Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry

2016 ◽  
Vol 96 (12) ◽  
pp. 4281-4287 ◽  
Author(s):  
Jovana Trbojević Ivić ◽  
Dušan Veličković ◽  
Aleksandra Dimitrijević ◽  
Dejan Bezbradica ◽  
Vladimir Dragačević ◽  
...  
Keyword(s):  
Potential Application ◽  
Food Industry ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Immobilized Candida Rugosa Lipase

Optimization of immobilized Candida rugosa lipase LIP2-catalyzed resolution to produce l-menthyl acetate

2009 ◽  
pp. 1-7
Author(s):  
Hsiao-Ching Chen ◽  
Yi-Ting Liang ◽  
Jiann-Hwa Chen ◽  
Cheng-Chang ◽  
Chwen-Jen Shieh
Keyword(s):  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Immobilized Candida Rugosa Lipase

scholarly journals Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C

Biocatalysis ◽  
2014 ◽  
Vol 1 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Daniele Spinelli ◽  
Simone Coppi ◽  
Riccardo Basosi ◽  
Rebecca Pogni
Keyword(s):  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Product Yield ◽  
Candida Rugosa Lipase ◽  
Maximum Activity ◽  
Ethyl Butyrate ◽  
Molar Ratio ◽  
Practical Applications ◽  
Solvent Free Conditions ◽  
Immobilized Candida Rugosa Lipase

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.

scholarly journals Response surface methodology for optimizing the glycerolysis reaction of olive oil by Candida rugosa lipase

2014 ◽  
Vol 20 (1) ◽  
pp. 127-134 ◽  
Author(s):  
Kumar Singh ◽  
Mausumi Mukhopadhyay
Keyword(s):  
Response Surface Methodology ◽  
Reaction Time ◽  
Olive Oil ◽  
Water Content ◽  
Response Surface ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Molar Ratio ◽  
Immobilized Candida Rugosa Lipase ◽  
Central Composite

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.

scholarly journals Investigating Enzyme Activity of Immobilized Candida rugosa Lipase

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Bhagya Sri Kaja ◽  
Stephen Lumor ◽  
Samuel Besong ◽  
Bettina Taylor ◽  
Gulnihal Ozbay
Keyword(s):  
Milk Fat ◽  
Candida Rugosa ◽  
Catalytic Efficiency ◽  
Hydrolytic Activity ◽  
Candida Rugosa Lipase ◽  
Support Materials ◽  
Fatty Acid Chain ◽  
Hydrolytic Activities ◽  
Immobilized Candida Rugosa Lipase ◽  
Immobilization Techniques

Candida rugosa lipase is a food-grade enzyme that is extensively utilized in the dairy processing industry for milk fat hydrolysis. The enzyme is mainly employed to modify the fatty acid chain length that results in the enhancement of flavors. The hydrolytic activities of C. rugosa lipase (fungal source) in its free and immobilized forms were investigated at different pH and temperature settings. The main objective of this study was to understand how different support materials (Celite-545, Sephadex G-25, and chitosan) and immobilization techniques alter lipase activity and stability. Our results indicated that hydrolytic activity increased significantly with immobilization on Celite-545. In general, immobilization resulted in considerable improvements in the stability of the enzyme with variations in pH and temperature. Immobilization on Celite-545 led to the highest catalytic efficiency. Remarkable improvements in the recovery and reusability of the immobilized lipases were noted. Comparatively, the acetone immobilization procedure resulted in higher activities than alcohol immobilization. In conclusion, the activity of C. rugosa lipase was enhanced most significantly when immobilized on Celite-545 using acetone as an adsorption solvent.

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