The sol-gel encapsulation of enzymes

Pierre, Alain C.

doi:10.1080/10242420412331283314

Cited by 366 publications

(283 citation statements)

References 100 publications

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“…The average structures of proteins encapsulated in the pores of wet-aged-based silica glasses were determined by CD spectroscopy in TMOS-based glasses [Si(OMe) 4 ] that were modified by addition of alkyltrimethoxysilane precursors [RSi(OMe) 3 ]. The CD signals originating from the protein in glass samples may be compared directly to the protein signal obtained in dilute solution because the data are normalized to units of molar ellipticity.…”

Section: Protein Structure In Alkyl-modified Silica Glassesmentioning

confidence: 99%

“…This hypothesis may be tested by encapsulating proteins into chemically-modified silica networks and by monitoring slight alterations in protein conformation by spectroscopic techniques. Even though many reports indicate that sol-gel glass encapsulation retains the activity of a wide variety of enzymes, as reviewed in [1][2][3][4][5][6], few of these reports attempt to quantify the fraction of properly-folded protein, and the specific enzyme activities (normalized per mass of protein) are often omitted. Also, in the case of encapsulated enzymes, activity measurements may be influenced by multiple factors; diffusion of substrates into the pores, accessibility of enzyme molecules, and the adsorption of substrates to the silica surface, in addition to changes in protein structure, may reduce enzyme activity relative to the activity measured in bulk solution.…”

Section: Introductionmentioning

confidence: 99%

“…In the past few years, numerous silica-and/or porous siloxane-based organic-inorganic materials have been employed to produce protein-doped hybrid materials as biosensors and as heterogeneous catalysts for industrial applications [1][2][3][4][5][6]. In particular, the design of organically-modified hydrophobic glasses for encapsulating lipases, a class of enzymes that mediate lipid reactions and function naturally at hydrophobic interfaces, has received much attention due to the potential application of these enzymes in the conversion of fats and oils to other products of value [7][8][9][10][11][12][13][14][15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

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Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses

et al. 2008

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Organically-modified siloxanes were used as host materials to examine the influence of surface chemistry on protein conformation in a crowded environment. The sol-gel materials were prepared from tetramethoxysilane and a series of monosubstituted alkoxysilanes, RSi(OR′) 3 , featuring alkyl groups of increasing chain length in the R-position. Using circular dichroism spectroscopy in the far-UV region, apomyoglobin was found to transit from an unfolded state to a native-like helical state as the content of the hydrophobic precursor increased from 0-15%. At a fixed molar content of 5% RSi(OR') 3 , the helical structure of apomyoglobin increased with the chain length of the R-group, i.e. methyl < ethyl < n-propyl < n-butyl < n-hexyl. This trend also was observed for the tertiary structure of ribonuclease A, suggesting that protein folding and biological activity are sensitive to the hydrophilic/hydrophobic balance of neighboring surfaces. The observed changes in protein structure did not correlate with total surface area or the average pore size of the modified glasses, but scanning electron microscopy images revealed an interesting relationship between surface morphology and alkyl chain length. The unexpected benefit of incorporating a low content of hydrophobic groups into a hydrophilic surface may lead to materials with improved biocompatibility for use in biosensors and implanted devices.

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Section: Protein Structure In Alkyl-modified Silica Glassesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses

et al. 2008

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“…[14][15][16][17]. The sol-gel reactions proceed by hydrolysis of an alkoxide precursor under acid or basic conditions and condensation of the hydroxylated monomers to form a porous siloxane polymer gel [18,19]. Enzyme encapsulation in sol-gel rather than in other matrices can improve some properties such as operational stability and activity compared to cross-linking with glutaraldehyde, and a longer linear range [14,[20][21][22].…”

Section: E-mail Address: Brett@ciucpt (Cma Brett)mentioning

confidence: 99%

Design and application of a flow cell for carbon-film based electrochemical enzyme biosensors

Bârsan

Klincar

Batič

et al. 2007

Talanta

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A flow cell has been designed for use with an electrochemical enzyme biosensor, based on low-cost carbon-film electrodes. Three types of mediators were used: cobalt and copper hexacyanoferrates and poly(neutral red) (PNR), covered with glucose oxidase (GOx) immobilised by cross-linking with glutaraldehyde in the presence of bovine serum albumin or inside a oxysilane sol-gel network. Mixtures of sol-gel precursors were made from 3-aminopropyl-triethoxysilane (APTOS) together with methyltrimethoxysilane (MTMOS), methyltriethoxysilane (MTEOS), tetraethyloxysilane (TEOS) or 3-glycidoxypropyl-trimethoxysilane (GOPMOS), and the best chosen for encapsulation. Optimisation in batch mode, using amperometric detection at fixed potential, showed the PNR-GOx modified carbon-film electrodes to be best for flow analysis for both glutaraldehyde and sol-gel enzyme immobilisation. Both types of enzyme electrode were tested under flow conditions and the reproducibility and stability of the biosensors were evaluated. The biosensors were used for fermentation monitoring of glucose in grape must and interference studies were also performed.

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“…β-galactosidase is a commercially important enzyme that are widely used in different industries, especially in food and pharmaceutical sectors. (PIERRE, 2004;HARTMANN, 2005;HUSAIN, 2010). According to the existing reports, major β-galactosidase producing bacteria species belong to Bacillus subtilis (EL-KADER et al, 2012), Lactobacillus gasseri (HONDA et al, 2012), Streptococcus thermophilus (PRINCELY et al, 2013) and Anoxybacillus sp.…”

mentioning

confidence: 99%

Chemical extraction and optimization of intracellular β-galactosidase production from the bacterium Arthrobacter oxydans using Box-Behnken design of response surface methodology

Banerjee¹,

Das²,

Kumar³

et al. 2016

Acta Alimentaria

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Present study demonstrated the isolation of most promising β-galactosidase producing bacterial strain SB from soil. Morphological, biochemical, and 16s rRNA sequence analysis identifi ed the bacterial strain as Arthrobacter oxydans. Several chemicals, including SDS, Triton X-100, Tween 20, isoamyl alcohol, and toluene-acetone mixture, were applied for extraction of intracellular β-galactosidase from the bacterial strain Arthrobacter oxydans. Among these, Tween 20 was recorded to be most effective. Role of pH, temperature, and shaker speed on production of β-galactosidase was evaluated using Box-Behnken design of response surface methodology. According to BoxBehnken analysis, optimum production of β-galactosidase (21.38 U (mg -1 protein)) is predicted at pH 6.76, temperature 36.1 °C, and shaker speed 121.37 r.p.m. The parameters are validated with the nearest value.

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The sol-gel encapsulation of enzymes

Cited by 366 publications

References 100 publications

Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses

Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses

Design and application of a flow cell for carbon-film based electrochemical enzyme biosensors

Chemical extraction and optimization of intracellular β-galactosidase production from the bacterium Arthrobacter oxydans using Box-Behnken design of response surface methodology

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