Open AccessPurification and investigation of physico-chemical properties of β-glucanase
Author(s) -
Alexey N. Yakovlev,
S. F. Yakovleva,
Г. В. Агафонов,
T. I. Romanyuk,
Н. В. Зуева
Publication year - 2020
Publication title -
iop conference series. earth and environmental science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.179
H-Index - 26
eISSN - 1755-1307
pISSN - 1755-1315
DOI - 10.1088/1755-1315/421/2/022057
Subject(s) - hydrolysis , chemistry , size exclusion chromatography , sephadex , starch , chromatography , polysaccharide , glucanase , thermal stability , cellulose , enzyme , ethanol precipitation , ion chromatography , ethanol , ion exchange , biochemistry , organic chemistry , ion
From the complex enzyme preparation Bruzaime BGX, β-glucanase enzyme with a specific activity of 369.5 units/mg of protein and a degree of purification of 57.7 was isolated by ethanol precipitation and purified by gel filtration on Sephadex G-25 and G-150 and ion-exchange chromatography on DEAE - cellulose. The influence of temperature and pH on the activity and stability of the enzyme was studied in the temperature range 30–70°C and pH 4.0–7.0. It was found that the optimum effect of β-glucanase corresponds to pH 4.8 and a temperature of 56°C, the enzyme has a sufficiently high thermal and acid stability, hydrolyzes non-starch polysaccharides containing both β- 1,3 and β- 1,4 - glucosidic bonds, which makes its use in biotechnology promising for the hydrolysis of non-starch polysaccharides of grain.