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Cytochrome P450 electrochemical biosensors transforming in vitro metabolism testing - Opportunities and challenges.

Bioelectrochemistry

January 2025

LAQV-REQUIMTE, Laboratory of Applied Chemistry, Department of Chemical Sciences, Faculty of Pharmacy, University of Porto, 4050-313 Porto, Portugal. Electronic address:

The ability of the living world to flourish in the face of constant exposure to dangerous chemicals depends on the management ability of a widespread group of enzymes known as heme-thiolate monooxygenases or cytochrome P450 superfamily. About three-quarters of all reactions determining the metabolism of endogenous compounds, of those carried in foods, of taken drugs, or even of synthetic chemicals discarded into the environment depend on their catalytic performance. The chromatographic and (photo)luminometric methods routinely used as predictive and analytical tools in laboratories have significant drawbacks ranging from limited shelf-life of reagents, use of synthetic substrates, laborious and tedious procedures for highly sensitive detection.

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Biologically mediated adsorption and precipitation of phosphorus (P) from waste streams can restrict environmental P discharges. Here, we appraise progress in this field over the past decade. The research discipline has grown considerably in recent years.

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Lipases, enzymes that perform the hydrolysis of triglycerides into fatty acids and glycerol, present a potential paradigm shift in the realms of food and detergent industries. Their enhanced efficiency, energy conservation and environmentally friendly attributes make them promising substitutes for chemical catalysts. Motivated by this prospect, this present study was targeted on the heterologous expression of a lipase gene, employing E.

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Engineering silica nanocoated whole-cell asymmetric biocatalyst for efficient preparation of a key chiral intermediate of (S)-Rivastigmine.

J Biotechnol

January 2025

Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China. Electronic address:

In our previous study, the whole cells containing an aldo-keto reductase (yhdN) and glucose dehydrogenase (GDH) were constructed and applied in a stereoselective carbonyl reduction reaction to prepare (S)-NEMCA-HEPE, being a key chiral intermediate of (S)-Rivastigmine which is widely prescribed for the treatment of Alzheimer's disease. Although the conversion and enantiomeric excess (e.e.

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Enzymes are natural biocatalysts with the advantages such as high catalytic efficiency, and strong substrate selectivity. However, the features of structure instability and low reusability rates have limited the industrial applications of enzyme. Fortunately, advancements in technology have made enzyme immobilization possible.

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