Optimization of isoamyl acetate production by using immobilized lipase from Mucor miehei by response surface methodology

Krishna, S. Hari; Manohar, B.; Divakar, Soundar; Prapulla, S. G.; Karanth, N. G.

doi:10.1016/s0141-0229(99)00149-0

Cited by 103 publications

(53 citation statements)

References 10 publications

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“…Various enzyme sources either in the form of free lipases [19,20] or immobilized lipases [9,21] have been used for production of flavor acetates in organic solvents. The effect The esterification reaction was carried out using alcohol/acid molar ratio of 1.6 with 100 g/l of mycelium bound lipase.…”

Section: Discussionmentioning

confidence: 99%

Lipase of Aspergillus niger NCIM 1207: A Potential Biocatalyst for Synthesis of Isoamyl Acetate

2010

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Commercial lipase preparations and mycelium bound lipase from Aspergillus niger NCIM 1207 were used for esterification of acetic acid with isoamyl alcohol to obtain isoamyl acetate. The esterification reaction was carried out at 30°C in n-hexane with shaking at 120 rpm. Initial reaction rates, conversion efficiency and isoamyl acetate concentration obtained using Novozyme 435 were the highest. Mycelium bound lipase of A. niger NCIM 1207 produced maximal isoamyl acetate formation at an alcohol/acid ratio of 1.6. Acetic acid at higher concentrations than required for the critical alcohol/acid ratio lower than 1.3 and higher than 1.6 resulted in decreased yields of isoamyl acetate probably owing to lowering of microaqueous environmental pH around the enzyme leading to inhibition of enzyme activity. Mycelium bound A. niger lipase produced 80 g/l of isoamyl acetate within 96 h even though extremely less amount of enzyme activity was used for esterification. The presence of sodium sulphate during esterification reaction at higher substrate concentration resulted in increased conversion efficiency when we used mycelium bound enzyme preparations of A. niger NCIM 1207. This could be due to removal of excess water released during esterification reaction by sodium sulphate. High ester concentration (286.5 g/l) and conversion (73.5%) were obtained within 24 h using Novozyme 435 under these conditions.

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Section: Discussionmentioning

confidence: 99%

Lipase of Aspergillus niger NCIM 1207: A Potential Biocatalyst for Synthesis of Isoamyl Acetate

2010

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“…The positive effect of enzyme concentration on the synthesis of butyric ester is in agreement with the reports of other authors dealing with the production of favour esters (ethyl hexanoate, isoamyl isovalerate, isoamyl acetate) using microbial lipases. 24,27,28 At a temperature of 30 ºC, the highest ester concentrations were found with a butyric acid concentration ranging from 0.3 to 0.7 mol L -1 and an enzyme concentration between 0.015 and 0.025 g mL -1 , respectively. At a temperature of 50 ºC, the highest values for ester concentration were found in the range from 0.5 to 0.9 mol L -1 with an enzyme concentration from 0.015 to 0.025 g mL -1 .…”

Section: Model Fitting 2 3 Central Composite Rotatable Design (Ccrd)mentioning

confidence: 99%

Enzymatic synthesis optimization of isoamyl butyrate

Anschau¹,

Aragão²,

Porciuncula³

et al. 2011

J. Braz. Chem. Soc.

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Lipozyme TL IM foi usada para catalisar a esterificação de álcool isoamílico e ácido butírico. Um planejamento fatorial fracionário foi utilizado para avaliar os efeitos da temperatura (30, 40, 50 ºC), razão molar álcool:ácido (1:1, 2:1, 3:1), concentração de enzima (0,003, 0,0115, 0,020 g mL -1 ), concentração de ácido butírico (0,1, 0,3, 0,5 mol L -1 ) e agitação (50, 115, 180 rpm) na produção de éster. Com esses resultados, os níveis foram redefinidos para um planejamento fatorial 2³. A máxima produção de éster foi obtida a 30 ºC, 180 rpm, razão molar álcool:ácido de 1:1, concentração de enzima 0,021 g mL -1 e concentração de ácido butírico de 0,5 mol L -1 . Sob essas condições ótimas foi obtido 92% de esterificação e concentração de éster de 0,9 mol L -1 . Álcool isoamílico obtido a partir de óleo fúsel foi utilizado nas mesmas condições resultando em 93% de esterificação e concentração de éster de 1,0 mol L -1 .Lipozyme TL IM was used to catalyse the esterification of isoamyl alcohol and butyric acid. A fractional factorial design was employed to evaluate the effects of temperature (30, 40, 50 °C), alcohol:acid molar ratio (1:1, 2:1, 3:1), enzyme concentration (0.003, 0.0115, 0.020 g mL -1 ), butyric acid concentration (0.1, 0.3, 0.5 mol L -1 ) and shaking rate (50, 115, 180 rpm) on the ester yield. With these results, the levels were redefined to a 2 3 factorial design. The maximum yield of ester was obtained at 30 ºC, 180 rpm, alcohol:acid molar ratio of 1:1, enzyme concentration of 0.021 g mL -1 and butyric acid concentration of 0.5 mol L -1 . Under the optimal conditions, 92% esterification was attained with an ester concentration of 0.9 mol L -1 . Isoamyl alcohol from fusel oil was used under the same conditions and resulted in 93% esterification and an ester concentration of 1.0 mol L -1 .

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“…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%

“…Besides, the same flavor and fragrance esters prepared by enzymatic synthesis may be labeled as "natural" (Gillies et al 1987). Consequently, lipases have been extensively employed for direct esterification and transesterification reactions in both non-aqueous and solvent-free systems to produce esters of shortchain aliphatic carboxylic acids and alcohols such as isoamyl acetate, and butyl acetate (Krishna et al 2000;Ozyilmaz and Gezer, 2010); ethyl butyrate, butyl butyrate and butyl isobutyrate (Yadav and Lathi, 2003;Santos and Castro, 2006;Pires-Cabral et al 2007), ethyl valerate (Ozyilmaz and Gezer, 2010). However, the synthesis of esters of medium-chain fatty acids and monohydric alcohols including amyl caprylate here investigated, has received lesser attention in the literature (Vaidya et al 2008).…”

Section: Introductionmentioning

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

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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.

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Optimization of isoamyl acetate production by using immobilized lipase from Mucor miehei by response surface methodology

Cited by 103 publications

References 10 publications

Lipase of Aspergillus niger NCIM 1207: A Potential Biocatalyst for Synthesis of Isoamyl Acetate

Lipase of Aspergillus niger NCIM 1207: A Potential Biocatalyst for Synthesis of Isoamyl Acetate

Enzymatic synthesis optimization of isoamyl butyrate

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

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