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Sugars immobilized

Because enzymes can be intraceUularly associated with cell membranes, whole microbial cells, viable or nonviable, can be used to exploit the activity of one or more types of enzyme and cofactor regeneration, eg, alcohol production from sugar with yeast cells. Viable cells may be further stabilized by entrapment in aqueous gel beads or attached to the surface of spherical particles. Otherwise cells are usually homogenized and cross-linked with glutaraldehyde [111-30-8] to form an insoluble yet penetrable matrix. This is the method upon which the principal industrial appHcations of immobilized enzymes is based. [Pg.291]

The success of IGI was a result of high quaHty immobilized preparations developed at a time when raw sugar was expensive (1975). When the technology was estabHshed and further improved, it remained competitive when raw sugar prices dropped. [Pg.291]

Figure 3.13 shows the thermal stability of immobilized ODN and PNA. The signal for the Thy- and Cyt-bases obtained with temperature-programmed (TP) SIMS starts to decrease at approximately 150 °C for ODN and 200 °C for PNA. This variance is caused by the different strengths of binding between the bases and the sugar-phosphate and peptide backbones, respectively. [Pg.101]

Enzyme activity for the polymerization of lactones was improved by the immobilization on Celite [93]. Immobilized lipase PF adsorbed on a Celite showed much higher catalytic activity than that before the immobilization. The catalytic activity was further enhanced by the addition of a sugar or poly(ethylene glycol) in the immobilization. Surfactant-coated lipase efficiently polymerized the ring-opening polymerization of lactones in organic solvents [94]. [Pg.250]

B. Mukhopadhyay, Sulfuric acid immobilized on silica An efficient promoter for one-pot acetalation-acetylation of sugar derivatives, Tetrahedron Lett., 47 (2006) 4337-4341. [Pg.94]

Guimaraes C, Porto P, Oliveira R, Mota M (2005) Continuous decolourization of a sugar refinery wastewater in a modified rotating biological contactor with phanerochaete chrysos-porium immobilized on polyurethane foam disks. Process Biochem 40 535-540... [Pg.38]

Table 6.4 Some lectins commonly used in immobilized format for the purification of glycoproteins. The sugar specificity is listed, as are the free sugars used to elute the bound glycoprotein... Table 6.4 Some lectins commonly used in immobilized format for the purification of glycoproteins. The sugar specificity is listed, as are the free sugars used to elute the bound glycoprotein...
Fig. 2 Determination of Bt values (amount of functional immobilized ligand in the column) for the immobilized Erythrina cristagalli agglutinin. / -Nitrophenyl, (pNP)-lactose, diluted to various concentrations (8 to 50 pM), was used for concentration-dependence analysis. (A) The solid and dotted lines demonstrate elution profiles of pNP-lactose and control sugar (pNP-mannose), respectively. (B) Woolf-Hofstee-type plot was made by using V-V0 values. Adapted from 47 with permission. Fig. 2 Determination of Bt values (amount of functional immobilized ligand in the column) for the immobilized Erythrina cristagalli agglutinin. / -Nitrophenyl, (pNP)-lactose, diluted to various concentrations (8 to 50 pM), was used for concentration-dependence analysis. (A) The solid and dotted lines demonstrate elution profiles of pNP-lactose and control sugar (pNP-mannose), respectively. (B) Woolf-Hofstee-type plot was made by using V-V0 values. Adapted from 47 with permission.
Scheme 7.7 Immobilization of a thiol-group containing sugar substrate on a hexavalent PEC-derivative for sulfatation and enzymatic glycosylation reactions. Scheme 7.7 Immobilization of a thiol-group containing sugar substrate on a hexavalent PEC-derivative for sulfatation and enzymatic glycosylation reactions.
Cost sensitivity studies have shown that the successful commercialization of cellulase-based processes, such as the conversion of cellulose to fermentable sugars, is highly dependent on the cost of enzyme production (i). Because fungal -D-glucosidase (EC 3.2.1.21) is the most labile enzyme in this system under process conditions (2), and k to efficient saccharification of cellulose, this enzyme was targeted for application of stabilization technology, both through chemical modification and immobilization to solid supports. [Pg.137]


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See also in sourсe #XX -- [ Pg.847 ]




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