ArticleApplied microbiology and biotechnology2020
Site-directed mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin.
Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 26 citations in OpenAlex.
- Transforming a Historical Chemical Synthetic Route for Vanillin Starting from Renewable Eugenol to a Cell-Free Bi-Enzymatic Cascade.ChemSusChem · 2025Article
- Robust enzyme discovery and engineering with deep learning using CataPro.Nature communications · 2025Article
- Engineering a coenzyme-independent dioxygenase for one-step production of vanillin from ferulic acid.Applied and environmental microbiology · 2024Article
- Strategies for improving the production of bio-based vanillin.Microbial cell factories · 2023Review
- Bio-Based Valorization of Lignin-Derived Phenolic Compounds: A Review.Biomolecules · 2023Review
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- The Effect of Xylooligosaccharide, Xylan, and Whole Wheat Bran on the Human Gut Bacteria.Frontiers in microbiology · 2020Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Vanillin is a popular flavoring compound and an important food additive. Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized. This system produces a slightly higher production yield (40.20%) than the largest yield reported for immobilized FDC and CSO2 (35.00%) with ferulic acid as a substrate. It was previously reported that the low catalytic activity and thermal instability of CSO2 restrict the overall productivity of vanillin. In present study, site-directed mutagenesis was applied to rate-limiting oxygenase CSO2 to generate positive mutants. The production yields of mutants A49P (58.44%) and Q390A (65.29%) were 1.45- and 1.62-fold that of CSO2 wild type, respectively. The potential mechanism for enhanced vanillin production using A49P involved increased thermostability and catalytic efficiency, while that using Q390A was probably associated with a better thermostable performance and increased catalytic efficiency resulting from a larger entrance channel.
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