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Use of hexadecyl fractosil as a hydrophobic carrier for adsorptive immobilization of proteins
Author(s) -
NematGorgani Mohsen,
Karimian Khashayar
Publication year - 1986
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.260280714
Subject(s) - chemistry , hydrophobic effect , bovine serum albumin , allosteric regulation , glutamate dehydrogenase , chymotrypsin , trypsin , immobilized enzyme , chromatography , combinatorial chemistry , biochemistry , organic chemistry , biophysics , enzyme , glutamate receptor , receptor , biology
Fractosil, a porous form of silica, has been used for the preparation of a hydrophobically derivatized carrier for protein immobilization. Interaction of a number of arbitrarily chosen proteins with hexadecyl‐substituted Fractosil has been investigated. Binding of proteins was found to take place with retention of their native properties. Glutamate dehydrogenase, used as a model allosteric protein, was found to retain its catalytic and allosteric properties upon binding to the adsorbent in the form of suspension or column. Positive cooperative interactions for binding of bovine serum albumin and glutamate dehydrogenase to the matrix were observed. These findings are discussed in terms of hydrophobic interactions occurring between various residues of the protein molecules and the hydrophobic ligands in addition to those interactions which may occur with the unsubstituted gel. Results presented on immobilized glutamate dehydrogenase, trypsin, α‐chymotrypsin, α‐amylase, and amyloglucosidase clearly indicate possible potential of the support for continuous catalytic transformations.