The enantioselectivity of Candida rugosa lipase is influenced by the particle size of the immobilising support material Accurel

Sabbani, Sunil; Hedenström, Erik; Nordin, Ove

doi:10.1016/j.molcatb.2006.05.003

Cited by 57 publications

(49 citation statements)

References 29 publications

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“…Sabbani et al [28] observed the important role of particle size and pore size in enantiomeric ratio, which demonstrates the significance of this kind of variables.…”

Section: Diethyl 2-phenylmalonate (Pro-3) Hydrolysismentioning

confidence: 93%

Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Cunha

Fernández‐Lorente

Gutarra

et al. 2008

Appl Biochem Biotechnol

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Lipases are an enzyme class of a great importance as biocatalysts applied to organic chemistry. However, it is still necessary to search for new enzymes with special characteristics such as good stability towards high temperatures, organic solvents, and high stereoselectivity presence. The present work's aim was to immobilize the lipases pool produced by Penicillium simplissicimum, a filamentous fungi strain isolated from Brazilian babassu cake residue. P. simplissicimum lipases were separated into three different fractions using selective adsorption method on different hydrophobic supports (butyl-, phenyl-, and octyl-agarose) at low ionic strength. After immobilization, it was observed that these fractions' hyperactivation is in the range of 131% to 1133%. This phenomenon probably occurs due to enzyme open form stabilization when immobilized onto hydrophobic supports. Those fractions showed different thermal stability, specificity, and enantioselectivity towards some substrates. Enantiomeric ratio for the hydrolysis of (R,S) 2-O-butyryl-2-phenylacetic acid ranged from 1 to 7.9 for different immobilized P. simplissicimum lipase fractions. Asymmetry factor for diethyl 2-phenylmalonate hydrolysis ranged from 11.8 to 16.4 according to the immobilized P. simplissicimum lipase fractions. Those results showed that sequential adsorption methodology was an efficient strategy to obtain new biocatalysts with different enantioselectivity degrees, thermostability, and specificity prepared with a crude extract produced by a simple and low-cost technology.

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“…Sabbani et al [28] observed the important role of particle size and pore size in enantiomeric ratio, which demonstrates the significance of this kind of variables.…”

Section: Diethyl 2-phenylmalonate (Pro-3) Hydrolysismentioning

confidence: 93%

Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Cunha

Fernández‐Lorente

Gutarra

et al. 2008

Appl Biochem Biotechnol

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“…For CALB, specific activity varied from 27.1 ± 1.20 to 8.68 ± 0.88 IU mgIP −1 , while for BTL2 the specific activity 34.4 ± 2.40 to 13.9 ± 1.80% by immobilizing on SPHB and LPHB, respectively. The conformational change on the three-dimensional structure of lipase (that influences its catalytic activity) depends on the structure of the enzyme and nature of the surface and pores of the support [70]. Among the biocatalysts prepared, the immobilization of TLL2 on small PHB beads displayed highest specific activity, while the immobilization of PFL on large PHB beads led to better conformation of the enzyme, rendering the highest specific activity among the biocatalysts prepared on LPHB.…”

Section: Immobilization Of Lipases On Sphb and Lphb Beadsmentioning

confidence: 99%

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Mendes

Oliveira

Velez

et al. 2012

International Journal of Biological Macromolecules

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Five microbial lipase preparations from several sources were immobilized by hydrophobic adsorption on small or large poly-hydroxybutyrate (PHB) beads and the effect of the support particle size on the biocatalyst activity was assessed in the hydrolysis of olive oil, esterification of butyric acid with butanol and transesterification of babassu oil (Orbignya sp.) with ethanol. The catalytic activity of the immobilized lipases in both olive oil hydrolysis and biodiesel synthesis was influenced by the particle size of PHB and lipase source. In the esterification reaction such influence was not observed. Geobacillus thermocatenulatus lipase (BTL2) was considered to be inadequate to catalyze biodiesel synthesis, but displayed high esterification activity. Butyl butyrate synthesis catalyzed by BTL2 immobilized on small PHB beads gave the highest yield (≈90 mmol L(-1)). In biodiesel synthesis, the catalytic activity of the immobilized lipases was significantly increased in comparison to the free lipases. Full conversion of babassu oil into ethyl esters was achieved at 72 h in the presence of Pseudozyma antarctica type B (CALB), Thermomyces lanuginosus lipase (Lipex(®) 100 L) immobilized on either small or large PHB beads and Pseudomonas fluorescens (PFL) immobilized on large PHB beads. The latter preparation presented the highest productivity (40.9 mg of ethyl esters mg(-1) immobilized protein h(-1)).

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“…The adsorption of lipases on this support is an interesting opportunity to immobilize and purify lipases in one-step process, because the selective adsorption of these enzymes on this hydrophobic support, because of their molecular properties, has been observed. 4,24,25 Another method that could be used to immobilize lipases is the covalent attachment on solid supports. 26 Eupergit V R C (made by copolymerization of N,N 0 -methylene-bis-(methacrylamide), glycidyl methacrylate, allyl glycidyl ether, and methacrylamide) is a very interesting support, because it is resistant to mechanical and chemical stresses.…”

Section: Introductionmentioning

confidence: 99%

Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

Guillén

Benaiges

Valero

2011

Biotechnology Progress

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The stability of a soluble extract containing a recombinant lipase from Rhizopus oryzae (Cursive) lipase (rROL) produced by Pichia pastoris (Cursive), as well as that for the commercial extract containing the lipase produced by the native organism (nROL), was investigated. The results showed higher residual activity values of the commercial protein compared with the recombinant one. Moreover, two different kinds of support, the polypropylene powder EP100 and Eupergit®C, were tested to immobilize the enzymes. The residual activity of the immobilizated derivatives was also tested to determine whether their stability was enhanced. The results showed a slight improvement in rROL using both supports but a decrease in nROL using Eupergit®C. The study of the residual activity of soluble and immobilized enzymes was performed by means of a central composite rotatable experiment design. In addition, EP100 adsorption isotherms were determined.

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The enantioselectivity of Candida rugosa lipase is influenced by the particle size of the immobilising support material Accurel

Cited by 57 publications

References 29 publications

Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

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