Lipase immobilized on HOOC-MCF: A highly enantioselective catalyst for transesterification resolution of (R,S)-1-phenylethanol

Xue, Ping; Yan, Xiang; Wang, Zheng

doi:10.1016/j.cclet.2007.06.005

Cited by 19 publications

(8 citation statements)

References 7 publications

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“…Using SiO 2 -CaLB-L a conversion of 39% and ee p > 99% were obtained in 48 h of reaction. These are good results according with the ones found in the literature when it was used Pseudomonas cepacia, 27 Burkholderia cepacia 23 and Aspergillus niger 19 lipases for enantioselective transesterification reactions, with high selectivity.…”

Section: All Lipases Were Able To Convert the Alcohol Into The (R)-(+supporting

confidence: 77%

Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases

Mittersteiner¹,

Machado²,

Jesus³

et al. 2016

J. Braz. Chem. Soc.

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In this study, lipase from Candida antarctica B (Lipozyme CaLB-L) was successfully immobilized on SiO 2 through adsorption and used to obtain (R)-(+)-esters derived from (R,S)-1-phenylethanol. The new immobilized enzyme was compared with commercially immobilized lipases (Novozyme 435, Lipozyme 435 and Pseudomonas cepacia (PSC-II and PSD-I)). Lipozyme CaLB-L adsorbed onto SiO 2 was found to be a good catalyst and, under optimal conditions, esters could be obtained with conversion 44%, enantiomeric excess of product (ee p ) > 99%, enantiomeric excess of substract (ee s ) 77% and enantiomeric ratio (E) > 200. The lipase maintained enantioselectivity under adverse conditions, such as in organic solvents, with an excess of substrate and at different temperatures. The immobilized lipase could be reused five times with no significant loss of the activity.

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Section: All Lipases Were Able To Convert the Alcohol Into The (R)-(+supporting

confidence: 77%

Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases

Mittersteiner¹,

Machado²,

Jesus³

et al. 2016

J. Braz. Chem. Soc.

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“…The above catalytic capabilities and characteristics testify lipase ZS04 to be an exceedingly useful biocatalyst focusing on the resolution of racemic compounds with 1-phenylethanol moiety. Compared to the lipase LC2-8 involved in the resolution of 1-phenylethanol with the conversion yield of 26.2 % after optimization [8], as well as the lipase PSL immobilized on HOOC-MCF with ee p > 99 % at 50 % conversion but only 7 % conversion with the free form [26], lipase ZS04 exhibited not only a highly strict selectivity toward (R)-1-phenylethanol analogs but also a more excellent conversion capacity and more promising application.…”

Section: Chiral Resolution Of Racemic Mope Analogsmentioning

confidence: 98%

A Calcium-Ion-Stabilized Lipase from Pseudomonas stutzeri ZS04 and its Application in Resolution of Chiral Aryl Alcohols

Qin

Zhao

et al. 2016

Appl Biochem Biotechnol

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An extracellular organic solvent-tolerant lipase-producing bacterium was isolated from oil-contaminated soil samples and was identified taxonomically as Pseudomonas stutzeri, from which the lipase was purified and exhibited maximal activity at temperature of 50 °C and pH of 9.0. Meanwhile, the lipase was stable below or at 30 °C and over an alkaline pH range (7.5-11.0). Ca could significantly improve the lipase thermal stability which prompts a promising application in biocatalysis through convenient medium engineering. The lipase demonstrated striking features such as distinct stability to the most tested hydrophilic and hydrophobic solvents (25 %, v/v), and DMSO could activate the lipase dramatically. In the enzyme-catalyzed resolution, lipase ZS04 manifested excellent enantioselective esterification toward the (R)-1-(4-methoxyphenyl)-ethanol (MOPE), a crucial chiral intermediate in pharmaceuticals as well as in other analogs with strict substrate specificity and theoretical highest conversion yield. This strong advantage over other related schemes made lipase ZS04 a promising biocatalyst in organic synthesis and pharmaceutical applications.

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“…It can be seen from Table 1, compared with related works on chiral resolution published in the past decades [9,[27][28][29][30][31][32], the immobilized BCL in this work exhibited a higher enantioselectivity and a shorter reaction time (2 h). As BCL was immobilized through physical absorption, the enhancement of resolution efficiency was mainly attributable to the properties of pH sensitive particles.…”

Section: In Comparison With Other Enzymesmentioning

confidence: 82%

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

Cui

et al. 2018

Catalysts

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Abstract:A kind of pH-responsive particle was synthesized using modified pullulan polysaccharide. The synthesized particle possessed a series of merits, such as good dispersity, chemical stability and variability of particle size, making it a suitable carrier for enzyme immobilization. Then, Burkholderia cepacia lipase (BCL), a promising biocatalyst in transesterification reaction, was immobilized on the synthesized particle. The highest catalytic activity and immobilization efficiency were achieved at pH 6.5 because the particle size was obviously enlarged and correspondingly the adsorption surface for BCL was significantly increased. The immobilization enzyme loading was further optimized, and the derivative lipase was applied in chiral resolution. Under the optimal reaction conditions, the immobilized BCL showed a very good performance and significantly shortened the reaction equilibrium time from 30 h of the free lipase to 2 h with a conversion rate of 50.0% and ee s at 99.2%. The immobilized lipase also exhibited good operational stability; after being used for 10 cycles, it still retained over 80% of its original activity. Moreover, it could keep more than 80% activity after storage for 20 days at room temperature in a dry environment. In addition, to learn the potential mechanism, the morphology of the particles and the immobilized lipase were both characterized with a scanning electron microscope and confocal laser scanning microscopy. It was found that the enlarged spherical surface of the particle in low pH values probably led to high immobilized efficiency, resulting in the improvement of enantioselectivity activity in chiral resolution.

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Lipase immobilized on HOOC-MCF: A highly enantioselective catalyst for transesterification resolution of (R,S)-1-phenylethanol

Cited by 19 publications

References 7 publications

Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases

Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases

A Calcium-Ion-Stabilized Lipase from Pseudomonas stutzeri ZS04 and its Application in Resolution of Chiral Aryl Alcohols

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

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