1981
DOI: 10.1007/bf02906194
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Entrapment of chemical derivatives of glycoamylase in calcium alginate gels

Abstract: Glucoamylase was retained in calcium alginate gels, when the molecular weight of the enzyme was increased, e.g., by attachment to polymeric supports or by intermolecular cross-linking. Alternatively, the enzyme could be retained by covalent attachment to the alginate matrix. In the majority of the glucoamylase derivatives more than 50 % of the initial activity determined with maltose or partially hydrolyzed starch as substrate was recovered, while upon entrapment in gel particles, less than 40 % and 6 % of the… Show more

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Cited by 16 publications
(5 citation statements)
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“…where the qn's are the non-zero roots of (2) expressed in terms of the final fractional uptake of solute by the bead, as follows:…”
Section: Swelling Of Dried Gel Particlesmentioning
confidence: 99%
“…where the qn's are the non-zero roots of (2) expressed in terms of the final fractional uptake of solute by the bead, as follows:…”
Section: Swelling Of Dried Gel Particlesmentioning
confidence: 99%
“…[2] For this purposes, enzymes have been immobilized onto solid supports materials, in order to improve the reusability properties of enzymes. [3] There have been intensive works to immobilize amyloglucosidase onto various matrices by using different methods such as, adsorption onto magnetic polystyrene beads [4], activated charcoal [2], macrostructured carbonized ceramics [5] and nonporous polystyrene/poly(sodium styrene sulfonate) microspheres [6]; covalent binding to polyglutaraldehyde-activated gelatin [7], macroporous poly(GMA-co-EGDMA) [3], magnetic nanoparticles [8]; and entrapment in alginate [9] and LentiKats®. [10] Enzymes have superior properties for industrial applications such as; they can catalyze the reactions under mild conditions with very high activity, also they have high enantio-and regio-selectivity and specificity towards their substrates.…”
Section: Introductionmentioning
confidence: 99%
“…Hagerdal & Mosbach (1981) covalently bound P-glucosidase to alginate, then entrapped the modified enzyme and yeast cells in calcium alginate to produce ethanol from cellobiose. Similarly Svensson & Ottesen (1981) increased the molecular size of glucoamylase by coupling it to soluble dextran before coimmobilizing it in alginate with yeast cells.…”
Section: Immobilized Cells As Sources O F Multi-enzyme Systems (A) Ethanol Productionmentioning
confidence: 99%