Efficient immobilisation of industrial biocatalysts: criteria and constraints for the selection of organic polymeric carriers and immobilisation methods

Cantone, Sara; Ferrario, Virgilio F.; Corîci, Livia; Ebert, Cynthia; Fattor, Diana; Spizzo, Patrizia; Gardossi, Lucia

doi:10.1039/c3cs35464d

Cited by 410 publications

(313 citation statements)

References 46 publications

(71 reference statements)

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“…Considering the data reported in literature, it must be noted that results in terms of molecular weight of polymerization products might be affected by detachment and dispersion of the enzyme when not covalently supported as demonstrated in previous studies [64]. In addition to adsorbed preparation with consequently problematic leaching, the mechanical strength of CLEAs preparations still has to be demonstrated on an industrially relevant scale [65].…”

Section: Cutinases As Biocatalysts For Polymerization Reactionsmentioning

confidence: 99%

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Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

et al. 2016

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Abstract:The polymer and plastic sectors are under the urge of mitigating their environmental impact. The need for novel and more benign catalysts for polyester synthesis or targeted functionalization led, in recent years, to an increasing interest towards cutinases due to their natural ability to hydrolyze ester bonds in cutin, a natural polymer. In this review, the most recent advances in the synthesis and hydrolysis of various classes of polyesters and polyamides are discussed with a critical focus on the actual perspectives of applying enzymatic technologies for practical industrial purposes. More specifically, cutinase enzymes are compared to lipases and, in particular, to lipase B from Candida antarctica, the biocatalyst most widely employed in polymer chemistry so far. Computational and bioinformatics studies suggest that the natural role of cutinases in attacking natural polymers confer some essential features for processing also synthetic polyesters and polyamides.

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Section: Cutinases As Biocatalysts For Polymerization Reactionsmentioning

confidence: 99%

“…Scanning Electron Micrograph (SEM) images of the beads showed that the average pore size is 10 times larger than CaLB or polystyrene molecules, implying that there is no physical barrier to enzyme or substrate diffusion throughout the beads [65].…”

Section: Cutinases As Biocatalysts For Polymerization Reactionsmentioning

confidence: 99%

Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

et al. 2016

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“…Due to its chemical structure, amino and hydroxyl functionalities are buried within the framework, making this material a promising candidate for covalent enzyme immobilization approaches. Since enzyme immobilization is preliminary performed using films and beads [1,2],…”

Section: Introductionmentioning

confidence: 99%

Approaching Immobilization of Enzymes onto Open Porous Basotect®

et al. 2017

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Abstract:For the first time, commercial macroporous melamine formaldehyde foam Basotect ® (BT) was used as a basic carrier material for both adsorptive and covalent enzyme immobilization. In order to access inherent amino groups, the Basotect ® surface was pretreated with hydrochloric acid. The resulting material revealed 6 nmol of superficial amino groups per milligram Basotect ® . Different optimized strategies for tethering the laccase from Trametes versicolor and the lipase from Thermomyces lanuginosus onto the pre-treated Basotect ® surface were studied. Particularly, for covalent immobilization, two different strategies were pursued: lipase was tethered via a cross-linking method using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, and laccase was bound after functionalizing Basotect ® with hydrophilic copolymer poly(ethylene-alt-maleic anhydride) (PEMA). Prior to laccase immobilization, the PEMA coating of Basotect ® was verified by ATR-FTIR analysis. Subsequent quantification of available high-reactive PEMA anhydride moieties revealed an amount of 1028 ± 73 nmol per mg Basotect ® . The surface-bound enzyme amounts were quantified as 4.1-5.8 µg per mg Basotect ® . A theoretical surface-covered enzyme mass for the ideal case that an enzyme monolayer was immobilized onto the Basotect ® surface was calculated and compared to the amount of adsorptive and covalently bound enzymes before and after treatment with SDS. Furthermore, the enzyme activities were determined for the different immobilization approaches, and the stability during storage over time and against sodium dodecyl sulfate treatment was monitored. Additionally, PEMA-BT-bound laccase was tested for the elimination of anthropogenic micropollutant bisphenol A from contaminated water in a cost-effective and environmentally-friendly way and resulted in a degradation rate higher than 80%.

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“…The carriers used for enzyme immobilization have one or more kinds of functional group (e.g., epoxy group, amino group, carboxylic acid), and are linked enzymatic protein by its functional group [12] [13]. Many types of immobilization beads are currently available on the market [13]. Various types of enzymes such as lipase, penicillin acylase, laccase and glucose isomerase have been applied in many industries with the use of immobilization [15] [16] [17].…”

Section: Introductionmentioning

confidence: 99%

“…Organic polymers can be sub-divided into natural polymers (e.g., cellulose, alginate, collagen, carbon) and synthetic polymers (e.g., polystyrene, polyacrylic, polypropylene) [12] [13] [14]. The carriers used for enzyme immobilization have one or more kinds of functional group (e.g., epoxy group, amino group, carboxylic acid), and are linked enzymatic protein by its functional group [12] [13]. Many types of immobilization beads are currently available on the market [13].…”

Section: Introductionmentioning

confidence: 99%

Continuous Saccharification of Laminarin by Immobilized Laminarinase ULam111 Followed by Ethanol Fermentation with a Marine-Derived Yeast

Mitsuya¹,

Yamamoto²,

Okai³

et al. 2017

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We isolated a novel laminarinase ULam111 from Flavobacterium sp. strain UMI-01. Purified ULam111 showed degradation activity against laminarin with the specific activity of 224 ± 18 U/mg at 30˚C and pH 6.0. Its optimum temperature was 50˚C, and degradation activities against laminarin were observed at 4˚C -80˚C. With a laminarin degradation system, we investigated the preparation and properties of immobilized ULam111 with the use of the 11 types of carriers. The high activity recoveries of immobilized ULam111 were as follows: 19.4% for IB-S60P carrier beads (the non-ionic type), 15.6% for IB-S60S carrier beads (the non-ionic type), 11.9% for IB-150P carrier beads (the covalent type), and 7.1% for IB-C435 carrier beads (the cationic type). With the repeated use of immobilized ULam111, the enzyme activities immobilized on IB-S60S and those on IB-S60P remained at 40% and 30% respectively after the sixth trial. We selected IB-S60S as suitable beads for enzyme immobilization, and we attempted to construct a reactor system with ULam111 immobilized on IB-S60S beads. In this system, 1.2 -1.9 g/L glucose was repeatedly produced from 30 mg/mL laminarin solutions after 20 hr when the reactor operation was repeated 10 times. We examined ethanol fermentation from the saccharified solutions with a marine-derived yeast (Saccharomyces cerevisiae C-19), and 0.51 -0.58 g/L bioethanol was produced from the saccharified solution that contained 1.71 -1.86 g/L of glucose.

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Efficient immobilisation of industrial biocatalysts: criteria and constraints for the selection of organic polymeric carriers and immobilisation methods

Cited by 410 publications

References 46 publications

Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

Approaching Immobilization of Enzymes onto Open Porous Basotect®

Continuous Saccharification of Laminarin by Immobilized Laminarinase ULam111 Followed by Ethanol Fermentation with a Marine-Derived Yeast

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