A Disposable Optrode Using Immobilized Tyrosinase Films

Paranjpe, Pallavi S; Dutta, Sabari; Karve, Meena; Padhyé, Subhash; Narayanaswamy, Ramaier

doi:10.1006/abio.2001.5154

Cited by 25 publications

(8 citation statements)

References 20 publications

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“…LOD values are comparable with other spectroscopic procedures using purified tyrosinase [15,[44][45][46][47][48] (Table 7). For l-tyrosine, no spectroscopic procedures were found in the literature; however, the comparison with electrochemical determination (LOD 1.0 × 10 −5 M [49]) allows us to conclude the same.…”

Section: Analytical Applicationsupporting

confidence: 77%

Agaricus bisporus Crude Extract: Characterization and Analytical Application

et al. 2020

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In the present work crude Agaricus bisporus extract (ABE) has been prepared and characterized by its tyrosinase activity, protein composition and substrate specificity. The presence of mushroom tyrosinase (PPO3) in ABE has been confirmed using two-dimensional electrophoresis, followed by MALDI TOF/TOF MS-based analysis. GH27 alpha-glucosidases, GH47 alpha-mannosidases, GH20 hexosaminidases, and alkaline phosphatases have been also detected in ABE. ABE substrate specificity has been studied using 19 phenolic compounds: polyphenols (catechol, gallic, caffeic, chlorogenic, and ferulic acids, quercetin, rutin, dihydroquercetin, l-dihydroxyphenylalanine, resorcinol, propyl gallate) and monophenols (l-tyrosine, phenol, p-nitrophenol, o-nitrophenol, guaiacol, o-cresol, m-cresol, p-cresol). The comparison of ABE substrate specificity and affinity to the corresponding parameters of purified A. bisporus tyrosinase has revealed no major differences. The conditions for spectrophotometric determination have been chosen and the analytical procedures for determination of 1.4 × 10−4–1.0 × 10−3 M l-tyrosine, 3.1 × 10−6–1.0 × 10−4 M phenol, 5.4 × 10−5–1.0 × 10−3 M catechol, 8.5 × 10−5–1.0 × 10−3 M caffeic acid, 1.5 × 10−4–7.5 × 10−4 M chlorogenic acid, 6.8 × 10−5–1.0 × 10−3 M l-DOPA have been proposed. The procedures have been applied for the determination of l-tyrosine in food supplements, l-DOPA in synthetic serum, and phenol in waste water from the food manufacturing plant. Thus, we have demonstrated the possibility of using ABE as a substitute for tyrosinase in such analytical applications, as food supplements, medical and environmental analysis.

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Section: Analytical Applicationsupporting

confidence: 77%

Agaricus bisporus Crude Extract: Characterization and Analytical Application

et al. 2020

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“…For that reason immobilized tyrosinase in the form of an optical biosensor can be used as an alternative to the conventional methods of detecting chemical compounds. The preponderance of optical biosensors results from their particularly high sensitivity, small size and cost effectiveness [13,36,37]. Tyrosinase immobilized on jellose/agarose membrane was used to detect and estimate micromolar quantities of 3,4-dihydroxyphenylalanine (L-DOPA)—a clinical indicator in the detection of pigmentory disorders.…”

Section: Immobilized Polyphenol Oxidases–valuable Enzymes In Biotementioning

confidence: 99%

“…Tyrosinase immobilized on jellose/agarose membrane was used to detect and estimate micromolar quantities of 3,4-dihydroxyphenylalanine (L-DOPA)—a clinical indicator in the detection of pigmentory disorders. However, this matrix is semi-opaque and the absorption of the light passing through the matrix causes only partial work of the sensor [36]. For this reason chitosan seems to be a better matrix for the construction of the optical biosensors.…”

Section: Immobilized Polyphenol Oxidases–valuable Enzymes In Biotementioning

confidence: 99%

Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

2014

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Abstract:The main objective of the immobilization of enzymes is to enhance the economics of biocatalytic processes. Immobilization allows one to re-use the enzyme for an extended period of time and enables easier separation of the catalyst from the product. Additionally, immobilization improves many properties of enzymes such as performance in organic solvents, pH tolerance, heat stability or the functional stability. Increasing the structural rigidity of the protein and stabilization of multimeric enzymes which prevents dissociation-related inactivation. In the last decade, several papers about immobilization methods have been published. In our work, we present a relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value. We also present our view on the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes.

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“…When a product is colorless, an indicator can interact with it to produce a change in color [64]. The colored product can also be detected by reflectance with a bifurcated optical fiber [65]. Anomalous reflection (AR) refers to the decrease in reflectivity of a gold surface under blue or violet light due to the adsorption of a surface layer, which is applicable to affinity biosensors based on fiber optics [66].…”

Section: Sensing Schemesmentioning

confidence: 99%

Miniature fiber-optic multicavity Fabry–Perot interferometric biosensor

et al. 2005

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(ABSTRACT)Fiber-optic Fabry-Perot interferometric (FFPI) sensors have been widely used due to their high sensitivity, ease of fabrication, miniature size, and capability for multiplexing. However, direct measurement of self-assembled thin films, receptor immobilization process or biological reaction is limited in the FFPI technique due to the difficulty of forming Fabry-Perot cavities by the thin film itself. Novel methods are needed to provide an accurate and reliable measurement for monitoring the thin-film growth in the nanometer range and under various conditions. In this work, two types of fiber-optic multicavity Fabry-Perot interferometric (MFPI) sensors with built-in temperature compensation were designed and fabricated for thin-film measurement, with applications in chemical and biological sensing. Both the tubing-based MFPI sensor and microgap MFPI sensor provide simple, yet high performance solutions for thin-film sensing. The temperature dependence of the sensing cavity is compensated by extracting the temperature information from a second multiplexed cavity. This provides the opportunity to examine the thin-film characteristics under different environment temperatures.To demonstrate the potential of this structure for practical applications, immunosensors were fabricated and tested using these structures. Self-assembled polyelectrolytes served as a precursor film for immobilization of antibodies to ensure they retain their biological activity. This not only provides a convenient method for protein immobilization but also presents the possibility of increasing the binding capacity

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A Disposable Optrode Using Immobilized Tyrosinase Films

Cited by 25 publications

References 20 publications

Agaricus bisporus Crude Extract: Characterization and Analytical Application

Agaricus bisporus Crude Extract: Characterization and Analytical Application

Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

Miniature fiber-optic multicavity Fabry–Perot interferometric biosensor

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