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Covalent bond between the enzyme amyloglucosidase and a porous glass carrier: The effect of shearing
Author(s) -
Weetall H. H.,
Havewala N. B.,
Garfinkel H. M.,
Buehl W. M.,
Baum G.
Publication year - 1974
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.260160203
Subject(s) - covalent bond , composite number , immobilized enzyme , siloxane , chemistry , shearing (physics) , adsorption , chromatography , chemical engineering , porosity , porous glass , enzyme , molecule , materials science , organic chemistry , composite material , polymer , engineering
The utility of an immobilized enzyme depends not only on initial loading but also on operational half‐life. The loss of activity of an immobilized enzyme in a column reactor may occur in several ways. It is therefore of interest to determine whether the decay in activity is due to the rupture of any of the enzyme‐carrier bonds in the composite. In order to do this, it is first necessary to establish whether the enzyme on the composite is in fact covalently bound or adsorbed. In this report we have shown that there are a number of covalent links per protein molecule. We have also shown that the bond energies are sufficient to prevent shearing of the enzyme itself from the composite under any stresses which may occur in a chromatography column or packed‐bed reactor during continuous operation. The effect of the siloxane linkage on composite stability is also discussed.