ANALISIS OF EQUILIBRIUM CONSTANT OF THE INULINASE BY USING DATA OF PARTICLE DISTRIBUTION IN GROUP
Authors:
1.
Voronezh State University
2.
Sevastopol State University
Type:
Article
Pages:
from 185
to 189
Status:
Published
Received:
20.06.2017
Accepted:
20.06.2017
Published:
25.06.2017
Subject area:
UDK 577 Материальные основы жизни. Биохимия. Молекулярная биология.Биофизика
Language:
Russian
Keywords:
inulinase, monomer, dimer
Abstract (English):
By using dynamic light scattering method was studded formation of supramolecular complexes with the enzyme inulinase. Obtained values of the radii of the particles inulinase in the fluid, value of the constant of dimerization. The equilibrium constant of aggregation of the inulinase satisfy to monomer and dimer state of the particles The conclusion about the feasibility of the obtained data in the framework of the simplest model of equilibrium monomer↔dimer. The value of the constants of dimerization for inulinase, satisfy to the typical values of the aggregation constants of medium molecular proteins and can be considered reliable.
By using dynamic light scattering method was studded formation of supramolecular complexes with the enzyme inulinase. Obtained values of the radii of the particles inulinase in the fluid, value of the constant of dimerization. The equilibrium constant of aggregation of the inulinase satisfy to monomer and dimer state of the particles The conclusion about the feasibility of the obtained data in the framework of the simplest model of equilibrium monomer↔dimer. The value of the constants of dimerization for inulinase, satisfy to the typical values of the aggregation constants of medium molecular proteins and can be considered reliable.
Keywords:
inulinase, monomer, dimer
inulinase, monomer, dimer
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