Stability of protein-coated microcrystals in organic solvents

Kreiner, M.; Fernandes, João F. Amorim; O'Farrell, Norah; Halling, Peter J.; Parker, Marie Claire

doi:10.1016/j.molcatb.2005.03.002

Cited by 19 publications

(10 citation statements)

References 25 publications

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“…71 It has also been shown that CALB-PCMCs lost only 10% of their activity after storage as a suspension in propanol with 1% water for one year, while the corresponding preparation of a Pseudomonas lipase lost about 50% of its activity during the same time. 72 When different excipients and precipitating solvents were evaluated in the preparation of PCMCs from BCL, it was found that potassium sulphate and acetone provided the catalysts with the highest activity in the ethanolysis of a vegetable oil. 73 In most reported studies, the enzyme molecules in PCMCs were not cross-linked.…”

Section: Adsorptionmentioning

confidence: 99%

Immobilisation and application of lipases in organic media

2013

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Different methods of preparing lipases for use in organic media are critically reviewed. Solid lipase preparations can be made by typical immobilisation methods such as adsorption, entrapment, covalent coupling or cross-linking. Immobilisation is especially attractive for lipases because, in addition to the normal benefits of enzyme immobilisation, it can also lead to a considerable increase in catalytic activity, probably caused by conformational changes in the lipase molecules. Activation can be achieved, for example, using hydrophobic support materials or surfactants during the immobilisation procedure. Surfactants can also be used to solubilise lipases in organic media via the formation of hydrophobic ion pairs, surfactant-coated lipase or reversed micelles. Lipase preparation methods are discussed with regard to potential lipase inactivation and activation effects, mass transfer limitations, lipase stability and other features important for applications. The practical applications of lipases in organic media reviewed include ester synthesis, modification of triacylglycerols and phospholipids, fatty acid enrichment, enantiomer resolution, biodiesel production and acylation of carbohydrates and bioactive compounds.

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Section: Adsorptionmentioning

confidence: 99%

Immobilisation and application of lipases in organic media

2013

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“…Protein-coated microcrystals (PCMCs) have been reported as an alternative biocatalyst design with great potential for catalysis in nonaqueous systems e.g. biodiesel synthesis and kinetic resolution of enantiomers in organic solvents [20,21]. PCMCs are characterized as a uniform enzyme layer on the surface of micron-sized salt crystals, which can be prepared by co-precipitation of enzyme and salt in an organic solvent.…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic ethanolysis of palm oil for biodiesel production using microcrystalline lipase in tert-butanol system

Raita

Champreda

Laosiripojana

2010

Process Biochemistry

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“…3.0 (citric acid) 4.0 (citric acid) 5.0 (citric acid) 6.0 (PBS) 7.0 (PBS) 8.0 (PBS) 9.0 (glycine-NaOH) 10.0 (glycine-NaOH) 11.0 (glycine-NaOH) 12.0 (glycine-NaOH) …”

Section: Hplc Analysis and Quantificationmentioning

confidence: 99%

“…Shah and Gupta have used PCMCs of Candida rugosa lipase (CRL) and Burkholderia cepacia lipase for kinetic resolution of (±)-phenylethanol by transesterification with vinylacetate in ionic liquid [BMIM][PF6] [10]. Subtilisin Carlsberg also showed that PCMCs enable 100-fold higher initial rates than "pH-tuned" freeze-dried enzyme [11].…”

Section: Introductionmentioning

confidence: 99%

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

Huang

et al. 2015

Appl Biochem Biotechnol

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In this study, an economical heterogeneous biocatalyst, protein-coated microcrystals (PCMCs), was prepared from a commercial Candida rugosa lipase (CRL) and used for catalyzing esterification of (R, S)-ibuprofen enantiomers with isooctanol in isooctane. The main variables controlling the process (precipitating solvents, pH, saturated K2SO4 solution, and water content) were optimized via single-factorial experiments. Under optimum conditions, the enantiomeric excess of active S(+)-ibuprofen and total conversion rate were 97.34 and 49.83 %, respectively, and the corresponding enzyme (PCMC-CRL) activity attained 387.29 μmol/min/g protein, a 5.78-fold enhancement over the free lipase powder. Additionally, the thermostability, organic-solvent tolerance, and operational stability of PCMC-CRL were greatly improved as compared to the free enzyme. Fourier transform infrared (FTIR) spectroscopy was employed to reveal the correlation between conformation and enzyme activity enhancement. Moreover, the PCMC-CRL retained most of its original activity following use in more than 15 successive batches, suggesting that it exhibits adequate operational stability. These results indicate that PCMC-CRL is of great potential use in industrial applications.

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Stability of protein-coated microcrystals in organic solvents

Cited by 19 publications

References 25 publications

Immobilisation and application of lipases in organic media

Immobilisation and application of lipases in organic media

Biocatalytic ethanolysis of palm oil for biodiesel production using microcrystalline lipase in tert-butanol system

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

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