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Durieux, Alain; Nicolay, Xavier; Simon, Jean-Paul

doi:10.1023/a:1005667611732

Cited by 47 publications

(10 citation statements)

References 12 publications

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“…[46] A mild and highly efficient method for preparing PVA hydrogels by partial drying at room temperature afforded lens-shaped hydrogels (Lentikats) exhibiting good mechanical stability, easy separation (diameter 3-5 mm and thickness 200-400 mm) and stability towards degradation. [47] Lentikats have been successfully used for the entrapment of whole cell biocatalysts, [48,49] for example, in the immobilization of whole cells of Rhodococcus equi A4, which contains nitrile hydratase and amidase activities. [49] However, free enzymes, owing to their smaller size, can diffuse out of the gel matrix and are, consequently, leached in an aqueous medium.…”

Section: Hydrogelsmentioning

confidence: 99%

Enzyme Immobilization: The Quest for Optimum Performance

2007

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Immobilization is often the key to optimizing the operational performance of an enzyme in industrial processes, particularly for use in non-aqueous media. Different methods for the immobilization of enzymes are critically reviewed. The methods are divided into three main categories, viz. (i) binding to a prefabricated support (carrier), (ii) entrapment in organic or inorganic polymer matrices, and (iii) cross-linking of enzyme molecules. Emphasis is placed on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross-linked enzyme aggregates (CLEAs).

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Section: Hydrogelsmentioning

confidence: 99%

Enzyme Immobilization: The Quest for Optimum Performance

2007

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“…This approach has been applied both on bacteria and yeast cells. The capability of cells to grow within the PVA matrix during the propagation cycles was proven on Oenococcus oeni in a work focused on the improvement of the malolactic fermentation of cider (Durieux et al 2000). Rebroš et al (2005) applied Zymomonas mobilis cells entrapped in LentiKats® (0.36 g biomass /L PVA ) for batch and continuous ethanol production.…”

Section: Voulgarismentioning

confidence: 99%

“…PVA hydrogel is an advantageous matrix, being cheap, biologically inert and non-toxic, with excellent physical and mechanical long-term stability ). LentiKats® biocatalysts have so far been used in the pharmaceutical industry, food processing industries, distilleries and wastewater treatment (Boušková et al 2011;Durieux et al 2000;Rebroš et al 2009;www.lentikats.eu). The ratio of particles' diameter (3-4 mm) vs. their thickness (250-400 μm) makes LentiKats® very amenable for separation from the reaction mixture and recycling, provides high concentration of biomass, avoids diffusion limitations and allows easy penetration of substrate into and product out of the matrix.…”

Section: Introductionmentioning

confidence: 99%

Immobilised whole-cell recombinant monoamine oxidase biocatalysis

Zajkoska

Rosenberg

Heath

et al. 2014

Appl Microbiol Biotechnol

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This work demonstrates the first example of the immobilisation of MAO-N whole cells to produce a biocatalyst that remained suitable for repetitive use after 11 months of storage and stable up to 15 months after immobilisation. The production of Escherichia coli expressing recombinant MAO-N was scaled up to bioreactors under regulated, previously optimised conditions (10% DO, pH 7), and the amount of biomass was almost doubled compared to flask cultivation. Subsequently, pilot immobilisation of the whole-cell biocatalyst using LentiKats technology was performed. The amount of the immobilised biomass was optimised and the process was scaled up to a production level by immobilising 15 g of dry cell weight per litre of polyvinyl alcohol to produce 3 kg of whole-cell ready-to-use biocatalyst. The immobilised biocatalyst retained its initial activity over six consecutive biotransformations of the secondary amine model compound 3-azabicylo [3,3,0]octane, a building block of the hepatitis C drug telaprevir. Consecutive cultivation cycles in growth conditions not only increased the initial specific activity of biocatalyst produced on the industrial plant by more than 30%, but also significantly increased the rate of the biotransformation compared to the non-propagated biocatalyst.

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“…PVA is a particularly interesting material because it is innocuous, cheap, and also mechanically and chemically robust [6,7]. Even though it has been mainly used for cell immobilization [8], it has been successfully applied to the immobilization of enzymepolymer composites [9,10] and enzyme aggregates [11].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

Nunes

Vila-Real

Fernandes

et al. 2009

Appl Biochem Biotechnol

101

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A synthetic polymer, polyvinyl alcohol (PVA), a cheap and nontoxic synthetic polymer to organism, has been ascribed for biocatalyst immobilization. In this work PVA-alginate beads were developed with thermal, mechanical, and chemical stability to high temperatures (<80 degrees C). The combination of alginate and bead treatment with sodium sulfate not only prevented agglomeration but produced beads of high gel strength and conferred enzyme protection from inactivation by boric acid. Naringinase from Penicillium decumbens was immobilized in PVA (10%)-alginate beads with three different sizes (1-3 mm), at three different alginate concentrations (0.2-1.0%), and these features were investigated in terms of swelling ratio within the beads, enzyme activity, and immobilization yield during hydrolysis of naringin. The pH and temperature optimum were 4.0 and 70 degrees C for the PVA-alginate-immobilized naringinase. The highest naringinase activity yield in PVA (10%)-alginate (1%) beads of 2 mm was 80%, at pH 4.0 and 70 degrees C. The Michaelis constant (K(Mapp)) and the maximum reaction velocity (V(maxapp)) were evaluated for both free (K(Mapp) = 0.233 mM; V(maxapp) = 0.13 mM min(-1)) and immobilized naringinase (K(Mapp) = 0.349 mM; V(maxapp) = 0.08 mM min(-1)). The residual activity of the immobilized enzyme was followed in eight consecutive batch runs with a retention activity of 70%. After 6 weeks, upon storage in acetate buffer pH 4 at 4 degrees C, the immobilized biocatalyst retained 90% of the initial activity. These promising results are illustrative of the potential of this immobilization strategy for the system evaluated and suggest that its application may be effectively performed for the entrapment of other biocatalysts.

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Cited by 47 publications

References 12 publications

Enzyme Immobilization: The Quest for Optimum Performance

Enzyme Immobilization: The Quest for Optimum Performance

Immobilised whole-cell recombinant monoamine oxidase biocatalysis

Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

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