Bacillus subtilis is a widely distributed aerobic Gram-positive species of bacteria. As a tool in the lab, it has the advantages of nonpathogenicity and limited likelihood of becoming drug resistant. It is a probiotic strain that can be directly used in humans and animals. It can be induced to produce spores under nutrient deficiency or other adverse conditions. B. subtilis spores have unique physical, chemical, and biochemical characteristics. Expression of heterologous antigens or proteins on the surface of B. subtilis spores has been successfully performed for over a decade. As an update and supplement to previously published research, this paper reviews the latest research on spore surface display technology using B. subtilis. We have mainly focused on the regulation of spore coat protein expression, display and application of exogenous proteins, and identification of developing research areas of spore surface display technology.
The effect of structural modifications on the enzyme-binding capacity of collagen has been studied using p-galactosidase (E. coli K, *) 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 @-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.
Immobilization procedureCollagen-lactase complexes were prepared by the interdiffusional
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