In vitro enzymic synthesis of polymers containing saccharides, lignins, proteins or related compounds: a review

Donnelly, Michael

doi:10.1002/(sici)1097-0126(199811)47:3<257::aid-pi8>3.0.co;2-2

Cited by 11 publications

(5 citation statements)

References 24 publications

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“…16 More recently Kroutil and co-workers identified a strain from Paracoccus pantotrophus, which secretes a DMSO-tolerant (up to 50% DMSO) alcohol dehydrogenase. 17 Given all this progress, the enzymes that work in anhydrous DMSO or DMF remain far from adequate, considering the immense potential of enzymatic catalysis in anhydrous DMSO or DMF, such as the derivation of mono-, di-, trisaccharides, polysaccharides, [18][19][20][21][22] and cellulose, 23,24 peptide synthesis. 25,26 Recent progress in incorporating enzymes into nanostructures, [27][28][29][30][31][32] such as the encapsulation of enzymes in mesoporous silica, 33 single enzyme nanoparticles, 34 single enzyme nano-gels, [35][36][37] and enzyme in molecular hydrogels, [38][39][40][41][42] has provided alternative methods for enhancing enzyme stability and activity under harsh conditions.…”

Section: Introductionmentioning

confidence: 99%

“…More recently Kroutil and co-workers identified a strain from Paracoccus pantotrophus, which secretes a DMSO-tolerant (up to 50% DMSO) alcohol dehydrogenase . Given all this progress, the enzymes that work in anhydrous DMSO or DMF remain far from adequate, considering the immense potential of enzymatic catalysis in anhydrous DMSO or DMF, such as the derivation of mono-, di-, trisaccharides, polysaccharides, − and cellulose, , peptide synthesis. , …”

Section: Introductionmentioning

confidence: 99%

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Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

Wang

et al. 2009

Biomacromolecules

103

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The present work showed that Candida rugosa lipase, which is inactive in anhydrous dimethyl sulfoxide (DMSO), has been granted its original catalytic activity and greatly enhanced stability when encapsulated into a polyacrylamide nanogel. The molecular simulation and structural analysis suggested that the polyacrylamide nanogel shielded the extraction of essential water and maintained the native configuration of encapsulated lipase in anhydrous DMSO at an elevated temperature. The electron and fluorescence microscopy showed that the lipase nanogel would be well dispersed in anhydrous DMSO where its native counterpart aggregated. The encapsulated lipase behaved as a stable catalyst for transesterification between dextran and vinyl decanoate in anhydrous DMSO at 60 degrees C for 240 h and yielded a dextran-based polymeric surfactant with regioselectivity toward the C-2 hydroxyl group in the glucopyranosyl unit of dextran. All these indicated a high potential of enzyme nanogel for nonaqueous biocatalysis.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

Wang

et al. 2009

Biomacromolecules

103

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“…Enzymes are used as catalysts in a wide variety of reactions due to their high activity and selectivity while also being more environmentally acceptable than some conventional catalysts − Enzyme catalysis has provided a new synthetic strategy for useful polymers, most of which are otherwise very difficult to produce by conventional chemical catalysts. , …”

Section: Introductionmentioning

confidence: 99%

“…1 In the past decades, there has been an increasing interest in polymer synthesis via enzyme catalysis. [2][3][4][5][6][7][8][9][10][11] Enzyme catalysis has provided a new synthetic strategy for useful polymers, most of which are otherwise very difficult to produce by conventional chemical catalysts. 12,13 Lipase has shown extraordinary activity for a range of polymer-forming reactions including enzymatic ring opening polymerization (eROP) of caprolactones 3,[14][15][16][17][18][19][20][21][22] as well as copolymerization of lactones with other monomers to make copolymers.…”

