Covalent bond between the enzyme amyloglucosidase and a porous glass carrier: The effect of shearing
- 1 February 1974
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 16 (2) , 169-179
- https://doi.org/10.1002/bit.260160203
Abstract
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.Keywords
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