with high esterase activity (579 nmol/mg of protein per min by 1-naphthyl acetate), which exceeds the activity of the homogenate by 24 times. Electrophoretic studies were carried out, and a high degree of enzyme purity was shown. The molecular mass (57.2 kDa) of carboxylesterase from the cytosolic fraction of Rapana venosa hepatopancreas was established for the first time. Complete inhibition of enzyme activity by di-(p-nitrophenyl)-phosphate confirmed the belonging of the obtained carboxylesterase to carboxylesterase family. It was shown that the pH and temperature optimum were 5.5 and 45 ºС, respectively; high preservation of esterase activity is observed at pH 5.5-9.0 and 40-50 ºС. Extremely high stability of the obtained carboxylesterase at acidic pH values was shown. After 8 days of incubation at pH 5.5, 37 °C, more than 90 % of the initial esterase activity was retained. It makes the obtained enzyme a promising biocatalyst that can be used in enantioselective hydrolysis reactions for a long time. Regioselectivity of carboxylesterase from Rapana venosa to 1- and 2-naphthyl acetate was studied. The specific esterase activity of the enzyme for 2-naphthyl acetate was 3.6 times higher than for 1-naphthyl acetate. Product Description popup.authors Illyushko Natalia О. Dekina Svitlana S. Kremer Viktoriya V. Romanovska Iryna I. Toptykov Valentin Anatoliyovych Shesterenko Yevheniya A. Shesterenko Yuliia A. popup.nrat_date 2024-01-02 Close