Mechanical stability and diffusional resistance of a polymeric gel used for biocatalyst immobilization.
The mechanical strength of gelatin gels insolubilized by crosslinking with formaldehyde was measured at various gelatin percentages and formaldehyde-to-gelatin ratios. This property was shown to be related to the characteristic sponge-like structure of the insolubilized gelatin gel, a structure that unexpectedly is also responsible for the resistance to substrate and product diffusion. A comparison between immobilizates of invertase and invertase-active yeast cells prepared with different gelatin concentrations showed that the enzyme, in contrast to cells, is deeply involved in the gel insolubilization process. The catalytic behavior of agar, kappa-carrageenan, alginate, and gelatin immobilizates was compared under the same conditions of cell loading.
Dipartimento di Fisiologia Generale e Ambientale, Università di Napoli, Italy.
E
E
de Alteriis
V
V
Scardi
P
P
Masi
P
P
Parascandola
D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005557:Formaldehyde; D005780:Gelatin; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007700:Kinetics; D008855:Microscopy, Electron, Scanning; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D043324:beta-Fructofuranosidase
D004800:Enzymes, Immobilized; D005557:Formaldehyde; D005780:Gelatin; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase