Chemoenzymatic Synthesis of the New 3-((2,3-Diacetoxypropanoyl)oxy)propane-1,2-diyl Diacetate Using Immobilized Lipase B from Candida antarctica and Pyridinium Chlorochromate as an Oxidizing Agent

To exploit the hydrolytic activity and high selectivity of immobilized lipase B from Candida antarctica on octyl agarose (CALB-OC) in the hydrolysis of triacetin and also to produce new value-added compounds from glycerol, this work describes a chemoenzymatic methodology for the synthesis of the new dimeric glycerol ester 3-((2,3-diacetoxypropanoyl)oxy)propane-1,2-diyl diacetate. According to this approach, triacetin was regioselectively hydrolyzed to 1,2-diacetin with CALB-OC. The diglyceride product was subsequently oxidized with pyridinium chlorochromate (PCC) and a dimeric ester was isolated as the only product. It was found that the medium acidity during the PCC treatment and a high 1,2-diacetin concentration favored the formation of the ester. The synthesized compounds were characterized using IR, MS, HR-MS, and NMR techniques. The obtained dimeric ester was evaluated at 100 ppm against seven bacterial strains and two Candida species to identify its antimicrobial activity. The compound has no inhibitory activity against the bacterial strains used but decreased C. albicans and C. parapsilosis growth by 49% and 68%, respectively. Hemolytic activity was evaluated, and the results obtained support the use of the dimeric ester to control C. albicans and C. parapsilosis growth in non-intravenous applications because the compound shows hemolytic activity.

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Immobilization on octyl-agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Biotechnology Progress ◽

10.1002/btpr.2735 ◽

2018 ◽

Vol 35 (1) ◽

pp. e2735 ◽

Cited By ~ 16

Author(s):

Sara Arana-Peña ◽

Yuliya Lokha ◽

Roberto Fernández-Lafuente

Keyword(s):

Immobilized Lipase ◽

Candida Antarctica ◽

Lipase B ◽

Agarose Beads ◽

Lipase A

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Kinetic model of biodiesel production using immobilized lipase Candida antarctica lipase B

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/j.molcatb.2012.09.011 ◽

2013 ◽

Vol 85-86 ◽

pp. 156-168 ◽

Cited By ~ 36

Author(s):

Sergey N. Fedosov ◽

Jesper Brask ◽

Anders K. Pedersen ◽

Mathias Nordblad ◽

John M. Woodley ◽

...

Keyword(s):

Kinetic Model ◽

Immobilized Lipase ◽

Candida Antarctica ◽

Biodiesel Production ◽

Candida Antarctica Lipase B ◽

Candida Antarctica Lipase ◽

Lipase B

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Influence of Glutaraldehyde Cross-Linking Modes on the Recyclability of Immobilized Lipase B from Candida antarctica for Transesterification of Soy Bean Oil

Molecules ◽

10.3390/molecules23092230 ◽

2018 ◽

Vol 23 (9) ◽

pp. 2230 ◽

Cited By ~ 13

Author(s):

Iago A. Modenez ◽

Diego Sastre ◽

Fernando C. Moraes ◽

Caterina Marques Netto

Keyword(s):

Magnetic Nanoparticles ◽

Immobilized Lipase ◽

Carbon Chain ◽

Candida Antarctica ◽

Cross Linking ◽

Carbon Chain Length ◽

Lipase B ◽

Factors Affecting ◽

Michael Type Addition ◽

Nanoparticle Agglomerate

Lipase B from Candida antarctica (CAL-B) is largely employed as a biocatalyst for hydrolysis, esterification, and transesterification reactions. CAL-B is a good model enzyme to study factors affecting the enzymatic structure, activity and/or stability after an immobilization process. In this study, we analyzed the immobilization of CAL-B enzyme on different magnetic nanoparticles, synthesized by the coprecipitation method inside inverse micelles made of zwitterionic surfactants, with distinct carbon chain length: 4 (ImS4), 10 (ImS10) and 18 (ImS18) carbons. Magnetic nanoparticles ImS4 and ImS10 were shown to cross-link to CAL-B enzyme via a Michael-type addition, whereas particles with ImS18 were bond via pyridine formation after glutaraldehyde cross-coupling. Interestingly, the Michael-type cross-linking generated less stable immobilized CAL-B, revealing the influence of a cross-linking mode on the resulting biocatalyst behavior. Curiously, a direct correlation between nanoparticle agglomerate sizes and CAL-B enzyme reuse stability was observed. Moreover, free CAL-B enzyme was not able to catalyze transesterification due to the high methanol concentration; however, the immobilized CAL-B enzyme reached yields from 79.7 to 90% at the same conditions. In addition, the transesterification of lipids isolated from oleaginous yeasts achieved 89% yield, which confirmed the potential of immobilized CAL-B enzyme in microbial production of biodiesel.

