Optimization of lipase-catalyzed synthesis of (z)-3-hexen-1-yl acetate by direct esterification in hexane and a solvent-free medium

Bourg-Garros, S.; Razafindramboa, N.; Pavia, A. A.

doi:10.1016/s0141-0229(97)83278-4

Cited by 38 publications

(25 citation statements)

References 27 publications

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“…This is probably because beyond a critical temperature, the lipase may have been deactivated. The results is similar in the findings by most reviewed papers that Novozym 435 was optimally used at 40ºC to 60ºC (Bourg-Garros et al 1998;Lozano et al 2003). The conversion decreased slightly after 60ºC probably caused by the vibration and movement of the enzyme molecule, which would affect the hydrogen bonds and other bonds in the lipase structure.…”

Section: Effect Of Reaction Temperaturesupporting

confidence: 90%

High performance enzymatic synthesis of oleyl oleate using immobilised lipase from Candida antartica

Radzi¹,

Basri²,

Salleh³

et al. 2005

Electron. J. Biotechnol.

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Section: Effect Of Reaction Temperaturesupporting

confidence: 90%

High performance enzymatic synthesis of oleyl oleate using immobilised lipase from Candida antartica

Radzi¹,

Basri²,

Salleh³

et al. 2005

Electron. J. Biotechnol.

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“…The samples were analyzed for isoamyl acetate content after 24 h The bioconversion reaction was carried out at 30°C with shaking at 120 rpm in 25 ml stoppered flasks with 10 ml n-hexane containing fusel oil (1.9 ml), acetic acid (360 ll), and known amount of enzyme source Indian J Microbiol (Oct-Dec 2010) 50(4):432-437 435 of various commercial lipases and also mycelium bound lipase on isoamyl acetate production was investigated. We found that the reaction rate and esterification were higher using Novozyme 435 yielding 100% esterification in 4 h. Novozyme 435 was also found suitable in the synthesis of other acetate esters in hexane [22], in heptane [23] and also in solvent-free systems [3]. A. niger NCIM 1207 produces lipase active at acidic pH and it was also found to produce isoamyl acetate (80 g/l) indicating the new potential candidate for production of flavor esters in organic solvents.…”

Section: Discussionmentioning

confidence: 83%

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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“…Esters such as (Z )-3-hexen-1-yl acetate are important flavor and fragrance compounds (green note compounds) used in the food and cosmetic industries. 14,15 Industrial production of flavor esters is accomplished via a nonspecific chemical process requiring complicated purification steps. Lipase-catalyzed esterification can be performed under more moderate conditions and yields a highquality product.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of (Z)‐3‐hexen‐1‐yl acetate by lipase immobilized in polyvinyl alcohol nanofibers

Nakane

Hotta

Ogihara

et al. 2007

J of Applied Polymer Sci

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Polyvinyl alcohol (PVA)-nanofibers-immobilized lipase were formed by electrospinning. The specific surface area of the nanofiber (5.96 m 2 /g) was about 250 times larger than that of PVA-film-immobilized lipase (0.024 m 2 /g). The PVA-nanofibers-immobilized lipase were used as the catalyst for the esterification of (Z )-3-hexen-1-ol (leaf alcohol) with acetic acid in hexane. The activity of the nanofiber is equivalent to that of commercially available immobilized lipase (Novozym-435). The ester conversions of the nanofibers, Novozym-435, the film and lipase powder reached 99.5% at 5 h, 100% at 5 h, 11.5% at 6 h, and 81.1% at 5.75 h, respectively. The nanofibers-immobilized lipase showed higher activity for the esterification than the film-immobilized lipase and lipase powder, probably because it has high specific surface area and high dispersion state of lipase molecules in PVA matrix.

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Optimization of lipase-catalyzed synthesis of (z)-3-hexen-1-yl acetate by direct esterification in hexane and a solvent-free medium

Cited by 38 publications

References 27 publications

High performance enzymatic synthesis of oleyl oleate using immobilised lipase from Candida antartica

High performance enzymatic synthesis of oleyl oleate using immobilised lipase from Candida antartica

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

Synthesis of (Z)‐3‐hexen‐1‐yl acetate by lipase immobilized in polyvinyl alcohol nanofibers

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