Ring-opening polymerization of ɛ-caprolactone catalyzed by a novel thermophilic lipase from Fervidobacterium nodosum

Li, Quanshun; Li, Guangquan; Yu, Shanshan; Zhang, Zuoming; Ma, Fuqiang; Feng, Yan

doi:10.1016/j.procbio.2010.08.019

Cited by 46 publications

(17 citation statements)

References 34 publications

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“…The filtrate was collected and roto-evaporated to remove dichloromethane, and the remaining viscous sample was precipitated in methanol at −20 o C. The cloudy solution was then centrifuged (8,000 rpm, 15 min), and the white precipitate was dried in a vacuum oven. The structure of PCL was identified by 1 H NMR, and the result was coincident with previous reports from our laboratory [16,22,23].…”

Section: Enzymatic Polymerization Of ε-Caprolactonesupporting

confidence: 89%

Thermophilic esterase from the archaeon Archaeoglobus fulgidus physically immobilized on hydrophobic macroporous resin: A novel biocatalyst for polyester synthesis

2011

Biotechnol Bioproc E

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This paper reviews the immobilization of a thermophilic esterase, AFEST from the archaeon Archaeoglobus fulgidus, on a hydrophobic macroporous resin and its application in polyester synthesis using the ring-opening polymerization of ε-caprolactone as a model. Using the physical adsorption technique, the AFEST loading concentration after 24 h was 152 mg AFEST per g of support.Particle size and surface morphology of the immobilized enzyme were investigated using laser scattering analysis and scanning electron microscopy. The effects of enzyme concentration, temperature, reaction time and reaction medium on monomer conversion and product molecular weight were systematically investigated. Through the optimization of reaction parameters, poly(ε-caprolactone) was obtained at an almost 100% monomer conversion rate and with a low average molecular weight (< 1,100 g/mol). Finally, the immobilized enzyme exhibited good operational stability, with a monomer conversion value of more than 55% after four batch reactions.

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Section: Enzymatic Polymerization Of ε-Caprolactonesupporting

confidence: 89%

Thermophilic esterase from the archaeon Archaeoglobus fulgidus physically immobilized on hydrophobic macroporous resin: A novel biocatalyst for polyester synthesis

2011

Biotechnol Bioproc E

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“…Research on enzymatic synthesis of PCL has mainly focused on: (1) screening novel biocatalysts, especially from thermophiles (Hunsen et al 2007;Ma et al 2009;Li et al 2011); (2) optimizing the reaction parameters to obtain a high isolated yield and M n values (Kumar & Gross 2000); (3) exploring new ' green ' reaction media, e.g. ionic liquids (Marcilla et al 2006), supercritical carbon dioxide (Loeker et al 2004) and hydrofl uorocarbon solvents Biocatalysis and Biotransformation, November-December 2011;29(6) (Garcia-Arrazola et al 2007); (4) elucidating the polymerization kinetics and mechanism through Michaelis -Menten kinetic analysis and computeraided molecular modelling (van der Mee et al 2006;Veld et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Lipase-catalyzed synthesis of poly(ε-caprolactone) and characterization of its solid-state properties

Yang

Zhao

et al. 2011

Biocatalysis and Biotransformation

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Ring-opening polymerization of ε-caprolactone has been successfully conducted using an immobilized form of Candida antarctica lipase B as catalyst. The effects of enzyme concentration, reaction medium, reaction temperature and time on monomer conversion and product molecular weight were investigated. Through optimization of reaction conditions, poly( ε -caprolactone) (PCL) was obtained with 99% monomer conversion and a number-average molecular weight ( M n ) of 18870 g/mol. The reaction system was then scaled up, and PCL was synthesized in 78% isolated yield, with M n and polydispersity index of 41540 g/mol and 1.69, respectively. The solid-state properties of this sample were systematically evaluated using thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), wide-angle X-ray diffraction (WAXD) and polarized optical microscopy (POM). The product PCL showed excellent thermal stability, with degradation of the main chain in the temperature range of 280 -450 ° C. Remarkably, this high molecular weight PCL was a typical crystalline polymer with a high degree of crystallinity observed by DSC, WAXD and POM.

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“…The same authors, more recently, developed also another catalyst for polyesters synthesis: a thermophilic lipase from Fervidobacterium nodosum (FNL) an extremely thermophilic, glycolytic anaerobic bacterium [78]. FNL showed different and broader substrate specificity: it catalyzes the hydrolysis of p-nitrophenyl esters from C12 to C16, and triglycerides of short to mid-acyl chain (C4 to C10) and olive oil.…”

Section: Polyesters Productionmentioning

confidence: 99%

A Review on Extremozymes Biocatalysis: A Green Industrial Approach for Biomaterials Production

Calarco¹

2015

J Biomol Res Ther

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Ring-opening polymerization of ɛ-caprolactone catalyzed by a novel thermophilic lipase from Fervidobacterium nodosum

Cited by 46 publications

References 34 publications

Thermophilic esterase from the archaeon Archaeoglobus fulgidus physically immobilized on hydrophobic macroporous resin: A novel biocatalyst for polyester synthesis

Thermophilic esterase from the archaeon Archaeoglobus fulgidus physically immobilized on hydrophobic macroporous resin: A novel biocatalyst for polyester synthesis

Lipase-catalyzed synthesis of poly(ε-caprolactone) and characterization of its solid-state properties

A Review on Extremozymes Biocatalysis: A Green Industrial Approach for Biomaterials Production

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