1,720,991 research outputs found
Purification of aspartate aminotransferase from cardiac muscle of the sword-fish (Xiphias gladius L.)
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Mechanical stability and diffusional resistance of a polymeric gel used for biocatalyst immobilization
No full textThe 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, κ-carrageenan, alginate, and gelatin immobilizates was compared under the same conditions of cell loading. 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, k-carrageenan, alginate, and gelatin immobilizations was compared under the same conditions of cell loading
"Thermodynamic analysis of the stability enhancement of acid phosphatase by gel immobilization in proteins"
No full textEffect of temperature and shear on the activity of acid-phosphatase in a membrane reactor
No full textEnzyme stability and glucose inhibition in cellulose saccharification
No full textPure cellulose as well as cellulosic wastes can be hydrolyzed by an enzyme complex generally named cellulase, of which two main sources are known, the microfungi Trichoderma viride and Aspergillus niger. The complex exhibits three major activities: an endo- and an exo-glucanase (C//1 and C//x) synergistically acting in the breakdown of both crystalline and amorphous regions of the cellulose chain, and a third component, beta -glucosidase, which catalyzes the hydrolysis of cellobiose to glucose. At present, however, various constraints still limit the enzymatic saccharification of cellulose. In the present study, our attention has been focused on thermal stability and on glucose inhibition
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