Lipase catalyzed synthesis of flavor esters in non-aqueous media: Optimization of the yield of pentyl 2-methylpropanoate by statistical analysis

Knežević‐Jugović, Zorica; Bezbradica, Dejan; Jakovljević, Živana; Brankovic-Dimitrijevic, Suzana; Mijin, Dušan Ž.

doi:10.2298/jsc0812139k

Cited by 17 publications

(13 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The initial water content (0.1-0.9% w/v), reaction temperature (25-65ºC), enzyme loading (16-60 mg g -1 ), acid/alcohol molar ratio (1:2-5:2) and time of addition of molecular sieves (0-20 hrs) were the variables investigated. These variables were chosen based on the results obtained in a preliminary study and are the most commonly used for modeling esterification reactions (Krishna et al 2000;Chiang et al 2003;Knežević-Jugović et al 2008).The ester yield in mol% (Y%) was taken as the response variable.…”

Section: Esterification Reaction In a Batch Reactor Systemmentioning

confidence: 99%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

View full text Add to dashboard Cite

Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion (> 99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g -1 dry support and in a relatively short time (24 hrs) at 37ºC, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.

show abstract

Section: Esterification Reaction In a Batch Reactor Systemmentioning

confidence: 99%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

View full text Add to dashboard Cite

show abstract

“…With respect to lipase catalyzed esterification reactions, RSM has been applied for certain systems such as those using free enzyme [46], enzyme immobilized in alginate beads [42], and adsorbed enzyme [47]. However, RSM has not been applied for studying the various interactions of process parameters regarding ester synthesis using lipase immobilized in MBGs.…”

Section: Resultsmentioning

confidence: 99%

Biocatalytic Synthesis of Flavor Ester “Pentyl Valerate” UsingCandida rugosaLipase Immobilized in Microemulsion Based Organogels: Effect of Parameters and Reusability

Raghavendra

Panchal

Divecha

et al. 2014

BioMed Research International

View full text Add to dashboard Cite

Pentyl valerate was synthesized biocatalytically using Candida rugosa lipase (CRL) immobilized in microemulsion based organogels (MBGs). The optimum conditions were found to be pH 7.0, temperature of 37°C, ratio of concentration of water to surfactant (Wo) of 60, and the surfactant sodium bis-2-(ethylhexyl)sulfosuccinate (AOT) for MBG preparation. Although kinetic studies revealed that the enzyme in free form had high affinity towards substrates (K m = 23.2 mM for pentanol and 76.92 mM for valeric acid) whereas, after immobilization, the K m values increased considerably (74.07 mM for pentanol and 83.3 mM for valeric acid) resulting in a slower reaction rate, the maximum conversion was much higher in case of immobilized enzyme (~99%) as compared to free enzyme (~19%). Simultaneous effects of important parameters were studied using response surface methodology (RSM) conjugated with Box-Behnken design (BBD) with five variables (process parameters), namely, enzyme concentration, initial water content (Wo), solvent used for MBG preparation, substrate ratio and time, and response as the final product formation, that is, pentyl valerate (%). The MBGs were reused for 10 consecutive cycles for ester synthesis. Efficacy of AOT/isooctane as dehydrating agent for extracting excess water from MBGs was found to exert a positive effect on the esterification reaction.

show abstract

“…A reaction time of 26.87 h gave maximum yield 24.32 of ethyl lactate synthesized from commercial lipase Novozyme 435 under optimal conditions 29 . Conversion of 92 was achieved in the synthesis of pentyl 2-methylpropanoate using Candida rugosa lipase in a relatively short time of 26 h at 35 33 . The synthesis of geranyl butyrate using Pseudomonas aeruginosa MTCC-4713 immobilised lipase was increased by increasing reaction time to 15 h 99.1 mM 31 .…”

Section: Effect Of Incubation Time On Synthesis Of Ethyl Lactatementioning

confidence: 99%

Application of Lipase Purified from <i>Aspergillus fumigatus</i> in the Syntheses of Ethyl Acetate and Ethyl Lactate

et al. 2020

View full text Add to dashboard Cite

Introduction Lipases triacylglycerol ester hydrolases E.C. 3.1.1.3 are ubiquitous enzymes that catalyse the breakdown of fats and oils with subsequent release of free fatty acid, diacylglycerol, monoacylglycerol and glycerol 1 4. They are found in animals, plants, fungi and bacteria and are of considerable physiological significance and industrial potential 5. However, the most suitable sources for lipase production are the microorganisms which can produce high quality lipases in lower cost and shorter time 6. Fungi are more preferred sources of lipases because of their stability at different temperature and pH 7. Purification of enzymes allows successful determination of their primary amino acid sequence and three-dimensional structure. Purified lipase preparations are needed in industries employing the enzymes for the biocatalytic production of food additives flavour modifying enzymes , industrial reagents glyceride hydrolyzing enzyme , stain removing agents detergent additives , digestive drugs, diagnostic enzymes in medical applications, nutraceuticals, surfactants and additives in cosmetics 8 10. Esters of short chain carboxylic acid and alcohols belong to the highly important natural aroma compounds. The production of natural aroma compounds by fermentation and enzymatic reactions in aqueous 11 , organic solvent 12, 13

show abstract

Lipase catalyzed synthesis of flavor esters in non-aqueous media: Optimization of the yield of pentyl 2-methylpropanoate by statistical analysis

Cited by 17 publications

References 29 publications

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Biocatalytic Synthesis of Flavor Ester “Pentyl Valerate” UsingCandida rugosaLipase Immobilized in Microemulsion Based Organogels: Effect of Parameters and Reusability

Application of Lipase Purified from <i>Aspergillus fumigatus</i> in the Syntheses of Ethyl Acetate and Ethyl Lactate

Contact Info

Product

Resources

About