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Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine DOPA and Its Application to Protein Conjugation
Published on: August 24, 2018
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Microplate based optical biosensor for L-Dopa using tyrosinase from Amorphophallus campanulatus
Amardeep Singh Saini1, Jitendra Kumar1, Jose Savio Melo1
1Nuclear Agriculture and Biotechnology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.
Analytica Chimica Acta
|October 11, 2014
Summary
This study presents a novel microplate biosensor for detecting l-Dopa (L-3,4-dihydroxyphenylalanine) using immobilized tyrosinase enzyme. The biosensor offers simultaneous multi-sample analysis with high sensitivity and reusability.
Area of Science:
- Biochemistry
- Biosensor Technology
- Analytical Chemistry
Background:
- Simultaneous monitoring of l-Dopa levels in multiple samples is crucial.
- Developing biosensors with small reaction volumes is highly desirable for efficiency.
Purpose of the Study:
- To develop a microplate-based biosensor for sensitive and simultaneous detection of l-Dopa.
- To immobilize tyrosinase enzyme effectively for enhanced biosensor performance.
Main Methods:
- Tyrosinase enzyme from Amorphophallus campanulatus was immobilized on microplate wells using glutaraldehyde.
- Environmental Scanning Electron Microscope-Energy Dispersive System (ESEM-EDS) and Atomic Force Microscopy (AFM) confirmed enzyme immobilization.
- An optical transducer was integrated for l-Dopa detection by measuring dopachrome formation at 475 nm.
Main Results:
- The biosensor demonstrated good reproducibility and a linear detection range of 10-1000 μM for l-Dopa.
- A low detection limit of 3 μM was achieved.
- The immobilized enzyme retained stability for 41 days and was reused up to nine times.
Conclusions:
- The developed microplate biosensor is a convenient and effective system for simultaneous l-Dopa detection in multiple samples.
- This approach offers a sensitive and reusable platform for l-Dopa analysis, applicable to real samples like blood plasma.
