ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The effect of structural modifications on the enzyme-binding capacity of collagen has been studied using p-galactosidase (E. coli K1 2) immobilized to collagen membranes. The immobilization process employs simple and inexpensive techniques to bind the enzyme to collagen through direct protein-protein interaction. The tertiary structure of the collagen matrix was modified by cross-linking with the difunctional reagent, glutaraldehyde, or by a natural cross-linking process associated with aging. Such modifications were found to markedly reduce the enzyme (β-galactosidase)-binding capacity of collagen films. The deleterious effect of cross-linking on the binding capacity of collagen was shown to be completely reversed by proteolytic enzyme treatment of aged films but only partly so for glutaraldehyde-treated films.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1976.tb14388.x
