Lipase-mediated direct in situ ring-opening polymerization of ε-caprolactone formed by a chemo-enzymatic method

Zhang, Yuanyuan; Lu, Peiyu; Sun, Quansen; Li, Tao; Zhao, Lingxia; Gao, Xin; Wang, Fanye; Liu, Junhong

doi:10.1016/j.jbiotec.2018.06.338

Cited by 8 publications

(10 citation statements)

References 54 publications

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“…Table gives the comparison of the experimental results of this study with ref . The conversion of cyclohexanone and yield of poly(ε-caprolactone) were 98.2% and 92.4%, respectively, which were much higher than those in ref (65.4% and 62.3%). This might be that the optimum conditions obtained were adopted in this study, i.e., stirring speed was 200 rpm, particle size of immobilized lipase catalyst was 0.45 mm, ratio of cyclohexanone/UHP was 1:1.5, reaction temperature was 60 °C, and 3 mL hydrophobic organic solvent toluene was added instead of 2 mL in ref .…”

Section: Resultsmentioning

confidence: 59%

Section: Resultsmentioning

confidence: 63%

“…Immobilized enzymes have been presented as practical catalysts owing to their significant advantages such as good stability, easy reusability, and increased resistance to inhibitors or chemicals. , Glutaraldehyde, a multifunctional cross-linker agent or activator of supports, has been widely applied in immobilization of enzyme . It was reported that this strategy has been successfully utilized in many works in which glutaraldehyde was used as a cross-linker agent to enhance the retention of lipases on the carriers. − The lipases from T. laibacchii are intracellular lipolytic enzymes that have been successfully used in the resolution of ketoprofen, the stereoselective synthesis of chiral 1,3-oxathiolane, and the direct in situ ring-opening polymerization of ε-caprolactone . In this work, T. laibacchii lipase was immobilized on diatomite supports using glutaraldehyde as a cross-linker in order to improve the stability of lipase.…”

Section: Introductionmentioning

confidence: 99%

“…14−16 The lipases from T. laibacchii are intracellular lipolytic enzymes that have been successfully used in the resolution of ketoprofen, 17 the stereoselective synthesis of chiral 1,3-oxathiolane, 18 and the direct in situ ring-opening polymerization of ε-caprolactone. 19 In this work, T. laibacchii lipase was immobilized on diatomite supports using glutaraldehyde as a cross-linker in order to improve the stability of lipase.…”

Section: ■ Introductionmentioning

confidence: 99%

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Lipase-Catalyzed Oxidation of Cyclohexanone To Form ε-Caprolactone and Kinetic Modeling

Zhang

Zhao

Jiang

et al. 2019

ACS Sustainable Chem. Eng.

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The chemoenzymatic conversion of cyclohexanone to ε-caprolactone (1.25 M) mediated by immobilized lipase from T. laibacchi was successfully achieved with a yield of 98.6%, which is much higher than that in previous studies. A proposed kinetic model consisting of two enzymatic reactions catalyzed by the lipase and one chemical reaction was developed, which fitted the experimental data very well. It was concluded that the enzymatic oxidation of ethyl acetate using urea hydrogen peroxide (UHP) to generate in situ peracetic acid mediated by the lipase may follow an irreversible ping-pong three–four mechanism with substrate inhibitions, which is proposed herein for the first time. Also, the oxidation of cyclohexanone to ε-caprolactone by peracetic acid in a chemical fashion may follow a power law. Finally, the reaction of formed acetic acid with UHP to form peracetic acid catalyzed by the lipase may follow an irreversible ping-pong Bi–Bi mechanism with substrate inhibitions. Reaction kinetic data reveal that UHP and acetic acid might have strong substrate inhibition, while peracetic acid might have no product inhibition. Results of enzyme stability test suggest that it is reasonable to adopt a simple exponential equation as the inactivation model of the lipase. The effect of Michaelis–Menten interaction on the reaction rate could be neglected due to the strong substrate inhibition, which makes the constant similar to Michaelis–Menten zero. The yield of in situ polymerization was significantly increased from 61.3% to 92.4% under the optimum conditions obtained in this study.

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Section: Resultsmentioning

confidence: 59%

Section: Resultsmentioning

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

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Lipase-Catalyzed Oxidation of Cyclohexanone To Form ε-Caprolactone and Kinetic Modeling

Zhang

Zhao

Jiang

et al. 2019

ACS Sustainable Chem. Eng.

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“…Terzopoulu et al [3] reported the ROP of CL using SO as a catalyst and initiator. Similarly, other novel initiators such as benzylalcohol [4,5], gelatin [6], lipase [7], mercaptohexanol [8], diethyleneglycol [9], bisphenolate ligand [10] and mPEG [11] were used for the ROP of CL. Due to the bio-degradability and bio-compatibility of PCL, it is used as a drug carrier material.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, characterization and sustainable drug release activity of drug bridged diblock copolymer

Anbarasan

Kailash²,

Meenarathi³

2019

SN Appl. Sci.

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Ring opening polymerization of ε-caprolactone and tetrahydrofuran were carried out by bulk polymerization technique in the presence of a drug molecule as an initiator at 160 °C for 2 h under nitrogen atmosphere. The synthesized homo and diblock copolymer was characterized by various analytical techniques. Further, the sustainable drug release study was carried out at gastric pH of 7.2. The diblock copolymer formation was confirmed by the appearance of aromatic C=O stretching around 1680 cm −1 . Due to the hydrophilic nature the diblock copolymer exhibited lower melting temperature. The drug release study confirmed the first order drug release model.

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Polymer Synthesis by Enzymatic Catalysis

Loos¹

2022

Macromolecular Engineering

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Enzymatic polymerizations are defined as in vitro enzyme‐catalyzed syntheses of polymers that do not follow biosynthetic pathways. Polymer synthesis using biocatalytic pathways holds enormous promise in the fields of science. Use of enzymes for polymer synthesis can have tremendous environmental benefits as chemical approaches require large scale use of hazardous chemical solvents and substantial energy input. Enzymatic reactions can be carried out at ambient temperature, and reaction medium in many cases is water, which is a green solvent. Moreover, it also reduces the waste generated by chemical processes. Thus, enzymatic approaches to polymer synthesis are socially, environmentally, and economically superior to chemical approaches.

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Lipase-mediated direct in situ ring-opening polymerization of ε-caprolactone formed by a chemo-enzymatic method

Cited by 8 publications

References 54 publications

Lipase-Catalyzed Oxidation of Cyclohexanone To Form ε-Caprolactone and Kinetic Modeling

Lipase-Catalyzed Oxidation of Cyclohexanone To Form ε-Caprolactone and Kinetic Modeling

Synthesis, characterization and sustainable drug release activity of drug bridged diblock copolymer

Polymer Synthesis by Enzymatic Catalysis

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