Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase

Roy, Joseph Jegan; Abraham, T. Emilia; Abhijith, K. S.; Kumar, Parveen; Thakur, M. S.

doi:10.1016/j.bios.2004.08.024

Cited by 128 publications

(48 citation statements)

References 17 publications

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“…When enzyme cross-linked with nanoparticle, neighbouring enzyme molecules sterically hinder the active centres of enzyme, so all enzyme molecules may not be available for the substrates, resulting the lower catalytic efficiency of enzyme. A lower catalytic efficiency of laccase crystal had been observed by Roy et al [35] wherein V max of CLEC laccase was only 12% than the V max of native laccase. Huang et al [22] …”

Section: Kinetic Studies Of Laccase Nanoparticlementioning

confidence: 89%

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Gahlout

Rudakiya

Gupte³

2017

Int Nano Lett

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Immobilization of enzyme with nanostructures enhances its ideal characteristics, which may allow the enzyme to become more stable and resistant. The present investigation deals with the formulation of laccase nanosilica conjugates to overcome the problems associated with its stability and reusability. Synthesized nanosilica and laccase nanoparticles were spherical shaped, with the mean size of 220 and 615 nm, respectively. Laccase nanoparticles had an optimum temperature of 55°C and pH 4.0 for the oxidation of ABTS. Laccase nanoparticle retained 79% of residual activity till 20th cycle. It also showed 91% of its initial activity at lower temperatures even after 60 days. Laccase nanoparticles were applied for Reactive Violet 1 degradation wherein 96.76% of decolourization was obtained at pH 5.0 and 30°C within 12 h. Toxicity studies on microbes and plants suggested that the degraded metabolites were less toxic than control dye. Thus, the method applied for immobilization increased storage stability and reusability of laccase, and therefore, it can be utilized for efficient degradation of azo dyes.

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Section: Kinetic Studies Of Laccase Nanoparticlementioning

confidence: 89%

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Gahlout

Rudakiya

Gupte³

2017

Int Nano Lett

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“…At the present time there is no ideal immobilization method generally usable for all enzymes, which have been anchored onto solid surfaces by a variety of techniques including adsorption cross-linking [3], sol-gel [4] and polymerization [5]. Unfortunately, in some cases films prepared by using these approaches present low reproducibility, stability and poor deposition homogeneity [6].…”

Section: Introductionmentioning

confidence: 97%

Acetylcholinesterase Immobilization on 3‐Mercaptopropionic Acid Self Assembled Monolayer for Determination of Pesticides

et al. 2007

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Studies on the immobilization of acetylcholinesterase onto a SAM gold electrode and the use of the fabricated biosensor for the determination of carbaryl and parathion are presented. The influence of pH, ionic strength, enzyme loading and concentration of glutaraldehyde on the response of the biosensor was investigated . The amperometric biosensor developed in this study provided linearity to parathion and carbaryl in the 2.0 a 30.0 Â 10 À6 mol L À1 concentration range. The detection limits under the optimum working conditions were found to be 9.3 mg L À1 for parathion and 9.0 mg L À1 for carbaryl. The enzyme electrode was found to be stable for 7 days.

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“…Application of CLECs in biosensor application have been reported using glucose oxidase (Mattos et al 2001), urease (Navia and St. Clair 1999), horseradish peroxidase (Roy and Abraham 2004), and recently with laccase (Roy et al 2005), for detection of compounds of medical and environmental importance. Compared to conventional immobilization of enzyme on electrode, CLECs exhibit increased sensitivity and stability.…”

Section: Introductionmentioning

confidence: 99%

Cross-linked enzyme crystals of organophosphate hydrolase for electrochemical detection of organophosphorus compounds

Laothanachareon

Champreda

Sritongkham

et al. 2008

World J Microbiol Biotechnol

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Cross-linked enzyme crystals of organophosphate hydrolase (CLEC-OPH) prepared from crude recombinant E. coli cell lysate was used for the development of an electrochemical biosensor for the detection of organophosphate pesticides. CLEC-OPH showed an increased V max of 0.721 U mg protein -1 and a slightly lower K m of 0.083 mM on paraoxon compared to the crude enzyme, resulting in an improved catalytic efficiency (k cat / K m = 4.17 9 10 5 M -1 min -1 ) with a remarkable increase on thermostability. An amperometric biosensor was constructed based on glutaraldehyde and albumin crosslinkage of CLEC-OPH with carbon nanotubes. The sensor exhibited greater sensitivity and operational stability with a lower limit of detection when compared with a sensor using an equivalent loading of crude OPH in a non-crystal form. The application of crude enzyme-based CLEC would offer a simple and economical approach for the fabrication of efficient electrochemical biosensors.

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Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase

Cited by 128 publications

References 17 publications

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Acetylcholinesterase Immobilization on 3‐Mercaptopropionic Acid Self Assembled Monolayer for Determination of Pesticides

Cross-linked enzyme crystals of organophosphate hydrolase for electrochemical detection of organophosphorus compounds

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