Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports

Barig, Susann; Funke, Andreas; Merseburg, Andrea; Schnitzlein, Klaus; Stahmann, K.‐Peter

doi:10.1016/j.enzmictec.2014.03.013

Cited by 10 publications

(3 citation statements)

References 49 publications

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“…When using a simple adsorption on the used MWCNTs having hydrophobic domains, the active site of the CAL-B close to its hydrophobic zones will spontaneously position toward the surface of the MWCNTs thus potentially limiting accessibility of substrates to its catalytic triad. This scenario is consistent with the good affinity of proteins and lipases for hydrophobic carrier material reported in literature [37][38][39][40] .…”

Section: Geranyl Acetate Synthesis In Scco2supporting

confidence: 92%

Non-covalent and covalent immobilization of Candida antarctica lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2

et al. 2020

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Candida antarctica B lipase (CAL-B) was immobilized on purified and functionalized multiwalled carbon nanotubes (MWCNTs). Both immobilization routes, physical adsorption and covalent bonding, were investigated. MWCNT functionalization by a non-aggressive oxidation by potassium permanganate led to an interesting balance between the hydrophilic and the hydrophobic areas of the MWCNT surface; the former being responsible of the good dispersion of MWCNTs in water and the latter having a favorable affinity with CAL-B. The enzyme loadings reached were significant: around 16 wt. % and 21 wt.% for non-covalent and covalent immobilization, respectively. The enzymatic activity was studied with the reaction of O-acylation of geraniol into geranyl acetate by CAL-B in supercritical CO2. Even if a decay in synthesis of geranyl acetate was observed over cycling for both CAL-B@MWCNT catalysts, it was demonstrated that the regioselectivity of CAL-B was unchanged through immobilization on the MWCNT surface for both routes. Interestingly, it was shown that a fully green enzymatic process can be achieved with these prepared CAL-B@MWCNT biocatalyst. Such approach could be transferred to other support/enzyme systems for developing new eco-friendly synthesis processes.

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Section: Geranyl Acetate Synthesis In Scco2supporting

confidence: 92%

Non-covalent and covalent immobilization of Candida antarctica lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2

et al. 2020

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“…Combining physical and chemical properties and geometry of the support has changed the interaction mechanism and properties of enzymes in the desired way [22,23]. Meso-and macroporous resins based on polystyrene, methacryl or epoxide, can be functionalized by different groups to introduce ionic, hydrophobic or absorptive interactions [17,24,25]. Furthermore, covalent immobilization can be realized using glyoxyl, epoxy or glutaraldehyde groups [25,26].…”

Section: Introductionmentioning

confidence: 99%

“…With chemical immobilization, covalent bonds are formed with the enzyme [10][11][12][13][14][15]. Polymers are of considerable interest among the various supports used for enzyme immobilization, as justified by their advantages like non toxicity, biocompatibility and biodegradability [16][17][18][19]. A high variety of polymeric support, including natural (chitin, chitosan, agarose and cellulose derivates) and synthetic (nylon, polysiloxane/polyaniline, polyvinylalcohol, polyacrylic polymers, sulfonated polystyrene type Amberlite) were used for the immobilization of laccase from different sources [20,21].…”

Section: Introductionmentioning

confidence: 99%

Effect of polymer support functionalization on enzyme immobilization and catalytic activity

Pârvulescu

Popa

Păun

et al. 2014

Pure and Applied Chemistry

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Two enzymes, laccase and peroxidase, were immobilized on chloromethylated styrene-divinylbenzene copolymers supports functionalized with phosphonates ((RO) 2 PO) or mixed ammonium and phosphonium groups (N + R 3 Cl -, P + Ph 3 Cl -). Phosphonates groups and quaternary ammonium salts were grafted on the "gel-type" copolymer by Michaelis-Becker polymer analogue reaction. Mixed polymer-supported ammonium and phosphonium salts were obtained by transquaternization of the ammonium groups to phosphonium group. The degrees of functionalization for obtained polymers were relatively high ensuring a sufficient concentration of active centers per unit mass of the copolymer. The obtained materials were characterized by thermal analysis, FTIR spectroscopy and SEM microscopy. The effects of OR1 and R2 radicals from phosphonate and respectively ammonium groups, as well as those of glutaraldehyde utilization on the immobilization yield and the catalytic properties of the supported enzymes were indicated. The activity of enzymes increased after immobilization and high immobilization yield was obtained for all the samples. The higher interaction of enzymes with support was indicated for mixed ammonium and phosphonium functions. A higher catalytic activity was obtained for peroxidase in oxidation of phenol and laccase in oxidation of anisole. The low effect of glutaraldehyde on enzyme activity reveals the strong interaction of enzyme with the polymer support, respectively with the functional groups.

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Poröses Kohlenstoffmaterial zur Immobilisierung von Lipase – Vergleichende Messungen mit Methacryl‐Beads

Barig

Utgenannt

Heine

et al. 2016

Chemie Ingenieur Technik

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Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports

Cited by 10 publications

References 49 publications

Non-covalent and covalent immobilization of Candida antarctica lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2

Non-covalent and covalent immobilization of Candida antarctica lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2

Effect of polymer support functionalization on enzyme immobilization and catalytic activity

Poröses Kohlenstoffmaterial zur Immobilisierung von Lipase – Vergleichende Messungen mit Methacryl‐Beads

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