Activation of polyvinyl chloride sheet surface for covalent immobilization of oxalate oxidase and its evaluation as inert support in urinary oxalate determination

Pundir, C.S.; Chauhan, Nar Singh; Bhambi, Manu

doi:10.1016/j.ab.2007.11.008

Cited by 41 publications

(19 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Barley OxO (98% identical to wheat germin) is used in kits to assay levels of oxalate in blood plasma and urine (Porowski et al, 2008), a process required in the treatment of patients with kidney stones (a crystallized form of calcium oxalate) (Marengo and Romani, 2008). Because of the importance of these diagnostic protocols, there is a continuous effort to improve the accuracy and efficiency of the assay (Fiorito et al, 2005;Bhambi and Pundir, 2007;Capra et al, 2007;Kumar et al, 2008;Pundir et al, 2008), and to develop more efficient heterologous expression systems for production of the purified enzyme, either in bacteria (Cassland et al, 2004) or yeast (Pan et al, 2007).…”

Section: B Germin and Medical Diagnosticsmentioning

confidence: 99%

Germin and Germin-like Proteins: Evolution, Structure, and Function

Dunwell

Gibbings

Mahmood

et al. 2008

Critical Reviews in Plant Sciences

205

161

View full text Add to dashboard Cite

Section: B Germin and Medical Diagnosticsmentioning

confidence: 99%

Germin and Germin-like Proteins: Evolution, Structure, and Function

Dunwell

Gibbings

Mahmood

et al. 2008

Critical Reviews in Plant Sciences

205

161

View full text Add to dashboard Cite

“…The effectiveness of biomolecule immobilization strongly depends on the thin film material (the support platform) that provides excellent stability, fast lateral wicking speed and reduces biomolecule desorption . Moreover, the thin film material should be insoluble in water and has a high binding capacity to the specifically targeted biomolecules . As an immunoassay, the biochemical reaction between antigen and antibody takes place on the surface of the porous support, which greatly influenced by the thin film morphology and its intrinsic chemical composition.…”

Section: Introductionmentioning

confidence: 99%

Morphological characteristics of polymeric nylon‐6 film as biological recognition interface for electrochemical immunosensor application

Shaimi

Low

2018

J of Applied Polymer Sci

View full text Add to dashboard Cite

The present study elucidates the morphology characteristic of nylon‐6 as protein immobilization film and their influences in biological recognition interface for a single‐use electrochemical immunosensor. A basic requirement of this polymer platform is to allow the testing analyte [conductive polyaniline‐Fe2O3‐glutaraldehyde‐conjugated‐N‐hydroxysuccinimidobiotin (PANI‐Fe2O3‐GA‐b‐NHS)] to access to the immobilized capture reagent [bovine serum albumin (BSA)] on a surface of the nylon‐6 film. As an immunoassay, the biochemical reaction between PANI‐Fe2O3‐GA‐b‐NHS and BSA takes place on a surface of the nylon‐6 support film, which then translated into measurable resistance signal through pulse‐mode measurement. The in‐house developed nylon‐6 film, N‐16B, with 16 wt % nylon polymer and methanol as nonsolvent had demonstrated the fastest lateral wicking speed (1.07 mm s−1) and excellent protein immobilization capacity (1650 ± 85.84 μg cm−3), leading to the higher electrical current signal with a minimal resistance of electrochemical responses (0.57 ± 0.04 MΩ). This work reflects the importance of the physical characteristics of the nylon‐6 film that determines the sensitivity and effectiveness of an immunosensor. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018, 135, 46741.

show abstract

“…During immobilization, vinyl polymers of plasticized PVC material were broken down by treating it with a HNO3 and H2SO4 mixture, which introduced nicks in the long-chain polymer, and generated free ends protruding from the polymer surface. 33 When free ends of the treated polymer were reacted with the aldehyde group of a bifunctional cross-linking agent, such as glutaraldehyde, one aldehyde group of a glutraldehyde reacted with the free end of the vinyl chain to form a -C=CH-bond between the plasticized PVC sheet of glutraldehyde, and thus led to activation of the surface for covalent immobilization of the enzymes. The -NH2 group on the surface of the enzyme was attached covalently onto another -CHO group of glutraldehyde, already attached to the plasticized PVC sheet, through Schiff-base formation.…”

Section: Immobilization Of Uricase Onto Plasticized Pvc/plastic Vialmentioning

confidence: 99%

“…33 The plasticized PVC surface was first treated with nitrating acid (mixture of conc. nitric acid and sulfuric acid in a 5:1 ratio) for 6 h to cleave plasticized PVC polymers oxidatively into small chain polymers having protruding ends toward the surface.…”

Section: Immobilization Of Uricase In Plasticized Pvc Vialmentioning

confidence: 99%

“…33,34 This report describes for the first time, the covalent immobilization of uricase on the inner wall of a plasticized PVC vial and its application for the determination of uric acid in serum and urine. The proposed plasticized PVC vial is expected to find its immediate use in the determination of serum/urine uric acid in clinical laboratories/hospitals for the diagnosis and medical management of gout patients and stone formers.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Covalent Immobilization of Uricase Inside a Plastic Vial for Uric Acid Determination in Serum and Urine

et al. 2014

View full text Add to dashboard Cite

Experimental Reagents and solutionsRecombinant uricase from Candida species expressed in E. coli, 4-aminophenazone, glutaraldehyde, uric acid, DEAE-Sephacel and Sephadex G-100 from Sigma Aldrich Co. (St. Louis, MO) and uric acid from SRL (Mumbai, India) were used. All other chemicals were of analytical reagent grade. Uricase from Candida species was immobilized covalently onto the inner wall of a plasticized polyvinyl chloride (PVC/plastic) vial through glutraldehyde coupling with a 65.23% retention of its initial activity and a conjugation yield of 0.37 mg/cm 2 . The vial-bound enzyme showed the optimum activity at pH 7.2, when incubated at 45 C for 5 min. There was a linear relationship between the immobilized uricase activity and the uric acid concentration in the range of 0.01 to 1.2 mM with an apparent Km for uric acid of 0.17 mM. The vial-bound enzyme was employed for an enzymic colorimetric determination of uric acid in serum and urine. The minimum detection limit of the method was 0.01 mM. The analytical recoveries of added uric acid in serum (10 and 20 mM) were 98.0 and 96.5%, respectively. Within and between assays, the coefficients of variation (CVs) for urate in sera determinations were 5.6 and 4.7%, respectively. A good correlation (r = 0.997) was obtained between the serum uric acid values by the standard enzymic colorimetric method using free enzyme and the present method. The vial was reused 200-times over a period of 4 months, when stored at 4 C.

show abstract

Activation of polyvinyl chloride sheet surface for covalent immobilization of oxalate oxidase and its evaluation as inert support in urinary oxalate determination

Cited by 41 publications

References 23 publications

Germin and Germin-like Proteins: Evolution, Structure, and Function

Germin and Germin-like Proteins: Evolution, Structure, and Function

Morphological characteristics of polymeric nylon‐6 film as biological recognition interface for electrochemical immunosensor application

Covalent Immobilization of Uricase Inside a Plastic Vial for Uric Acid Determination in Serum and Urine

Contact Info

Product

Resources

About