Enhancement of glucose isomerase activity by pretreatment with substrates prior to immobilization

Yue, Song; Kim, Ji Eun; Park, Chulhwan; Kim, Seung Wook

doi:10.1007/s11814-010-0464-4

Cited by 12 publications

(4 citation statements)

References 20 publications

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“…For example, Song and coworkers immobilized S. rubiginosus GI on aminopropylsilane-activated silica gel using glutaraldehyde as a cross-linking agent, resulting in multipoint covalent attachment of the enzyme to the support. 79 The enzyme was immobilized with and without substrate pretreatment, using both D-xylose and D-glucose. After optimizing the pretreatment conditions with regard to time, temperature and agitation, the authors reported that pretreated immobilized GI (PIGI) displayed 2.5 fold higher activity relative to non-pretreated IGI.…”

Section: Methods For Gi Immobilizationmentioning

confidence: 99%

Industrial use of immobilized enzymes

et al. 2013

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Although many methods for enzyme immobilization have been described in patents and publications, relatively few processes employing immobilized enzymes have been successfully commercialized. The cost of most industrial enzymes is often only a minor component in overall process economics, and in these instances, the additional costs associated with enzyme immobilization are often not justified. More commonly the benefit realized from enzyme immobilization relates to the process advantages that an immobilized catalyst offers, for example, enabling continuous production, improved stability and the absence of the biocatalyst in the product stream. The development and attributes of several established and emerging industrial applications for immobilized enzymes, including high-fructose corn syrup production, pectin hydrolysis, debittering of fruit juices, interesterification of food fats and oils, biodiesel production, and carbon dioxide capture are reviewed herein, highlighting factors that define the advantages of enzyme immobilization.

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Section: Methods For Gi Immobilizationmentioning

confidence: 99%

Industrial use of immobilized enzymes

et al. 2013

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“…However, major drawbacks of the process are inactivation of GI at higher temperatures (above 60 °C), narrow pH operation window, inhibition of GI in the presence of Ca 2+ ions (prerequisite for the action of amylase when liquefaction, saccharification, and isomerization are carried out simultaneously), requirement of Co 2+ ions for enzyme activity, and suboptimal concentrations of the product . Notably, the combination of divalent metal ions (e.g., Co, Mn, Mg, and Fe) with the amino-acid compositions of GI (e.g., histidine) can contribute to the improvements in terms of both activity and stability of the enzymes. − The immobilization of GI with porous materials (e.g., silica/chitosan hybrid microspheres) can somewhat extend the narrow range of pH (5.8–8.0) and temperature (40–80 °C), but still not widely enough. − For these reasons, the enzyme efficiency is still low from an economic point of view, and a large quantity of enzyme is thus needed to obtain viable throughputs. , To overcome these drawbacks, a suitable chemo-catalytic system is thus desirable and the later sections discuss both homogeneous and heterogeneous catalyzed isomerization.…”

Section: Biocatalytic Processesmentioning

confidence: 99%

Glucose Isomerization by Enzymes and Chemo-catalysts: Status and Current Advances

et al. 2017

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The well-known interconversion of aldoses to their corresponding ketoses was discovered more than a century ago, but has recently attracted renewed attention due to alternative application areas. Since the pioneering discovery, much work has been directed toward improving the process of isomerization of aldoses in terms of yields, catalysts, solvents, catalytic systems, etc., by both enzymatic and chemo-catalytic approaches. Among aldose–ketose interconversion reactions, fructose production by glucose isomerization to make high-fructose corn syrup (HFCS) is an industrially important and large biocatalytic process today, and a large number of studies have been reported on the process development. In parallel, also alternative chemo-catalytic systems have emerged, as enzymatic conversion has drawbacks, though they are typically more selective and produce fructose under mild reaction conditions. Isomerization of glucose is also a central reaction for making renewable platform chemicals, such as lactic acid, 5-hydroxymethylfurfural (HMF), and levulinic acid. In these other applications, thermally stable catalysts are required, thus making use of enzymatic catalysis inadequate, since enzymes generally possess a limited temperature operating window, typically less than 80 °C. From this viewpoint, the chemo-catalystsespecially solid heterogeneous catalystsare playing a key role for the development of not only making HFCS, but also making chemicals and fuels from glucose via the isomerized product/intermediate fructose. This review focuses on how both enzyme- and chemo-catalysts are being useful for the isomerization of glucose to fructose. Specifically, development of Lewis acid-containing zeolites for glucose isomerization is reviewed in detail, including mechanism, isotopic labeling, and computational studies.

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“…21 Therefore, we attribute increased apparent activity to reduced intrafiber diffusion due to surface enrichment of the enzyme during processing. We also considered additives 56 such as glycerol trehalose, known to improve protein stability, as well as a substrate, 57,58 raffinose, to protect the enzyme from deactivation during immobilization. Using concentrations comparable to these previous studies, the addition of 1 M glycerol in the electrospinning solution resulted in an approximate 2-fold increase in apparent activity when compared to α-gal immobilized in the absence of any additive (Figure 6) similar to previous reports.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

Cross-linked Polymer Nanofibers for Hyperthermophilic Enzyme Immobilization: Approaches to Improve Enzyme Performance

Tang

Saquing

Morton

et al. 2014

ACS Appl. Mater. Interfaces

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We report an enzyme immobilization method effective at elevated temperatures (up to 105 °C) and sufficiently robust for hyperthermophilic enzymes. Using a model hyperthermophilic enzyme, α-galactosidase from Thermotoga maritima, immobilization within chemically cross-linked poly(vinyl alcohol) (PVA) nanofibers to provide high specific surface area is achieved by (1) electrospinning a blend of a PVA and enzyme and (2) chemically cross-linking the polymer to entrap the enzyme within a water insoluble PVA fiber. The resulting enzyme-loaded nanofibers are water-insoluble at elevated temperatures, and enzyme leaching is not observed, indicating that the cross-linking effectively immobilizes the enzyme within the fibers. Upon immobilization, the enzyme retains its hyperthermophilic nature and shows improved thermal stability indicated by a 5.5-fold increase in apparent half-life at 90 °C, but with a significant decrease in apparent activity. The loss in apparent activity is attributed to enzyme deactivation and mass transfer limitations. Improvements in the apparent activity can be achieved by incorporating a cryoprotectant during immobilization to prevent enzyme deactivation. For example, immobilization in the presence of trehalose improved the apparent activity by 10-fold. Minimizing the mat thickness to reduce interfiber diffusion was a simple and effective method to further improve the performance of the immobilized enzyme.

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Enhancement of glucose isomerase activity by pretreatment with substrates prior to immobilization

Cited by 12 publications

References 20 publications

Industrial use of immobilized enzymes

Industrial use of immobilized enzymes

Glucose Isomerization by Enzymes and Chemo-catalysts: Status and Current Advances

Cross-linked Polymer Nanofibers for Hyperthermophilic Enzyme Immobilization: Approaches to Improve Enzyme Performance

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