Immobilization of cellulase on a silica gel substrate modified using a 3-APTES self-assembled monolayer

Zhang, Dezhi; Hegab, H.; Lvov, Yuri; Snow, Lynn; Palmer, James M.

doi:10.1186/s40064-016-1682-y

Cited by 89 publications

(72 citation statements)

References 55 publications

(100 reference statements)

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“…Importantly, the characteristic amide peaks are also present in the final immobilized product–the MWCNT/PPy/PEG–inulinase. However, the bands have lower intensity due to the lower concentration of inulinase in the immobilized preparation . This FTIR data unambiguously confirm that the enzyme becomes successfully incorporated into the target nanocomposite.…”

Section: Resultssupporting

confidence: 65%

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

Temkov

Petrovski

Gjorgieva

et al. 2019

Engineering in Life Sciences

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This paper describes the development of a simple method for mixed non‐covalent and covalent bonding of partially purified inulinase on functionalized multiwall carbon nanotubes (f‐MWCNTs) with polypyrrole (PPy). The pyrrole (Py) was electrochemically polymerized on MWCNTs in order to fabricate MWCNTs/PPy nanocomposite. Two multiple forms of enzyme were bound to N‐H functional groups from PPy and ‐COO− from activated MWCNTs to yield a stable MWCNTs/PPy/PEG immobilized preparation with increased thermal stability. Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) were used to confirm functionalization of nanoparticles and immobilization of the enzyme. The immobilization yield of 85% and optimal enzyme load of 345 μg protein onto MWCNTs was obtained. The optimum reaction conditions and kinetic parameters were established using the UV‐Vis analytical assay. The best functional performance for prepared heterogeneous catalyst has been observed at pH 3.6 and 10, and at the temperatures of 60 and 80ºC. The half‐life (t1/2) of the immobilized inulinase at 60 and 80ºC was found to be 231 and 99 min, respectively. The reusability of the immobilized formulation was evaluated based on a method in which the enzyme retained 50% of its initial activity, which occurred after the eighteenth operation cycle.

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Section: Resultssupporting

confidence: 65%

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

Temkov

Petrovski

Gjorgieva

et al. 2019

Engineering in Life Sciences

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“…This can probably be attributed to a reduction in the dissociation of peptide subunits and in the enzyme denaturation rate [39]. A significant increase in the storage stability of immobilized cellulase was also reported when graphene oxide supplemented by magnesium oxide nanoparticles was used as a support.…”

Section: Stability Study Of Immobilized Cellulasementioning

confidence: 93%

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

et al. 2017

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Abstract:Cellulase from Aspergillus niger was immobilized on a synthesized TiO 2 -lignin hybrid support. The enzyme was effectively deposited on the inorganic-organic hybrid matrix, mainly via physical interactions. The optimal initial immobilization parameters, selected for the highest relative activity, were pH 5.0, 6 h process duration, and an enzyme solution concentration of 5 mg/mL. Moreover, the effects of pH, temperature, and number of consecutive catalytic cycles and the storage stability of free and immobilized cellulase were evaluated and compared. Thermal and chemical stability were significantly improved, while after 3 h at a temperature of 50 • C and pH 6.0, the immobilized cellulase retained over 80% of its initial activity. In addition, the half-life of the immobilized cellulase (307 min) was five times that of the free enzyme (63 min). After ten repeated catalytic cycles, the immobilized biocatalyst retained over 90% of its initial catalytic properties. This study presents a protocol for the production of highly stable and reusable biocatalytic systems for practical application in the hydrolysis of cellulose.

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“…Silica nanoparticles with well‐defined morphology and structures have good biocompatibility and stability, as well as high porosity, good transparency, low toxicity, high permeability and mechanical stability, and an easily controllable and functionalized surface . Because of these properties, silica has been used in the immobilization of various enzymes, including lipase, catalase, cellulase, and peroxidase …”

Section: Introductionmentioning

confidence: 99%

Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

Kołodziejczak-Radzimska

Zdarta

Jesionowski

2018

Biotechnology Progress

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Acylase I from Aspergillus melleus was immobilized on supports consisting of unmodified and modified silica. Modification was performed using 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The effectiveness of immobilization was investigated using the standard Bradford method in addition to a number of physicochemical techniques, including spectroscopic methods (FTIR, Si and C CP MAS NMR), porous structure and elemental analysis, and zeta potential measurement. A determination of catalytic activity was made based on the deacetylation reaction of N-acetyl-l-methionine. Furthermore, the effect of pH and temperature on the catalytic activity of the free and immobilized enzyme, as well as the reusability of the silica-bound aminoacylase, were determined. The immobilized systems demonstrated a high degree of catalytic activity. The best catalytic parameters were those of aminoacylase immobilized on silica modified with APTES (apparent activity 3937 U/g, relative activity 61.6%). © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:767-777, 2018.

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Immobilization of cellulase on a silica gel substrate modified using a 3-APTES self-assembled monolayer

Cited by 89 publications

References 55 publications

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

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