2015
DOI: 10.1016/j.enzmictec.2015.02.001
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Immobilization of lipases on hydrophobic supports involves the open form of the enzyme

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Cited by 460 publications
(321 citation statements)
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“…Generally, the immobilization is a powerful tool to enhance the reusability and stability of enzymes in modern biotechnology [41][42][43]. In this study, MML was immobilized on SBA-15 mesoporous silica via physical adsorption according to the previous study in our Lab [44,45], and the immobilized MML was used in the synthesis of indolyl 4H-chromenes.…”
Section: Resultsmentioning
confidence: 99%
“…Generally, the immobilization is a powerful tool to enhance the reusability and stability of enzymes in modern biotechnology [41][42][43]. In this study, MML was immobilized on SBA-15 mesoporous silica via physical adsorption according to the previous study in our Lab [44,45], and the immobilized MML was used in the synthesis of indolyl 4H-chromenes.…”
Section: Resultsmentioning
confidence: 99%
“…5 mM of buffer, or even in the presence of glycerin or polyethyleneglycol), the only water soluble protein able to become adsorbed in a moderately hydrophobic support will be the lipases ( Figure 10) . The influence of the experimental conditions neither do not fit a conventional hydrophobic adsorption (Manoel et al, 2015). This process involves the open form of the lipase., high High ionic strength during adsorption has a double negative effect in immobilization/purification process: other proteins may become adsorbed on the hydrophobic support (reducing the purification impact of the strategy) and lipase adsorption is slower, because the closed form is favored and the lipase needs to be adsorbed via conventional hydrophobic adsorption, which is not as efficient a process not as efficient as interfacial activation , Manoel et al, 2015.…”
Section: 1-the Case Of Lipases Immobilization Via Interfacial Activmentioning
confidence: 99%
“…Irreversible inactivation of the lipases adsorbed on this kind of supports using chemical Ser-hydrolases inhibitors, that need to have access to the catalytic Ser and depend only in the exposition of this group to the medium, is much more rapid after the immobilization on hydrophobic supports than in the free enzyme or in other immobilized preparations (Carrasco-López et al, 2009, Manoel et al, 2015, Santos et al, 2014a. This confirms that this strategy keeps the active form of the lipase open.…”
Section: 1-the Case Of Lipases Immobilization Via Interfacial Activmentioning
confidence: 99%
“…It is well known that lipases have a high affinity for hydrophobic surfaces and most of them express higher catalytic activity towards poorly soluable substrates. This is a consequence of the phenomenon called interfacial activation 17 . In most cases, the active site of the lipase is covered by short amphiphathic α-helix called the lid (closed form) make it inaccessible in the medium 18 .…”
Section: Introductionmentioning
confidence: 99%