Section: Introductionmentioning

confidence: 99%

One-Step Chemoenzymatic Synthesis of Poly(ε-caprolactone-block-methyl methacrylate) in Supercritical CO₂

et al. 2006

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Enzymatic ring-opening polymerization (eROP) of ε-caprolactone (ε-CL) and atom-transfer radical polymerization (ATRP) of methyl methacrylate (MMA) were integrated into a one-step chemoenzymatic route to yield poly(ε-CL-block-MMA) (PCL-b-PMMA) in supercritical carbon dioxide (scCO2). The interaction between eROP and ATRP during the copolymerization was studied: Cu(I)Br/bpy as ATRP catalyst was compatible with eROP, while Ni(PPh)3Br2 inhibited enzyme activity; under the reaction conditions, both ε-CL and PCL improved the solubility of poly(MMA) (PMMA) in the reaction system, and thus the ATRP proceeded successfully. The propagation of PMMA block exhibited living kinetics during the copolymerization, ensuring the molecular weight was well controlled. PCL-b-PMMA copolymers with varying molecular weight were synthesized with good control of the composition of the block copolymer. The one-step chemoenzymatic polymerization provides a very simple and versatile route for the synthesis of block copolymers.

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“…Hydrolases, discovered to be capable of functioning in the reverse synthetic direction in organic solvents, have found widespread applications in ester synthesis (12). A number of successful examples have been reported on utilization of hydrolases to acylation on carbohydrates such as mono‐, di‐, and trisaccharides (13 − 18), but relatively few on polysaccharides (19, 20). Both Sereti et al (2) and Xie and Hsieh (21) investigated the heterogeneous enzymatic esterification of cellulose solids in organic solvents.…”

Section: Introductionmentioning

confidence: 99%

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

Yang

Wang

2003

Biotechnology Progress

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Screening for lipases capable of catalyzing acetylation of cellulosic substrates was conducted in aqueous buffer solution using water-soluble carboxymethyl cellulose (CMC) as substrate. Lipase A12 from Aspergillus niger (A. niger) showed the most promising acetylation activity among 11 tested commercial microbial lipases and was further applied to catalyzing acetylation of solid cellulose in aqueous solution. This reaction was shown to be feasible with an acetylation extent of 0.16 wt % achieved compared with no detectable acetylation in the absence of enzyme. Pretreatments on cellulose substrate by ultrasonic irradiation and surfactant solution only slightly improved the acetylation extent by 44 and 27%, respectively. Alternatively, this lipase-catalyzed acetylation was remarkably improved with solubilized cellulose as substrate in the dimethyl sulfoxide/paraformaldehyde solvent system, with an acetylation extent (7.87 wt %) nearly 50 times higher than that achieved in aqueous solution. This improvement was attributed to (1) the absence of bulk water and the increase in substrate solubility by the transition of reaction media from aqueous solution to organic solvents and (2) the ability of lipase A12 to remain catalytically active in highly polar DMSO. This discovery that the A. niger lipase was capable of surviving its contact with polar solvents was further confirmed by its considerably preserved catalytic activity on CMC acetylation in aqueous media after enzyme pretreatments with organic solvents of various polarities and in mixture media with the aqueous phase partially replaced by organic solvents.

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In vitro enzymic synthesis of polymers containing saccharides, lignins, proteins or related compounds: a review

Cited by 11 publications

References 24 publications

Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

One-Step Chemoenzymatic Synthesis of Poly(ε-caprolactone-block-methyl methacrylate) in Supercritical CO₂

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

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In vitro enzymic synthesis of polymers containing saccharides, lignins, proteins or related compounds: a review

Cited by 11 publications

References 24 publications

Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

Lipase Nanogel Catalyzed Transesterification in Anhydrous Dimethyl Sulfoxide

One-Step Chemoenzymatic Synthesis of Poly(ε-caprolactone-block-methyl methacrylate) in Supercritical CO2

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

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One-Step Chemoenzymatic Synthesis of Poly(ε-caprolactone-block-methyl methacrylate) in Supercritical CO₂