The molecular mechanism of adsorption immobilization of inulinase on polymer matrices


Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Тек жазылушылар үшін

Аннотация

The conditions and mechanisms of the immobilization of inulinase on polymeric carriers were studied using the VION KN-1 and KU-2 cation-exchangers, VION AN-1 and AV-17-2P anion-exchangers, and the ampholyte KOPAN-90. The calculated data showed a significant role of van der Waals interactions and hydrogen bonding in the formation of virtually all inulinase complexes with the immobilization matrices. The AV-17-2P anion-exchanger was the only one of the studied polymer matrices that was unable to form hydrogen bonds with inulinase. The mechanisms of the interaction between inulinase and various ampholytes and cation and anion exchange resins differ from each other. The strongest differences are observed in mechanisms of the sorption of inulinase on VION KN-1 and chitosan matrices. Approximately 87% of the identical amino-acid residues are involved in the interaction of the enzyme with the KU-2 and AV-17-2P resins and the VION AN-1 and KOPAN-90 fibers.

Авторлар туралы

M. Holyavka

Voronezh State University

Хат алмасуға жауапты Автор.
Email: holyavka@rambler.ru
Ресей, Voronezh, 394018

M. Kondratyev

Institute of Cell Biophysics

Email: holyavka@rambler.ru
Ресей, Pushchino, Moscow Region, 142290

V. Terentyev

Institute of Basic Biological Problems

Email: holyavka@rambler.ru
Ресей, Pushchino, Moscow Region, 142290

A. Samchenko

Institute of Cell Biophysics

Email: holyavka@rambler.ru
Ресей, Pushchino, Moscow Region, 142290

A. Kabanov

Institute of Cell Biophysics

Email: holyavka@rambler.ru
Ресей, Pushchino, Moscow Region, 142290

V. Komarov

Institute of Cell Biophysics

Email: holyavka@rambler.ru
Ресей, Pushchino, Moscow Region, 142290

V. Artyukhov

Voronezh State University

Email: holyavka@rambler.ru
Ресей, Voronezh, 394018

Қосымша файлдар

Қосымша файлдар
Әрекет
1. JATS XML

© Pleiades Publishing, Inc., 2017