Immobilization as a Strategy for Improving Enzyme  Properties-Application to Oxidoreductases

Guzik, Urszula; Hupert-Kocurek, Katarzyna; Wojcieszyńska, Danuta

doi:10.3390/molecules19078995

Cited by 463 publications

(259 citation statements)

References 94 publications

(201 reference statements)

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“…Generally, free enzymes show lower thermal and operational stability, and it is also much difficult to separate the free enzyme from reaction mixture after the product formation. These constraints can be overcome by increasing the stability of the enzymes by immobilizing them within various synthetic and non synthetic matrices for continuous production of metabolites (Guzik et al 2014;Cowan and Fernandez-Lafuente 2011;Mateo et al 2007). Enzyme immobilization may provide stabilization through multipoint attachment, support in prevention of enzyme dissociation, and can generate favorable environment for enzyme-substrate reaction for the production of different biological molecules (Garcia-Galan et al 2011;Rodrigues et al 2011;Mateo et al 2007;Pedroche et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

2015

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Exploration of microbial pool from extremely diversified ecosystem is significantly important for various industrial applications. Bacterial communities from extreme habitats including volcanic vents, hot springs, and industrial sectors are eagerly explored for the isolation of thermophiles. Geobacillus stearothermophilus KIBGE-IB29, isolated from blast furnace site of a steel processing industry, is capable of producing thermostable endo-β-1,4-xylanase. In the current study, this enzyme was immobilized within calcium alginate beads using entrapment technique. Amalgamation of sodium alginate (40.0 gL(-1)) and calcium chloride (0.4 M) was used for the formation of immobilized beads. It was observed that temperature (50 °C) and pH (7.0) optima of immobilized enzyme remained same, but enzyme-substrate reaction time increased from 5.0 to 30.0 min as compared to free enzyme. Diffusion limit of high molecular weight xylan (corncob) caused a decline in V max of immobilized enzyme from 4773 to 203.7 U min(-1), whereas K m value increased from 0.5074 to 0.5722 mg ml(-1) with reference to free enzyme. Immobilized endo-β-1,4-xylanase showed its stability even at high temperatures as compared to free enzyme and retained 18 and 9 % residual activity at 70 and 80 °C, respectively. Immobilized enzyme also exhibited sufficient recycling efficiency up to five reaction cycles which indicated that this enzyme can be a plausible candidate in paper and pulp industry.

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Section: Introductionmentioning

confidence: 99%

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

2015

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“…Moreover, considering that the immobilization is in most cases a requirement to use the enzyme as an industrial biocatalyst, many researchers have endeavored to couple immobilization with the improvement of other enzyme properties , Guzik et al, 2014, Hernandez and FernandezLafuente, 2011, Hwang and Gu, 2013, Stepankova et al, 2013, Zucca and Sanjust, 2014. Multipoint (Mateo et al, 2007c) or multisubunit (in multimeric enzymes (Fernandez-Lafuente, 2009)) immobilization may improve enzyme rigidity and thus, improve enzyme stability (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

Barbosa

Ortíz

Berenguer-Murcia

et al. 2015

Biotechnology Advances

613

318

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Enzyme immobilization and purification are two steps that are usually required in the development of any industrial biocatalyst. In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies (versus the target enzyme or versus some domains), the development of specific domains with affinity for some specific supports or just to increase the affinity for standard ones (ionic exchangers, silicates) will be revised. We will show how the control of the immobilization conditions may convert some unspecific supports in largely specific ones. The development of tailormade heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbents groups and a dense layer of groups able to give an intense multipoint covalent attachment. The final coupling of mutagenesis and tailor made supports will be a the last part of the review.

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“…Additionally, immobilization of cells offers significant advantages over submerged cell suspension. Immobilization of fungal cells has been reported for production of laccase wherein immobilization methods are stated to improve the stability and half life of laccases enabling efficient biotechnological application of this enzyme [9]. However, there is a dearth of reports of Versatile peroxidase production under immobilized conditions.…”

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Versatile Peroxidases: Super Peroxidases with Potential Biotechnological Applications-A Mini Review

Ravich¹,

Sridhar²

2016

JDVAR

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Ligninolytic enzymes play a crucial role in the carbon cycle on account of their ability to degrade the macromolecule lignin. Versatile peroxidase is a high redox potential enzyme of the lignin degrading family of enzymes widely studied for its unique characteristics of degradation of aromatics without use of redox mediators and presence of polyvalent catalytic sites. These traits make them useful in diverse biotechnological and industrial applications which include textile bleaching, production of bioethanol, bioremediation of xenobiotic compounds, degradation of EDCs and in enhancing the digestibility of animal feed. In this article the features of versatile peroxidases and their potential industrial and biotechnological applications are highlighted. for production of these enzymes as they mimic the natural substrate conditions of the fungi. Significant amount of Versatile peroxidase have been produced by solid state fermentation of Pleurotus eryngii and Pleurotus Ostreatus on wheat straw, Saw dust, banana peel [7,8]. Disparately, submerged fermentation involves culturing of microorganisms in free flowing liquid substrates with high water activity. Some examples of Versatile peroxidase produced under submerged fermentation are growth of Pleurotus ostreatus, Bjerkandera in glucose-peptone broth and glucose ammonium medium [7]. Additionally, immobilization of cells offers significant advantages over submerged cell suspension. Immobilization of fungal cells has been reported for production of laccase wherein immobilization methods are stated to improve the stability and half life of laccases enabling efficient biotechnological application of this enzyme [9]. However, there is a dearth of reports of Versatile peroxidase production under immobilized conditions. Keywords: Mechanism of actionVersatile peroxidases are unique among the heme peroxidases for its polyvalent catalytic sites for oxidation of Mn 2+ , low and high molecular weight substrates [10]. The catalytic cycle of oxidation of low molecular substrates at the heme center is initiated by binding of hydrogen peroxide to the ferric state of heme forming an iron peroxide complex. This activated heme complex is a two electron deficient intermediate designated as compound I, a radical with significant oxidizing ability. Compound I is reduced to compound II, a one electron deficient compound and finally to resting form of enzyme with concomitant oxidation of two substrates [10]. While the initial reaction of compound I formation is pH independent, the latter reduction steps are pH dependent with the oxidized substrates yielding radical products which undergo several non-enzymatic reactions based on the nature of the substrate to yield final products. The non-enzymatic reactions include aromatic ring cleavage, hydroxylation, demethoxylation, ether bond cleavage, side chain cleavage and phenol formation [10]. The reaction scheme for oxidation of aromatic substrates is described in Figure 1. Interestingly, Versatile peroxidase possesses an additional manga...

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Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

Cited by 463 publications

References 94 publications

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

Versatile Peroxidases: Super Peroxidases with Potential Biotechnological Applications-A Mini Review

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