Improved Immobilization Supports for
            <i>Candida Antarctica</i>
            Lipase B

Saunders, P. R.; Brask, Jesper

doi:10.1002/9783527632534.ch3

Cited by 12 publications

(13 citation statements)

References 26 publications

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“…There are also frequent disadvantages, however, including difficult enzyme recovery, low product concentration, low productivity due to substrate and/or product inhibition and, hence, high recovery costs [34]. An important route to improving the performance of enzymes in non-natural environments and their ability to work in continuous processes is to immobilize them by either adsorption, covalent attachment or by incorporation in hydrophobic organic-inorganic hybrid materials [35][36][37][38].…”

Section: Biocatalysismentioning

confidence: 99%

Conversion Technologies for the Production of Liquid Fuels and Biochemicals

Dobbelaere¹,

Anthonis²,

Soetaert³

2014

Cellulosic Energy Cropping Systems

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Section: Biocatalysismentioning

confidence: 99%

Conversion Technologies for the Production of Liquid Fuels and Biochemicals

Dobbelaere¹,

Anthonis²,

Soetaert³

2014

Cellulosic Energy Cropping Systems

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“…1 Furthermore, enzymes can operate in organic solvents, which is beneficial for new types of reactions (synthesis of novel monomers, oligomers, or polymers). 3 The most commonly used biocatalyst in polymerization reactions is immobilized Candida antarctica lipase B (CAL-B) on acrylic resin, commercially available as N435. CAL-B is used due to its stability at elevated temperature and its acceptance of various substrates.…”

Section: ■ Introductionmentioning

confidence: 99%

Lipase-Catalyzed Ring-Opening Copolymerization of ε-Caprolactone and β-Lactam

Stavila¹,

Ekenstein²,

Woortman³

et al. 2013

Biomacromolecules

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The enzymatic ring-opening copolymerization of ε-caprolactone (ε-CL) and β-lactam by using Candida antarctica lipase B (CAL-B) as catalyst was studied. Variation of the feed ratios of 25:75, 50:50, and 75:25 of ε-CL/β-lactam was performed. The products contain poly(ε-CL-co-β-lactam) and the homopolymers of poly(ε-CL) and poly(β-lactam). The structure of the copolymers was determined by MALDI-ToF MS. Poly(ε-CL-co-β-lactam) has an alternating and random structure consisting of alternating repeating units with oligo(ε-CL) or oligo(β-lactam). The highest fraction of the alternating copolymers resulted from the reaction with a feed ratio 50:50. The copolymer is a semicrystalline polymer with a T m at 124 °C and T g s at −15 and 50 °C. Interestingly, the copolymer also demonstrated cold crystallization at 29 and 74 °C, after quenching the sample from the melt in liquid nitrogen.

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“…The first industrial applications of immobilized enzymes were in the production of optically pure amino acids (Tosa et al, 1969) and the hydrolysis of penicillin G (Carleysmith and Lilly, 1979). Since then a lot of research has been conducted (Tischer and Wedekind, 1999;Gross et al, 2001;Krajewska, 2004;Miletić et al, 2009b;Pavlidis et al, 2010;Saunders and Brask, 2010).…”

Section: Background On Enzyme Immobilizationmentioning

confidence: 99%

“…In most reported enzymatic polymerizations it is used as an immobilized enzyme. Novozym 435 is a commercially available heterogeneous biocatalyst that consists of CALB physically immobilized within a macroporous resin of poly(methyl methacrylate) (Saunders and Brask, 2010).…”

Section: Enzymatic Polymerizationsmentioning

confidence: 99%

“…The productivity (space, time, yield) of enzymatic processes is often low due to substrate and/or product inhibition. An important route to improving enzymes' performance in non-natural environments is to immobilize them by either adsorption, covalent attachment or by incorporation in hydrophobic organic-inorganic hybrid materials with the help of a sol-gel process (Tischer and Wedekind, 1999;Miletić et al, 2009a;Pavlidis et al, 2010;Saunders and Brask, 2010).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications

Miletić¹,

Nastasović

Loos

2012

Bioresource Technology

188

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a b s t r a c tBiotechnology also holds tremendous opportunities for realizing functional polymeric materials. Biocatalytic pathways to polymeric materials are an emerging research area with not only enormous scientific and technological promise, but also a tremendous impact on environmental issues. Many of the enzymatic polymerizations reported proceed in organic solvents. However, enzymes mostly show none of their profound characteristics in organic solvents and can easily denature under industrial conditions. Therefore, natural enzymes seldom have the features adequate to be used as industrial catalysts in organic synthesis. The productivity of enzymatic processes is often low due to substrate and/or product inhibition. An important route to improving enzyme performance in non-natural environments is to immobilize them.In this review we will first summarize some of the most prominent examples of enzymatic polymerizations and will subsequently review the most important immobilization routes that are used for the immobilization of biocatalysts relevant to the field of enzymatic polymerizations.

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Improved Immobilization Supports for Candida Antarctica Lipase B

Cited by 12 publications

References 26 publications

Conversion Technologies for the Production of Liquid Fuels and Biochemicals

Conversion Technologies for the Production of Liquid Fuels and Biochemicals

Lipase-Catalyzed Ring-Opening Copolymerization of ε-Caprolactone and β-Lactam

Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications

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