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The effect of methylacrylate on the activity of glucomylase immobilized on granular polyacrylonitrile
Author(s) -
Handa Takashi,
Hirose Akira,
Yoshida Shoji,
Tsuchiya Haruo
Publication year - 1982
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260240715
Subject(s) - polyacrylonitrile , chemistry , chemical engineering , polymer science , organic chemistry , polymer , engineering
Abstract Glucoamylase was immobilized on granular polyacrylonitrile (PAN) and the optimum condition in its immobilization reaction was determined. The effect of the ratio of the imidoester and methylester to the total cyanogen on the activity of the immobilized enzyme was studied. The activity of the immobilized enzyme increased in proportion to the molar number of imidoester and decreased with that of methylester. The K m and V m values of immobilized glucoamylase which were prepared at various conditions of immobilization were determined. There were opposite trends in K m S between glucoamylase immobilized on imidoester‐rich support and immobilized on methylester in the support, evidenced as functions of temperature. This suggests that opposite charges in the support, produced by heat deformation of PAN by hydrolysis of methylester, were an influence on the apparent K m of immobilized glucoamylase, besides the diffusional limitation.