Understanding the pH-dependent immobilization efficacy of feruloyl esterase-C on mesoporous silica and its structure–activity changes

Thörn, Christian; Udatha, D.B.R.K. Gupta; Christakopoulos, Paul; Olsson, Lisbeth

doi:10.1016/j.molcatb.2013.04.011

Cited by 21 publications

(18 citation statements)

References 43 publications

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“…In relation to enzyme immobilization this allows protein modeling of the enzyme structure and calculation of surface potential or charge distribution on the surface at different pH (see Figure 9) [9,47,108,113]. This information can partly be used to predict how strongly enzymes can bind to the surface and how the strength depends on the environmental conditions upon immobilization [9].…”

Section: Protein Modeling and Molecular Dynamics Simulationsmentioning

confidence: 99%

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Carlsson

Gustafsson

Thörn

et al. 2014

Advances in Colloid and Interface Science

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211

167

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Section: Protein Modeling and Molecular Dynamics Simulationsmentioning

confidence: 99%

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Carlsson

Gustafsson

Thörn

et al. 2014

Advances in Colloid and Interface Science

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211

167

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“…Several factors during the immobilization process can influence enzyme immobilization and enzyme selectivity [ 23 , 24 ]. Therefore, different buffers were tested at various pH values as well as different enzyme concentration and different pore sizes of the MPS.…”

Section: Resultsmentioning

confidence: 99%

Feruloyl esterase immobilization in mesoporous silica particles and characterization in hydrolysis and transesterification

et al. 2018

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BackgroundEnzymes display high reactivity and selectivity under natural conditions, but may suffer from decreased efficiency in industrial applications. A strategy to address this limitation is to immobilize the enzyme. Mesoporous silica materials offer unique properties as an immobilization support, such as high surface area and tunable pore size.ResultsThe performance of a commercially available feruloyl esterase, E-FAERU, immobilized on mesoporous silica by physical adsorption was evaluated for its transesterification ability. We optimized the immobilization conditions by varying the support pore size, the immobilization buffer and its pH. Maximum loading and maximum activity were achieved at different pHs (4.0 and 6.0 respectively). Selectivity, shown by the transesterification/hydrolysis products molar ratio, varied more than 3-fold depending on the reaction buffer used and its pH. Under all conditions studied, hydrolysis was the dominant activity of the enzyme. pH and water content had the greatest influence on the enzyme selectivity and activity. Determined kinetic parameters of the enzyme were obtained and showed that Km was not affected by the immobilization but kcat was reduced 10-fold when comparing the free and immobilized enzymes. Thermal and pH stabilities as well as the reusability were investigated. The immobilized biocatalyst retained more than 20% of its activity after ten cycles of transesterification reaction.ConclusionsThese results indicate that this enzyme is more suited for hydrolysis reactions than transesterification despite good reusability. Furthermore, it was found that the immobilization conditions are crucial for optimal enzyme activity as they can alter the enzyme performance.Electronic supplementary materialThe online version of this article (10.1186/s12858-018-0091-y) contains supplementary material, which is available to authorized users.

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“…[44][45][46][47][48][49][50][51][52] Resorting to computational modeling, detailed analysis of the surface charge characteristics of a given enzyme can be gained and be used for directing the design of support materials with compatible surface charges in the nanopores. Naturally, except for the hydrophobic/hydrophilic balance, the electrostatic feature of the nanopore surface has also been recognized as an important factor concerning the chemical microenvironment of immobilized enzymes.…”

Section: Surface Charge Of Nanoporesmentioning

confidence: 99%

Towards efficient chemical synthesis via engineering enzyme catalysis in biomimetic nanoreactors

Liu

Yang

2015

Chem. Commun.

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Biocatalysis with immobilized enzymes as catalysts holds enormous promise in developing more efficient and sustainable processes for the synthesis of fine chemicals, chiral pharmaceuticals and biomass feedstocks. Despite the appealing potentials, nowadays the industrial-scale application of biocatalysts is still quite modest in comparison with that of traditional chemical catalysts. A critical issue is that the catalytic performance of enzymes, the sophisticated and vulnerable catalytic machineries, strongly depends on their intracellular working environment; however the working circumstances provided by the support matrix are radically different from those in cells. This often leads to various adverse consequences on enzyme conformation and dynamic properties, consequently decreasing the overall performance of immobilized enzymes with regard to their activity, selectivity and stability. Engineering enzyme catalysis in support nanopores by mimicking the physiological milieu of enzymes in vivo and investigating how the interior microenvironment of nanopores imposes an influence on enzyme behaviors in vitro are of paramount significance to modify and improve the catalytic functions of immobilized enzymes. In this feature article, we have summarized the recent advances in mimicking the working environment and working patterns of intracellular enzymes in nanopores of mesoporous silica-based supports. Especially, we have demonstrated that incorporation of polymers into silica nanopores could be a valuable approach to create the biomimetic microenvironment for enzymes in the immobilized state.

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Understanding the pH-dependent immobilization efficacy of feruloyl esterase-C on mesoporous silica and its structure–activity changes

Cited by 21 publications

References 43 publications

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Feruloyl esterase immobilization in mesoporous silica particles and characterization in hydrolysis and transesterification

Towards efficient chemical synthesis via engineering enzyme catalysis in biomimetic nanoreactors

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