Protein-Coated Microcrystals from Candida rugosa Lipase: Its Immobilization, Characterization, and Application in Resolution of Racemic Ibuprofen

Huang, Shuangshuang; Li, Xiang; Xu, Li; Ke, Changbin; Zhang, Rui; Yan, Yunjun

doi:10.1007/s12010-015-1725-9

Cited by 12 publications

(6 citation statements)

References 38 publications

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“…Previous studies indicated that the second derivative FT-IR spectra in the amide I region of an enzyme was used as a particularly sensitive probe of protein conformation 19 20 21 . To date, there have also been some reports on the use of the second derivative FT-IR spectra to study the conformational changes of an enzyme after immobilization 22 23 24 25 . Therefore, it was of great interest to comparatively investigate the secondary structure contents of PCL and PCL@MCNC and their conformational changes using FT-IR spectra to get some insight of the stabilization mechanism of the immobilized enzyme PCL@MCNC.…”

Section: Resultsmentioning

confidence: 99%

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Cao

Huang

et al. 2016

Sci Rep

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Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading (82.2 mg enzyme/g) and activity recovery (95.9%). Compared with free PCL, PCL@MCNC exhibited significantly enhanced stability and solvent tolerance, due to the increase of enzyme structure rigidity. The observable optimum pH and temperature for PCL@MCNC were higher than those of free PCL. PCL@MCNC manifested relatively higher enzyme-substrate affinity and catalytic efficiency. Moreover, PCL@MCNC was capable of effectively catalyzing asymmetric hydrolysis of ketoprofenethyl ester with high yield of 43.4% and product e.e. of 83.5%. Besides, immobilization allowed PCL@MCNC reuse for at least 6 consecutive cycles retaining over 66% of its initial activity. PCL@MCNC was readily recycled by magnetic forces. Remarkably, the as-prepared nanobiocatalyst PCL@MCNC is promising for biocatalysis.

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Section: Resultsmentioning

confidence: 99%

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Cao

Huang

et al. 2016

Sci Rep

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“…Later, Kim and co‐workers reported the accomplishment of lipase activation through lyophilization with ionic liquids or ionic surfactants [45–48]. Koo and co‐workers also reported efficient activation of lipase through lyophilizaton of ionic liquid type sol‐gel silica [49]; similar activation methods have been demonstrated by several groups [50–57].…”

Section: Introductionmentioning

confidence: 79%

Phosphonium alkyl PEG sulfate ionic liquids as coating materials for activation of Burkholderia cepacia lipase

Matsubara

Kadotani

Nishihara

et al. 2015

Biotechnology Journal

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Lipases are among the most widely used enzymes applicable for various substrates; however, the slow reactions or poor enantioselective reactions are sometimes obtained. To develop ionic liquid type activating agents for lipase, four types of phosphonium cetyl(PEG)10 sulfate ionic liquids have been synthesized and used as coating materials of Burkholderia cepacia lipase (Lipase PS) through the lyophilization process. Tributyl ([2-methoxy]ethoxymethyl)phosphonium cetyl(PEG)10 sulfate ([P444MEM ][C16 (PEG)10 SO4 ]) (PL1) worked best among them, and PL1-coated lipase PS displayed high reactivity in transesterification of broad types of secondary alcohols using vinyl acetate as an acylating reagent with perfect enantioselectivity (E > 200). The substrate preference of PL1-PS differs from that of commercial lipase PS or [bdmim] [C16 (PEG)10 SO4 ]-coated lipase (IL1-PS); PL1-PS displayed excellent enantioselectivity in the reaction of 2-chloro-1-phenylethanol with E > 200, though insufficient E values were recorded for lipase PS (E = 12) and IL1-PS (E = 123) for this alcohol. PL1-PS also showed perfect enantioselectivity (E > 200) for the reaction of 1-(pyridin-2-yl)ethanol, while IL1-PS showed E = 130 for this compound. We further succeeded in demonstrating the recyclable use of PL1-PS five times in tributyl(3-methoxypropyl)phosphonium bis(trifluoromethylsulfonyl)amide ([P444PM ][Tf2 N]) as a solvent. Since PL1-PS is easily applicable to 10-20 gram-scaled reactions, it is expected that the IL-coated enzyme might be useful for practical preparation of a wide variety of chiral secondary alcohols.

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“…After optimization, a yield of 80% in 1 h was obtained, clearly surpassing the results obtained with the commercial Lipozyme RM-IL [136]. In another contribution, lipase from Candida rugosa was used to produce PCMCs [137]. The preparation of the biocatalysts was optimized via single-factorial experiments (the studied variables were precipitating solvents, pH, saturated K 2 SO 4 solution, and water content).…”

Section: Immobilization Of Enzyme By Protein-coated Microcrystals (Pcmentioning

confidence: 91%

Enzyme-Coated Micro-Crystals: An Almost Forgotten but Very Simple and Elegant Immobilization Strategy

et al. 2020

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The immobilization of enzymes using protein coated micro-crystals (PCMCs) was reported for the first time in 2001 by Kreiner and coworkers. The strategy is very simple. First, an enzyme solution must be prepared in a concentrated solution of one compound (salt, sugar, amino acid) very soluble in water and poorly soluble in a water-soluble solvent. Then, the enzyme solution is added dropwise to the water soluble solvent under rapid stirring. The components accompanying the enzyme are called the crystal growing agents, the solvent being the dehydrating agent. This strategy permits the rapid dehydration of the enzyme solution drops, resulting in a crystallization of the crystal formation agent, and the enzyme is deposited on this crystal surface. The reaction medium where these biocatalysts can be used is marked by the solubility of the PCMC components, and usually these biocatalysts may be employed in water soluble organic solvents with a maximum of 20% water. The evolution of these PCMC was to chemically crosslink them and further improve their stabilities. Moreover, the PCMC strategy has been used to coimmobilize enzymes or enzymes and cofactors. The immobilization may permit the use of buffers as crystal growth agents, enabling control of the reaction pH in the enzyme environments. Usually, the PCMC biocatalysts are very stable and more active than other biocatalysts of the same enzyme. However, this simple (at least at laboratory scale) immobilization strategy is underutilized even when the publications using it systematically presented a better performance of them in organic solvents than that of many other immobilized biocatalysts. In fact, many possibilities and studies using this technique are lacking. This review tried to outline the possibilities of this useful immobilization strategy.

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Protein-Coated Microcrystals from Candida rugosa Lipase: Its Immobilization, Characterization, and Application in Resolution of Racemic Ibuprofen

Cited by 12 publications

References 38 publications

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Phosphonium alkyl PEG sulfate ionic liquids as coating materials for activation of Burkholderia cepacia lipase

Enzyme-Coated Micro-Crystals: An Almost Forgotten but Very Simple and Elegant Immobilization Strategy

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