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S. Colowick, M. Joshi, Jagannathan, N. Kaplan (1966)
Methods in Enzymology , Vol
W. Hornby, H. Filippusson (1970)
The preparation of trypsin chemically attached to nylon tubes.Biochimica et biophysica acta, 220 2
A. Klibanov, G. Samokhin, K. Martínek, I. Berezin (1976)
Enzymatic mechanochemistry: a new approach to studying the mechanism of enzyme action.Biochimica et biophysica acta, 438 1
T. Chase, E. Shaw (1967)
p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin.Biochemical and biophysical research communications, 29 4
(1972)
in Critical Reviews in Macromolecular Science, vol
G. Schonbaum, B. Zerner, M. Bender (1961)
The spectrophotometric determination of the operational normality of an alpha-chymotrypsin solution.The Journal of biological chemistry, 236
L. Goldstein, A. Freeman, M. Sokolovsky (1974)
Chemically modified nylons as supports for enzyme immobilization. Polyisonitrile-nylon.The Biochemical journal, 143 3
A new mechanochemical method for enzyme immobilization has been elaborated. The principle of this method consists of the following precepts. Partially hydrolyzed nylon fiber, the surface of which is known to be strewn with micro‐cracks, is reversibly stretched (∼25%) and placed into an enzyme solution. Then, in the same solution, the fiber is made to relax and is taken out. The fiber retains considerable enzymatic activity even after numerous thorough washings (in a similar procedure without fiber stretching, equivalent washing removed all the enzymatic activity from the fiber). Immobilization on the fiber proceeds due to trapping of enzyme molecules by the microcavities on the surface of the support. The catalytic activity of mechanochemically immobilized chymotrypsin and trypsin is commensurable with their activity on covalent immobilization on nylon (calculated per unit of the macrosurface). A wide range of commercial polymers may be made of use as supports in the mechanochemical method of immobilization.
Biotechnology and Bioengineering – Wiley
Published: Feb 1, 1977
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