1-Butyl oleate synthesis by immobilized lipase from Rhizopus oryzae: a comparative study between n-hexane and solvent-free system

Ghamgui, Hanen; Karra-Châabouni, Maha; Gargouri, Youssef

doi:10.1016/j.enzmictec.2004.06.002

Cited by 133 publications

(75 citation statements)

References 34 publications

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“…Noteworthy, the conversion yield of the obtained propyl gallate synthesis when using immobilized SXL, is higher than that obtained by free lipase. This result is also in agreement with that obtained by Ghamgui et al [28] and Horchani et al [29] who state that the immobilization of staphylococcal lipases into CaCO 3 increases both their stability at high temperature and their ability to tolerate the presence of organic solvents. In addition, one can relate the low conversion yield obtained with free enzyme and its inactivation at the interface of the biphasic media.…”

Section: Interpretation Of the Response Surface Modelsupporting

confidence: 82%

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Bouaziz¹,

Horchani²,

Salem³

et al. 2010

Journal of Molecular Catalysis B: Enzymatic

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a b s t r a c tThe ability of a non-commercial immobilized Staphylococcus xylosus lipase to catalyze the esterification of propanol with gallic acid was investigated and the antioxidant as well as the antimicrobial activities of the ester formed were evaluated. The response surface methodology, based on a three variables Box-Behnken design (reaction temperature, enzyme amount and 1-propanol/gallic acid molar ratio), was used to optimize the experimental conditions of propylgallate synthesis. The maximum conversion yield (90% ±3.5) was obtained by using 400 IU of immobilized lipase and a propanol/gallic acid at a molar ratio of 160 at 52 • C. The obtained ester was characterized by spectroscopic methods, NMR and FTIR. The antioxidant activity of propyl gallate was evaluated and compared to the synthetic classical antioxidants, BHA and ascorbic acid, taken as references. In addition, the antimicrobial activity of the propyl gallate was tested against S. xylosus, Escherchia coli and Staphylococcus aureus using disc diffusion and macrodilution methods. Our results show that the synthesized propyl gallate ester presents a higher antioxidant and antimicrobial power than the parent gallic acid as well as the synthetic classical antioxidants.

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Section: Interpretation Of the Response Surface Modelsupporting

confidence: 82%

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Bouaziz¹,

Horchani²,

Salem³

et al. 2010

Journal of Molecular Catalysis B: Enzymatic

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“…28 The loss of activity during reuse of the biocatalyst immobilized by physical adsorption can be explained by electrostatic interactions or weak links in the support/enzyme, which resulted in desorption during the washing or other process stages. 29 Reuse of Rizophus oryzae lipase (ROL) immobilized by adsorption on calcium carbonate and oxidised cellulose carried out by producing oleate butyl were obtained by six and three cycles respectively in the work of Guamgui et al, 30 and Karra-Châabouni et al, 31 The CB and CBIL showed an increase in the number of reuses compared with ADS and ADSIL. This behaviour occurred because immobilization by covalent binding becomes stronger binding of enzymes on the silica aerogel to prevent leaching because of the chemical bonding between the amino groups of the lipase and the terminal aldehyde of the support is irreversible and resist.…”

Section: The Total Activity Recovery Yield (H %) Results For the Immentioning

confidence: 99%

The Novel Mesoporous Silica Aerogel Modified With Protic Ionic Liquid for Lipase Immobilization

Barbosa¹,

Lisboa²,

Silva³

et al. 2016

Química Nova

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Recebido em 24/08/2015; aceito em 22/12/2015; publicado na web em 11/02/2016Mesoporous silica supports (aerogels) were used to immobilize Burkholderia cepacia lipase (BC) by encapsulation (EN or ENIL), physical adsorption (ADS or ADSIL) and covalent binding (CB or CBIL) into or onto the aerogel modified with protic ionic liquid (PIL). Yield immobilization (Ya) and operational stability were determined by the hydrolytic reaction of olive oil. Ya (37% to 83% by physical adsorption) and operational stability (2 to 23 batches by encapsulation) increased when the support was modified with PIL. For immobilized derivates observed by the BET method, in this case ADS and CB for ADSIL and CBIL, increased pores size was observed, possibly due to the higher amount of BC immobilized conferring Ya and operational stability. This effect was probably attributed to the entry of the enzyme into the pores of the silica aerogel structure. SEM images showed a change in the structure and properties of immobilized lipase derived with PIL. A characteristic FTIR band was obtained for the silanol groups and amides I, IV and V, demonstrating the efficiency of immobilization of BC. The most efficient biocatalysts were ADSIL with regard to yield immobilization and ENIL for operational stability.

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“…A change of the optimum pH for porcine pancreatic lipase entrapped in carragenan beads was previously reported 27 . Ghamgui et al reported the maximum activity of free lipase of Rhizopus oryzae at pH 8 28 . In contrast when the enzyme was immobilized, the optimum pH was shifted to pH 7.…”

Section: Comparative Study Of Free and Immobilized Lipasementioning

confidence: 99%

Fabrication and Characterization of Core-Shell Magnetic Chitosan Nanoparticles as a Novel carrier for Immobilization of <i>Burkholderia cepacia</i> Lipase

et al. 2015

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1-Butyl oleate synthesis by immobilized lipase from Rhizopus oryzae: a comparative study between n-hexane and solvent-free system

Cited by 133 publications

References 34 publications

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

The Novel Mesoporous Silica Aerogel Modified With Protic Ionic Liquid for Lipase Immobilization

Fabrication and Characterization of Core-Shell Magnetic Chitosan Nanoparticles as a Novel carrier for Immobilization of <i>Burkholderia cepacia</i> Lipase

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