Lipase catalyzed formation of flavour esters

Langrand, G.; Triantaphylidès, C.; Baratti, J.

doi:10.1007/bf01027127

Cited by 150 publications

(70 citation statements)

References 12 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 main advantages of this compared to direct synthesis are (i) no water molecules are formed or consumed in the reaction (ii) the enzyme stability is usually higher under these conditions (Langrand et al, 1988). A mathematical basis for the design and operation of a continuous, packed-bed reactor for the interesterifiction of soybean oil was developed by Akimoto et al (1999).…”

Section: Interesterificationmentioning

confidence: 99%

“…due to its versality and a high level of stereo control (Sanchez et al, 2000). Langrand et al (1988) checked thirteen commercial lipase preparations for their ability to catalyze the formation of flavour esters. Acetic acid esters were more difficult to obtain than isomyl, gernoyl acetate, propionate and butyrate.…”

Section: Esterificationmentioning

confidence: 99%

Lipase catalyzed ester synthesis for food processing industries

Rajendran

Palanisamy

Viruthagiri

2009

Braz. arch. biol. technol.

141

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“…To achieve complete conversion, less than 18 and »20 and 23 h were needed for laboratory, intermediate and large-scale syntheses, respectively. The need for increasing reaction time with increasing reaction volume was previously reported (Bloomer et al, 1992;Langrand et al., 1988). This may result from mass transfer limitations.…”

Section: Scale-up Of Processmentioning

confidence: 81%

Scale‐up of pseudo solid‐phase enzymatic synthesis of α‐methyl glucoside acrylate

Rethwisch²

2002

Biotech & Bioengineering

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The successful scale-up of the enzymatic synthesis of alpha-methyl glucoside acrylate from laboratory-scale (milliliter) to pilot-scale (liter) was examined. Specifically, Candida antarctica lipase B (Novozym 435) was used as a biocatalyst to produce alpha-methyl glucoside acrylate via the transesterification of alpha-methyl glucoside (MG) with vinyl acrylate (VA) using acetone as a solvent. This is a pseudo-solid-phase synthesis; only a fraction of the alpha-methyl glucoside and the product are soluble in acetone. Molecular sieves were used to remove traces of water in the reaction medium and to increase enzyme stability by removing the acetaldehyde by-product. A general method was also developed to purify and recover the monoacrylate product from unreacted sugar and undesired diester by a simple crystallization and precipitation process.

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Lipase catalyzed formation of flavour esters

Cited by 150 publications

References 12 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

Lipase catalyzed ester synthesis for food processing industries

Scale‐up of pseudo solid‐phase enzymatic synthesis of α‐methyl glucoside acrylate

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