Borago officinalis oil: Fatty acid fractionation by immobilized Candida rugosa lipase

1999 ◽  
Vol 76 (5) ◽  
pp. 557-562 ◽  
Author(s):  
Murielle Schmitt-Rozieres ◽  
Guillaume Vanot ◽  
Valérie Deyris ◽  
Louis-Claude Comeau
Author(s):  
Hsiao-Ching Chen ◽  
Yi-Ting Liang ◽  
Jiann-Hwa Chen ◽  
Cheng-Chang ◽  
Chwen-Jen Shieh

2016 ◽  
Vol 78 (5-6) ◽  
Author(s):  
Mohd Basyaruddin Abdul Rahman ◽  
Siti Salhah Othman ◽  
Noor Mona Md Yunus

The enzymatic selectivity of Lipase from Candida rugosa immobilized onto a calcined layered double hydroxide (CLDHs-CRL) towards the chain-length of fatty acids and alcohols in the synthesis of fatty acid esters was investigated.  The results showed that CMAN-CRL catalyzed the esterification process with fatty acids of medium chain lengths (C10-C14) effectively while, CNAN-CRL and CZAN-CRL exhibited high percentage conversion in fatty acids with carbon chain lengths of C8-C12 and C10-C18, respectively. In the alcohol selectivity study, CMAN-CRL showed high selectivity toward alcohols with carbon chain lengths of C4, C6 and C10.  On the other hand, both CNAN-CRL and CZAN-CRL exhibited rather low selectivity towards longer carbon chain length of alcohols. 


Biocatalysis ◽  
2014 ◽  
Vol 1 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Daniele Spinelli ◽  
Simone Coppi ◽  
Riccardo Basosi ◽  
Rebecca Pogni

AbstractLipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry.


2016 ◽  
Vol 96 (12) ◽  
pp. 4281-4287 ◽  
Author(s):  
Jovana Trbojević Ivić ◽  
Dušan Veličković ◽  
Aleksandra Dimitrijević ◽  
Dejan Bezbradica ◽  
Vladimir Dragačević ◽  
...  

2014 ◽  
Vol 20 (1) ◽  
pp. 127-134 ◽  
Author(s):  
Kumar Singh ◽  
Mausumi Mukhopadhyay

In the present work, solvent free olive oil glycerolysis for the monoglycerides (MG) and diglycerides (DG) production with an immobilized Candida rugosa lipase was studied. MG and DG production were optimized using experiment design techniques and response surface methodology (RSM). RSM based on five-level, a five-variable central composite design (CCD) was used to optimize MG and DG production: reaction time, temperature, molar ratio of glycerol to oil, amount of lipase, and water content in glycerol. The reaction time, temperature, and amount of lipase were observed to be the most significant factors on the process response. The immobilized Candida rugosa lipase revealed optimum yield of MG and DG as 38.71 and 40.45 wt% respectively following a 5h reaction time with 0.025 g of lipase and 5% water content in glycerol at 40?C temperature. The yield of MG and DG production can be enhanced 1.5 fold by RSM.


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