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Thermal stabilization of immobilized lipase B from Candida antarctica on different supports: Effect of water activity on enzymatic activity in organic media

Enzyme and Microbial Technology ◽

10.1016/s0141-0229(98)00067-2 ◽

1999 ◽

Vol 24 (1-2) ◽

pp. 3-12 ◽

Cited By ~ 130

Author(s):

Miguel Arroyo ◽

José Marı́a Sánchez-Montero ◽

José Vicente Sinisterra

Keyword(s):

Enzymatic Activity ◽

Water Activity ◽

Immobilized Lipase ◽

Thermal Stabilization ◽

Candida Antarctica ◽

Organic Media ◽

Lipase B ◽

Effect Of Water

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Screening of solvents for favoring hydrolytic activity of Candida antarctica Lipase B

Bioprocess and Biosystems Engineering ◽

10.1007/s00449-019-02252-0 ◽

2019 ◽

Vol 43 (4) ◽

pp. 605-613 ◽

Cited By ~ 4

Author(s):

Bartłomiej Zieniuk ◽

Agata Fabiszewska ◽

Ewa Białecka-Florjańczyk

Keyword(s):

Hydrolytic Activity ◽

Candida Antarctica ◽

Candida Antarctica Lipase B ◽

Candida Antarctica Lipase ◽

Lipase B

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Outperformance in Acrylation: Supported D-Glucose-Based Ionic Liquid Phase on MWCNTs for Immobilized Lipase B from Candida antarctica as Catalytic System

Materials ◽

10.3390/ma14113090 ◽

2021 ◽

Vol 14 (11) ◽

pp. 3090

Author(s):

Anna Szelwicka ◽

Karol Erfurt ◽

Sebastian Jurczyk ◽

Slawomir Boncel ◽

Anna Chrobok

Keyword(s):

Ionic Liquid ◽

Ionic Liquids ◽

Liquid Phase ◽

Acrylic Acid ◽

Butyl Acrylate ◽

Promising Result ◽

Immobilized Lipase ◽

Candida Antarctica ◽

Molar Ratio ◽

Lipase B

This study presents a highly efficient method of a synthesis of n-butyl acrylate via esterification of acrylic acid and n-butanol in the presence of supported ionic liquid phase (SILP) biocatalyst consisting of the lipase B from Candida antarctica (CALB) and multi-walled carbon nanotubes (MWCNTs) modified by D-glucose-based ionic liquids. Favorable reaction conditions (acrylic acid: n-butanol molar ratio 1:2, cyclohexane as a solvent, biocatalyst 0.150 g per 1 mmol of acrylic acid, temperature 25 °C) allowed the achievement of a 99% yield of n-butyl acrylate in 24 h. Screening of various ionic liquids showed that the most promising result was obtained if N-(6-deoxy-1-O-methoxy-α-D-glucopyranosyl)-N,N,N-trimethylammonium bis-(trifluoromethylsulfonyl)imide ([N(CH3)3GlcOCH3][N(Tf)2]) was selected in order to modify the outer surface of MWCNTs. The final SILP biocatalyst–CNTs-[N(CH3)3GlcOCH3][N(Tf)2]-CALB contained 1.8 wt.% of IL and 4.2 wt.% of CALB. Application of the SILP biocatalyst led to the enhanced activity of CALB in comparison with the biocatalyst prepared via physical adsorption of CALB onto MWCNTs (CNTs-CALB), as well as with commercially available Novozyme 435. Thus, the crucial role of IL in the stabilization of biocatalysts was clearly demonstrated. In addition, a significant stability of the developed biocatalytic system was confirmed (three runs with a yield of ester over 90%).

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