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

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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%