Recent advances of enzyme biosensors for pesticide detection in foods
Journal of Food Measurement and Characterization, ISSN: 2193-4134, Vol: 15, Issue: 5, Page: 4582-4595
2021
- 42Citations
- 83Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Review Description
Many enzymatic electrochemical biosensors have been developed as user-friendly and time-saving analytical methods to detect many analytes for food and environmental analysis in recent years. In recent years, many biosensing methods have been developed for the detection of pesticides using integrated enzymatic biosensors. Based on enzymatic biosensors, various electrochemical signal converters, different enzyme immobilization methods, and various measurement methodologies have improved. Enzymatic detection of pesticides is mostly based on the inhibition of selected enzymes such as organophosphate hydrolase, cholinesterases, ascorbate oxidase, alkaline and acid phosphatase, aldehyde dehydrogenase, and acetolactate synthase. This review, focused on enzymatic electrochemical biosensors, aims to focus on the latest advances in the development of innovative electrochemical mediators and new enzymatic immobilization strategies to realize highly sensitive, selective, and stable biosensors for food and environmental applications. In this review, the latest studies on enzyme-based biosensors for pesticide detection in food samples between 2016 and 2021 were summarized.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85108810414&origin=inward; http://dx.doi.org/10.1007/s11694-021-01032-3; https://link.springer.com/10.1007/s11694-021-01032-3; https://link.springer.com/content/pdf/10.1007/s11694-021-01032-3.pdf; https://link.springer.com/article/10.1007/s11694-021-01032-3/fulltext.html; https://dx.doi.org/10.1007/s11694-021-01032-3; https://link.springer.com/article/10.1007/s11694-021-01032-3
Springer Science and Business Media LLC
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