The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study

Bezbradica, Dejan; Mijin, Dušan Ž.; Šiler-Marinković, Slavica; Knežević, Zorica

doi:10.1016/j.molcatb.2005.10.004

Cited by 74 publications

(54 citation statements)

References 32 publications

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“…Using free Candida rugosa lipase, similar activity values (0.005-0.060 mM/min-g protein) were obtained for amyl alcohol and butyric acid esterification in iso-octane [59].…”

Section: Protein Load and Esterification Activitysupporting

confidence: 53%

Preparation and characterization of chitosan membranes by using a combined freeze gelation and mild crosslinking method

Orrego

Valencia

2008

Bioprocess Biosyst Eng

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When gelification is performed by freezing-thawing repeated cycles, the resultant gel-like polymer systems are called cryogels. This work aims to assess the effect of the addition of glutaraldehyde and 18 Crown Ether-6 on surface properties and protein loading of dried chitosan cryogel films. Residual water content of treated chitosan membranes ranged between 11.93 and 13.86%, while their water activities vary from 0.5 to 0.7 (measured from 4 to 60 degrees C). Based on thermal data, water evaporation peak and degradation temperatures of chitosan membranes shifted to a higher temperature for crosslinked samples. X-ray diffractograms provide high values of crystallinity for all the samples (70.67-92.86%), the highest value being for the glutaraldehyde-treated membrane. Candida rugosa lipase can be immobilized successfully on chitosan membranes. Lipase immobilized on glutaraldehyde-crosslinked chitosan yielded the highest efficiency in terms of total coupled protein and protein loading efficiency.

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“…Using free Candida rugosa lipase, similar activity values (0.005-0.060 mM/min-g protein) were obtained for amyl alcohol and butyric acid esterification in iso-octane [59].…”

Section: Protein Load and Esterification Activitysupporting

confidence: 53%

Preparation and characterization of chitosan membranes by using a combined freeze gelation and mild crosslinking method

Orrego

Valencia

2008

Bioprocess Biosyst Eng

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“…The optimum temperature for lipase activity was observed at 40°C. This value is in agreement with the optimal temperatures reported for free and immobilized C. rugosa lipase catalyzed esterifications in non aqueous media for the synthesis of butyl oleate in hexane, 40°C [28], amyl isobutyrate in iso-octane, 45°C [34] and citronellyl laurate in iso-octane, 37°C [35].…”

Section: Optimum Reaction Temperaturesupporting

confidence: 90%

Candida rugosa Lipase Supported on High Crystallinity Chitosan as Biocatalyst for the Synthesis of 1-Butyl Oleate

2009

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Lipase from Candida rugosa was immobilized onto chitosan using four different protocols. The variation of crystallinity (5.57-92.86%), which was a result of thermal treatments and crosslinking of the chitosan, influenced the protein load (7.46-25.15 mg g -1 chitosan) and protein load efficiency (21.67-41.68%) for immobilization assays made with identical lipase solution concentration (1.3 mg of protein/mL). The effects of protein load (10, 30, 50 and 70 mg of lipase), reaction temperature (30, 40, 50, 60, 70°C) and substrates molar ratio (0.05-0.30 M) have been studied in the butyl oleate synthesis in iso-octane when water activity of the free and immobilized enzymes were fixed around 0.53 ± 0.04. The catalytic activity of the immobilized lipase has also been tested. The Ping-Pong bi-bi mechanism with dead end complex of n-butanol was found to fit the initial rate data. The values of the apparent kinetic parameters were determined by graphic and parametric method as: V max = 18.2-19.0 mmol min -1 g -1 ; K M; Acid = 0.599-0.640 mol L -1 ; K M; Alcohol = 0.128-0.149 mol L -1 ; and K i; Alcohol = 1.933 mol L -1 .

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“…Wu et al [23] reported an esterification reaction catalyzed by surfactant-coated C. rugosa lipase in iso-octane to be successful. Other literature also reported that the use of iso-octane as the media for esterification or transesterification reaction was successful when C. rugosa lipase was employed [3,[22][23][24][25]. All subsequent experiments to be discussed in the successive sections were conducted using 60 g/L of immobilized lipase in iso-octane as solvent.…”

Section: Effect Of Different Solventsmentioning

confidence: 99%

Studies of reaction parameters on synthesis of Citronellyl laurate ester via immobilized Candida rugosa lipase in organic media

Serri

Kamaruddin

Long

2006

Bioprocess Biosyst Eng

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Immobilized Candida rugosa lipase was used for the synthesis of citronellyl laurate from citronellol and lauric acid. Screening of different types of support (Amberlite MB-1 and Celite) for immobilization of lipase and solvent (n-hexane, n-heptane, and iso-octane) and optimization of reaction conditions, such as catalyst loading, effect of substrates molar ratio and temperature, have been studied. The maximum enzyme activity was obtained at 310 K. The immobilized C. rugosa lipase onto Amberlite MB-1 support was found to be the best support with a conversion of 89% of citronellyl laurate ester in iso-octane compared to Celite 545. Deactivation of C. rugosa lipase at 313, 318 and 323 K were observed. Ordered bi bi mechanism with dead end complex of lauric acid was found to fit the initial rate data and the kinetic parameters were obtained by non-linear regression analysis.

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The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study

Cited by 74 publications

References 32 publications

Preparation and characterization of chitosan membranes by using a combined freeze gelation and mild crosslinking method

Preparation and characterization of chitosan membranes by using a combined freeze gelation and mild crosslinking method

Candida rugosa Lipase Supported on High Crystallinity Chitosan as Biocatalyst for the Synthesis of 1-Butyl Oleate

Studies of reaction parameters on synthesis of Citronellyl laurate ester via immobilized Candida rugosa lipase in organic media

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