Highly stable adsorptive and covalent immobilization of Thermomyces lanuginosus lipase on tailor-made porous carbon material

Reichardt, Christina; Utgenannt, Stephan; Stahmann, K.‐Peter; Klepel, Olaf; Barig, Susann

doi:10.1016/j.bej.2018.07.003

Cited by 28 publications

(7 citation statements)

References 92 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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“…Cellulose is not resistant to pyrolysis and its decomposition leads to an increase in pore diameter. One of the most important parameters evaluated in a porous support, which will be used in the immobilization of enzymes by adsorption, is the surface area, since the higher surface area leads to a greater available area for the enzyme to bind to the support 54,55 . In addition, a high surface area of the support will allow a higher number of metallic particles binding to its surface during the metallization process.…”

Section: Resultsmentioning

confidence: 99%

Incorporation of metallic particles in activated carbon used in lipase immobilization for production of isoamyl acetate

Oliveira

Santos

Brito

et al. 2022

J of Chemical Tech & Biotech

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BACKGROUND: Biotechnology has revolutionized the use of enzymes for application in industrial processes. The present work evaluated the effect of functionalizing activated carbon with metallic nanoparticles obtained from corn cob residue on lipase immobilization. The aim was to improve the enzymatic activity of the immobilized enzyme and subsequent application of derivatives in the synthesis of isoamyl acetate ester (banana flavor). RESULTS:The activated carbon (CCAC) had a mesoporous structure and specific surface area of 1135 m 2 g −1 , characteristic of supports from precursor material with a high cellulose content, which was reduced in metalized carbon (CCACM) due to the insertion of metallic particles (760 m 2 g −1 ). CCACM showed a slightly higher lipase absorptive capacity than CCAC (280.72 ± 0.27 mg g −1 and 276.46 ± 0.03 mg g −1 , respectively). Furthermore, for derivatives the optimal reaction medium conditions were pH 7.0 and 30 °C, confirming the advantage associated with lipase immobilization, obtaining activity values of 84.0 ± 2.12 U, 72.3 ± 1.7 U and 31.4 ± 1.9 U, for lipase immobilized on CCACM, CCAC and native form, respectively. The derivatives showed potential application in the synthesis of isoamyl acetate ester, with conversions above 90% and stability during five cycles of use. CONCLUSION:The activated carbon metallization process showed an increase in lipase immobilization efficiency and proved to be a promising support, since there was an increase in its enzymatic activity and the derivatives obtained showed potential application in aroma synthesis, reaching conversion above 90%.

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“…For the other tested lipases from Candida antarctica [49][50][51][52][53], Thermomyces lanuginosa [54][55][56][57], Rhizomucor Fig. 7 Biocatalyst effect: educt amounts and product yields after transesterification catalyzed by different immobilized lipases.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic transesterification of urethane-bond containing ester

et al. 2020

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Here we demonstrate the feasibility and successful application of enzymes in polyurethane network synthesis as well as occurring hurdles that have to be addressed when using urethanes synthesis substrates. The enzymatic transesterification of an urethanebond containing monofunctional ester and a model alcohol carbitol using lipases is discussed. The reaction is optimized in terms of transesterification time and temperature, the reaction solvent, the possibility of a cosolvent and the alcohol amount, the used transesterification environment, and the biocatalyst. Enzymatic cross-linking of polyurethanes can open up a pool of new possibilities for cross-linking and related polyurethane network properties due to the enzymes high enantio-, stereo-, and regioselectivity and broad substrate spectrum.

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Highly stable adsorptive and covalent immobilization of Thermomyces lanuginosus lipase on tailor-made porous carbon material

Cited by 28 publications

References 92 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

Incorporation of metallic particles in activated carbon used in lipase immobilization for production of isoamyl acetate

Enzymatic transesterification of urethane-bond containing ester

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