Enantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase

Majumder, Abir B.; Shah, Shweta; Gupta, Munishwar N.

doi:10.1186/1752-153x-1-10

Cited by 17 publications

(8 citation statements)

References 17 publications

(29 reference statements)

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“…The kinetic resolution of racemates to obtain chiral compounds has emerged as a major application of enzymes [ 15 - 19 , 29 ]. Table 4 shows that free enzyme showed poor transesterification rates during kinetic resolution of (±) 1-phenyl ethanol.…”

Section: Resultsmentioning

confidence: 99%

Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes

Shah

Solanki

Gupta

2007

Chemistry Central Journal

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BackgroundImmobilization of biologically active proteins on nanosized surfaces is a key process in bionanofabrication. Carbon nanotubes with their high surface areas, as well as useful electronic, thermal and mechanical properties, constitute important building blocks in the fabrication of novel functional materials.ResultsLipases from Candida rugosa (CRL) were found to be adsorbed on the multiwalled carbon nanotubes with very high retention of their biological activity (97%). The immobilized biocatalyst showed 2.2- and 14-fold increases in the initial rates of transesterification activity in nearly anhydrous hexane and water immiscible ionic liquid [Bmim] [PF6] respectively, as compared to the lyophilized powdered enzyme. It is presumed that the interaction with the hydrophobic surface of the nanotubes resulted in conformational changes leading to the 'open lid' structure of CRL. The immobilized enzyme was found to give 64% conversion over 24 h (as opposed to 14% with free enzyme) in the formation of butylbutyrate in nearly anhydrous hexane. Similarly, with ionic liquid [Bmim] [PF6], the immobilized enzyme allowed 71% conversion as compared to 16% with the free enzyme. The immobilized lipase also showed high enantioselectivity as determined by kinetic resolution of (±) 1-phenylethanol in [Bmim] [PF6]. While free CRL gave only 5% conversion after 36 h, the immobilized enzyme resulted in 37% conversion with > 99% enantiomeric excess. TEM studies on the immobilized biocatalyst showed that the enzyme is attached to the multiwalled nanotubes.ConclusionSuccessful immobilization of enzymes on nanosized carriers could pave the way for reduced reactor volumes required for biotransformations, as well as having a use in the construction of miniaturized biosensensor devices.

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Section: Resultsmentioning

confidence: 99%

Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes

Shah

Solanki

Gupta

2007

Chemistry Central Journal

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“…FTIR has been used to prove that enzyme conformation can be retained if freeze drying is replaced by solvent rinsing [109]. However, freeze drying of samples are still widely used [51,107] and can cause structural changes not observed when the immobilized enzymes are in solution.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Carlsson

Gustafsson

Thörn

et al. 2014

Advances in Colloid and Interface Science

219

167

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“…However, after propanol rinsing of immobilised RML, a preparation with an a-helical content similar to that of the native enzyme and good catalytic performance was obtained. 70 2.2.5 Protein-coated microcrystals. One way to obtain highly active enzyme preparations in organic media is to prepare protein-(enzyme-) coated microcrystals (PCMCs).…”

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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Enantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase

Cited by 17 publications

References 17 publications

Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes

Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Immobilisation and application of lipases in organic media

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