Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The production of high fructose corn syrups was greatly facilitated by the use of immobilized glucose isomerase. Similarly, in Japan, the fermentation industry proved its processing efficiency for amino acids through the use of immobilized amino acid acylase. This article discusses the use of soluble enzymes in the food industry followed by a section on the various available methods to immobilize enzymes. Once enzymes are immobilized, many of their operational parameters could be altered. Rationale for the determination of the effects of immobilization is provided. A relatively new concept is the use of a single matrix for immobilizing more than one enzyme. Immobilized multi-enzyme systems offer many attractive advantages; however, such a process also raises some interesting questions about kinetics. These questions and their suggested answers are discussed in the penultimate section. The major emphasis of this article is on the use of immobilized enzymes in the food industry. Two systems--amino acylase and glucose isomerase--have been demonstrated to be techno-economically feasible. Immobilization of other enzymes, such as glucoamylase, lactase, protease, and flavor modifying enzymes, has received some attention. The potential of these new systems are also discussed.
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PMID:The use of immobilized enzymes in the food industry: a review. 11 2

A series of water-soluble disubstituted carbodiimides of different structure was tested for enzyme immobilization. In the experiments, a polyacrylamide-type bead polymer possessing carboxylic functional groups was used as support. The enzymes immobilized were aminoacylase (N-acylamino acid amidohydrolase; EC 3.5.1.14), arginase (L-arginine amidinohydrolase; EC 3.5.3.1), cyclodextrin glycosyltransferase (alpha-1,4-glucan 4-glycosyltransferase, cyclizing; EC 3.2.1.19), glucoamylase (1,4-alpha-D-glucan glycohydrolase, EC 3.2.1.3), and carboxypeptidase B (peptidyl-L-lysine [L-arginine] hydrolase; EC 3.4.17.2). It was found that the degree of immobilization strongly depended on the structure of carbodiimide used.
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PMID:Effects of carbodiimide structure on the immobilization of enzymes. 195 34

Two natural glycoproteins/glycoenzymes, invertase and glucoamylase, and two neoglycoconjugates, synthetized from Saccharomyces cerevisiae mannan, bovine serum albumin and penicillin G acylase were tested for interaction with lectin Concanavalin A (Con A). The interaction of natural and synthetic glycoproteins with Con A was studied using three different experimental methods: (i). quantitative precipitation in solution (ii). sorption to Con A immobilized on bead cellulose; and (iii). kinetic measurement of the interaction by surface plasmon resonance. Prepared neoglycoproteins were further characterized: saccharide content, molecular weight, polydispersion, kinetic and equilibrium association constants with Con A were determined. It can be concluded that the used conjugation method proved to be able to produce neoglycoproteins with similar properties like natural glycoproteins, i.e. enzymatic activity (protein part) and lectin binding activity (mannan part) were preserved and the neoglycoconjugates interact with Con A similarly as natural mannan-type glycoproteins.
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PMID:Influence of mannan epitopes in glycoproteins--Concanavalin A interaction. Comparison of natural and synthetic glycosylated proteins. 1229 32

The properties of a new commercially available amino-epoxy support (amino-epoxy-Sepabeads) for immobilizing enzymes have been compared to those of conventional epoxy supports. The new support has a layer of epoxy groups over a layer of ethylenediamine that is covalently bound to the support. Thus, this support has a great anionic exchanger power and a high number of epoxy groups. We have found a number of advantages to this new heterofunctional support. Immobilization proceeds at low ionic strength using amino epoxy Sepabeads while requiring high ionic strength using conventional monofunctional epoxy supports. Immobilization is much more rapid using amino-epoxy supports than employing conventional epoxy supports. The possibility of achieving immobilized preparations in which the enzyme orientation may be different to that obtained using the traditional hydrophobic supports (with likely effects in terms of activity or stability). Stability of the immobilized enzyme has been found to be much higher using the new support than in preparations using the conventional ones in many cases. Here we show some examples of these advantages using different enzymes (beta-galactosidases, lipase, glutaryl acylase, invertase, and glucoamylase).
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PMID:Epoxy-amino groups: a new tool for improved immobilization of proteins by the epoxy method. 1274 97