Cicer α-galactosidase immobilization onto functionalized graphene nanosheets using response surface method and its applications

Singh, Neera; Srivastava, Garima; Talat, Mahe; Raghubanshi, Himanshu; Srivastava, O. N.; Kayastha, Arvind M.

doi:10.1016/j.foodchem.2013.07.079

Cited by 79 publications

(32 citation statements)

References 21 publications

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“…This property further confirmed the enzyme molecules were adsorbed by graphene sheets. A different result was shown in the FT-IR spectra when cicer α -galactosidase was immobilized on graphene 28 . Compared with this reference, the light transmission of graphene-immobilized naringinase was lower.…”

Section: Resultsmentioning

confidence: 77%

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Gong

Zhu

et al. 2017

Sci Rep

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Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inability to the biocatalysts in microchannel reactors. A fluid and unsinkable immobilized enzyme were firstly applied in a microchannel reactor for biocatalysis in this study. Functionalized forms of graphene-immobilized naringinase flowing in microchannels have yielded excellent results for isoquercitrin production. A maximum yield of 92.24 ± 3.26% was obtained after 20 min in a microchannel reactor. Ten cycles of enzymatic hydrolysis reaction were successively completed and an enzyme activity above 85.51 ± 2.76% was maintained. The kinetic parameter V m/K m increased to 1.9-fold and reaction time was decreased to 1/3 compared with that in a batch reactor. These results indicated that the moving and unsinkable graphene sheets immobilized enzyme with a high persistent specificity and a mild catalytic characteristic enabled the repetitive use of enzyme and significant cost saving for the application of enzyme catalysis. Thus, the developed method has provided an efficient and simple approach for the productive and repeatable microfluidic biocatalysis.

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Section: Resultsmentioning

confidence: 77%

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Gong

Zhu

et al. 2017

Sci Rep

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“…The most common two-dimensional (2D) nanomaterials are probably those carbon-based ones, such as graphene, graphyne and their derivatives, which have attracted tremendous interests in many fields including biomedicine since its discovery1234567. Novel 2D nanomaterials, such as MoS 2 8, WS 2 9, and WO 3 10, are quickly catching up and emerge as a new research frontier.…”

mentioning

confidence: 99%

Robust Denaturation of Villin Headpiece by MoS2 Nanosheet: Potential Molecular Origin of the Nanotoxicity

Yang

Kang

et al. 2016

Sci Rep

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MoS2 nanosheet, a new two-dimensional transition metal dichalcogenides nanomaterial, has attracted significant attentions lately due to many potential promising biomedical applications. Meanwhile, there is also a growing concern on its biocompatibility, with little known on its interactions with various biomolecules such as proteins. In this study, we use all-atom molecular dynamics simulations to investigate the interaction of a MoS2 nanosheet with Villin Headpiece (HP35), a model protein widely used in protein folding studies. We find that MoS2 exhibits robust denaturing capability to HP35, with its secondary structures severely destroyed within hundreds of nanosecond simulations. Both aromatic and basic residues are critical for the protein anchoring onto MoS2 surface, which then triggers the successive protein unfolding process. The main driving force behind the adsorption process is the dispersion interaction between protein and MoS2 monolayer. Moreover, water molecules at the interface between some key hydrophobic residues (e.g. Trp-64) and MoS2 surface also help to accelerate the process driven by nanoscale drying, which provides a strong hydrophobic force. These findings might have shed new light on the potential nanotoxicity of MoS2 to proteins with atomic details, which should be helpful in guiding future biomedical applications of MoS2 with its nanotoxicity mitigated.

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“…The advantage of graphene over other nanomaterials is its ability to form uniform nanosheets of single carbon atoms, which provides a large and uniform area for the attachment of enzymes (Zhang et al, 2010). aand b-galactosidase enzymes have been immobilized on derivatized graphene nanosheets using cysteamine as the spacer arm and glutaraldehyde as the cross-linker (Singh et al, 2014). These nano-biocatalysts are easily separated from the reaction mixture using low-speed centrifugation or sedimentation methods, making the recovery process simple.…”

Section: The Application Of Nanotechnologymentioning

confidence: 99%

“…aand b-galactosidase enzymes have been immobilized on derivatized graphene nanosheets using cysteamine as the spacer arm and glutaraldehyde as the cross-linker (Singh et al, 2014). The immobilized enzyme has been used for the selective degradation of the raffinose family of oligosaccharides (RFOs) from soy milk, reducing the flatulence caused by consumption of soybean products (Singh et al, 2014). The a-galactosidase enzyme immobilized using this method showed an improved thermal stability from 50 to 80°C and also retained 70% residual activity after 12 repeated uses.…”

Section: The Application Of Nanotechnologymentioning

confidence: 99%

Enzyme engineering (immobilization) for food applications

Agyei

Shanbhag

2015

Improving and Tailoring Enzymes for Food Quality and Functionality

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Cicer α-galactosidase immobilization onto functionalized graphene nanosheets using response surface method and its applications

Cited by 79 publications

References 21 publications

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Robust Denaturation of Villin Headpiece by MoS2 Nanosheet: Potential Molecular Origin of the Nanotoxicity

Enzyme engineering (immobilization) for food applications

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