Studies on the properties of graphene oxide–alkaline protease bio-composites

Su, Ruijing; Shi, Penghui; Zhu, Meifang; Hong, Feng; Li, Dengxin

doi:10.1016/j.biortech.2011.12.085

Cited by 59 publications

(28 citation statements)

References 29 publications

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“…For example, using glutaraldehyde as a cross-linker, alkaline protease was covalently attached on the GO sheets [124] . A more complicated protocol was proposed and used to immobilize trypsin chemically on the GO sheets by Xu et al [125] .…”

Section: Covalently Binding Enzyme/protein On Gomentioning

confidence: 99%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

209

107

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This review selectively describes the recent progress in the interactions of proteins (enzymes) and shortchain peptides with graphene and graphene oxide (GO). Particularly, the advances of the immobilization mechanisms of enzymes on graphene and GO, the catalytic properties of the immobilized enzymes, and their applications are summarized in detail. The interfacings of the peptides with graphene and GO, the as assembled conjugates, and their potential applications are discussed briefly. The possible ongoing development for the assembly of conjugates of graphene and GO with proteins and peptides in a controlled manner is speculated upon.

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Section: Covalently Binding Enzyme/protein On Gomentioning

confidence: 99%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

209

107

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“…Several studies have reported the immobilization of peptides and enzymes on GO via covalent bonding or non-covalent interactions (Pavlidis et al, 2012;Su et al, 2012;Zhang et al, 2010;Zhang et al, 2011;Zhang et al, 2013). Alkaline protease immobilized on GO exhibited enhanced thermal stability at its optimum temperature of 60°C (Su et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Increased thermal stability of cold-adapted esterase at ambient temperatures by immobilization on graphene oxide

Lee

Jeong

Han

et al. 2013

Bioresource Technology

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“…facilitate continuous operation, recover substrate and product, significantly reduce costs, and prevent product contamination (Su et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Facile preparation of magnetically functionalized graphite nanosheets for porcine pancreatic lipase immobilization

Hou

Zhu

et al. 2014

J Nanopart Res

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The graphite nanosheets decorated with Fe 3 O 4 nanoparticles (about 15-20 nm), i.e., Fe 3 O 4 @graphite nanosheets, have been prepared via a facile one-pot method. The resulting composites with large specific surface area, high affinity, and rapid magnetic response were characterized by means of Fourier transform infrared spectra, Raman spectra, powder X-ray diffraction, scanning electron microscopy, transmission electron microscopy, elemental analysis, and thermogravimetric analysis, which indicated that the Fe 3 O 4 nanoparticles were chemically integrated on the graphite nanosheets. The porcine pancreatic lipase (PPL) was immobilized onto the Fe 3 O 4 @graphite nanosheets through covalent bonding using glutaraldehyde as a coupling reagent, and the properties of the resulting immobilized PPL such as enzymatic activity, stability, and reusability were researched at the same time. The result proved that the immobilized PPL displayed excellent properties and demonstrated that the prepared Fe 3 O 4 @graphite nanosheets would present a potential application as a novel carrier for enzyme immobilization, enrichment, and separation.

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Studies on the properties of graphene oxide–alkaline protease bio-composites

Cited by 59 publications

References 29 publications

Interactions of graphene and graphene oxide with proteins and peptides

Interactions of graphene and graphene oxide with proteins and peptides

Increased thermal stability of cold-adapted esterase at ambient temperatures by immobilization on graphene oxide

Facile preparation of magnetically functionalized graphite nanosheets for porcine pancreatic lipase immobilization

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