Immobilization of lipase from Fusarium solani FS1

Knight, Kirsty; Pimentel, Maria do Carmo B.; Morais, Márcia Maria Camargo de; Ledingham, W. M.; Filho, José Luiz de Lima; Maia, Maria de Mascena Diniz

doi:10.1590/s1517-83822000000300013

Cited by 10 publications

(3 citation statements)

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“…1 The enzymatic activity in bulk solution is usually low, 2 and it is therefore common practice to use lipases in immobilized form. 3 The requirement of an interface is at least partly understood for those lipases that have been found to possess a "lid" that covers the active site. This lid, which is hydrophobic underneath, will fold open when approached by a hydrophobic surface.…”

Section: Introductionmentioning

confidence: 99%

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Lipase-Catalyzed Reactions at Different Surfaces

et al. 2006

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Starting from gold chips, we have tailor-made three surfaces by the self-assembly monolayer technique: one entirely hydrophobic, one hydrophobic with dispersed carboxyl groups, and one hydrophilic, containing hydroxyl groups. Rhizomucor miehei lipase has been adsorbed to the hydrophobic and the hydrophilic surfaces and covalently bound to the surface containing carboxyl groups. The adsorption of two substrates-capric acid (decanoic acid) and monocaprin-on the lipase-covered surfaces was monitored by the surface plasmon resonance (SPR) technique. Biocatalysis was also performed in the SPR instrument by circulating a solution of the substrate, dissolved in an 85:15 water-glycerol mixture at a(w) = 0.81, through the instrument, thus exposing the capric acid or the monocaprin to the lipase-covered surfaces. The product composition was found to depend on the type of surface used. Lipase adsorbed at the hydrophilic surface favored hydrolysis, and capric acid was the main product formed when monocaprin was used as substrate. Lipase adsorbed at a hydrophobic surface and, in particular, lipase covalently bound to a hydrophobic surface favored condensation. More dicaprin than capric acid was formed in experiments with monocaprin as the substrate. Reactions performed outside the SPR instrument showed that small amounts of triglyceride were also formed under these conditions. We believe that this work constitutes the first example of the SPR instrument being used for in-situ biotransformation.

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Section: Introductionmentioning

confidence: 99%

“…Lipases therefore normally work at an interface . The enzymatic activity in bulk solution is usually low, and it is therefore common practice to use lipases in immobilized form . The requirement of an interface is at least partly understood for those lipases that have been found to possess a “lid” that covers the active site.…”

Section: Introductionmentioning

confidence: 99%

Lipase-Catalyzed Reactions at Different Surfaces

et al. 2006

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“…Most enzymes become less active and stable in organic solvents [19]. Therefore, the enzymes used in the literature for the chemoenzymatic epoxidation of vegetable oils are immobilized using low-cost supports, such as polyacrylamide as used by Knight et al [20]. The lipase immobilization from Fusarium solani FS1, with retention of 53% of enzymatic activity, increased specificity, selectivity, and improved stability of its structure, allows for its recovery and reuse [21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic and Synthetic Routes of Castor Oil Epoxidation

Montenegro,

Ries,

Silva

et al. 2023

Polymers

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Epoxidation of castor oil in synthetic and enzymatic routes was carried out in order to promote a system with less environmental impact. The epoxidation reactions of castor oil compounds upon addition of lipase enzyme with and without acrylic immobilization and with reaction times of 24 and 6 h, as well as the synthetic compounds upon addition of Amberlite resin and formic acid, were investigated using Fourier transform infrared spectroscopy (FTIR) and nuclear magnetic resonance in hydrogen molecules (1H-NMR). The analysis indicated that the enzymatic reactions (6 h) and synthetic reactions provided a conversion from 50 to 96% and epoxidation from 25 to 48%, resulting from peak stretching and signal disintegration in the hydroxyl region due to the appearance of H2O in the interaction of peracid with catalyst. In systems without toluene, a dehydration event with a peak absorbance of 0.02 AU, indicating a possible vinyl group at 2355 cm−1 in enzymatic reactions without acrylic immobilization, was observed and resulted in a selectivity of 2%. In the absence of a solid catalyst, an unsaturation conversion of castor oil above 90% was achieved; however, this catalyst is necessary for the epoxidation to take place, whereas the lipase enzyme becomes able of epoxidizing and dehydrating the castor oil upon changing the time or reaction system. The conversation from 28 to 48% of solid catalysts (Amberlite and lipase enzyme) displays their importance to the instauration conversion of castor oil into oxirane rings.

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