Properties of free and immobilized glucose isomerase

Giovenco, S.; Morisi, F.; Pansolli, P.

doi:10.1016/0014-5793(73)80336-9

Cited by 33 publications

(8 citation statements)

References 8 publications

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“…Only about 15% was measured after entrapment in polyacrylamide (Strandberg and Smiley, 1971), but much of the apparent activity loss in this case might have been due to diffusional influences. As already pointed out, Giovenco, et al, (1973) claimed that no isomerase activity was lost upon immobilization in spun cellulose triacetate fibers, but only 60% of the activity was measured, probably because of diffusional limitations. As also already mentioned, Takasaki, et al (1969b) claimed that 80-90% of the total glucose isomera;e present in a cell culture could be cellfixed.…”

Section: 4mentioning

confidence: 95%

“…The fall of activity with batch number in this case is comparable to that observed by Sipos (1973) immobilized on DEAE-cellulose ( Figure 5). When evaluating these two methods of stabilization (cell-free immobilized isomerase vs. cell-fixed isomerase) it should be kept in mind that Takasaki, et al claimed that 80-90% of the total glucose isomerase present in a-cell culture could be cell-fixed, while the corresponding figure for immobilization procedures typically appears to be lower than 40% (Sipos, 1973;Havewala and Pitcher, 1974;Smiley, 1971, 1972), although Giovenco, et al (1973) claimed that no isomerase activity was lost upon-rmmobilization in spun cellulose triacetate fibers.…”

Section: Enzyme-catalyzed Reactionmentioning

confidence: 97%

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Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Hamilton

Colton

Cooney

1974

Immobilized Enzymes in Food and Microbial Processes

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Process engineering considerations important in the exploitation of enzyme-catalyzed reactions for large-scale production of desired products are illustrated in the context of a case study of glucose isomerase technology. The state of the art of glucose isomerase processing as revealed by journal and patent literature is reviewed and assessed. Among topics covered are enzyme production, immobilization and stabilization, kinetics, reactor design, and product recovery. Some possible future processing objectives, such as production of pure fructose, are discussed.

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Section: 4mentioning

confidence: 95%

Section: Enzyme-catalyzed Reactionmentioning

confidence: 97%

Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Hamilton

Colton

Cooney

1974

Immobilized Enzymes in Food and Microbial Processes

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“…Despite the low purification factor (4-5 times) the specific activity after DEAE-Sephadex chromatography was relatively high compared with preparations obtained from Streptomyces phaeochromogenes, Lactobacillus brevis, Bacillus coagulans, lo and Streptomyces griseolus . 4 …”

Section: Purification Of Glucose Isomerasementioning

confidence: 97%

Immobilization of glucose isomerase to ion‐exchange materials

Huitrón

Limón-Lason

1978

Biotech & Bioengineering

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SummaryGlucose isomerase (D-XylOSe ketol-isomerase EC 5.3. I . 5 ) from Bacillus coagu~ans was partially purified and immobilized by adsorption to anion exchangers. The highest activities were obtained when the enzyme was adsorbed to DEAE-cellulose. On immobilization to DEAE-cellulose the measured optimum pH value for enzyme activity shifted from 7.2 to 6.8. There was no appreciable difference between the heat stabilities of soluble and immobilized enzyme. The K , Bpp values for the immobilized enzyme were found to be 0.25M in the presence of 0.01M Mg2+ and 0.19M with O.OO5M Mg2+, while those for the soluble enzyme were 0.11 and 0.17M, respectively. Under conditions of continuous isomerization of D-glucose, a decrease of activity with time was observed, but this decrease was less at a low Mg2+ concentration and was affected by column geometry. There were no appreciable diffusional limitation effects in packed-bed columns.

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“…GI producing organisms generally require Co 2+ to stimulate the formation of GI (Giovenco and Morisi 1973). Our study indicated that GI production by Aspergillus sp is independent of Co 2+ supplementation.…”

Section: Influence Of Carbon Sourcementioning

confidence: 62%

Constitutive production of extracellular glucose isomerase by an osmophillic Aspergillus sp. under submerged conditions

2010

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We report constitutive production of glucose isomerase (GI) under submerged growth of Aspergillus sp. in glucose phosphate broth (GPB). The fungus produced significant quantities of extracellular GI in GPB without supplementing the inducer (xylose). The maximum biomass (872 mg) and highest level of GI (1126 U) were obtained in 42 h at 30°C and 120 rpm. Equal level of biomass and enzyme were produced in GPB with glucose and xylose, but

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Properties of free and immobilized glucose isomerase

Cited by 33 publications

References 8 publications

Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Immobilization of glucose isomerase to ion‐exchange materials

Constitutive production of extracellular glucose isomerase by an osmophillic Aspergillus sp. under submerged conditions

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