ArticleBMC biotechnology2018
Cloning and characterization of enoate reductase with high β-ionone to dihydro-β-ionone bioconversion productivity.
Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Characteristics and functions of volatile organic compounds in the tripartite symbiotic system ofPlant signaling & behavior · 2024Article
- Applications of Ene-Reductases in the Synthesis of Flavors and Fragrances.Journal of agricultural and food chemistry · 2024Review
- Purification and biochemical characterization of a novel ene- reductase from Kazachstania exigua HSC6 for dihydro-β-ionone from β-ionone.Biotechnology letters · 2023Article
- Analyzing Volatile Compounds of Young and MatureFoods (Basel, Switzerland) · 2022Article
- Sixty-One Volatiles Have Phylogenetic Signals Across Bacterial Domain and Fungal Kingdom.Frontiers in microbiology · 2020Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDihydro-β-ionone is a principal aroma compound and has received considerable attention by flavor and fragrance industry. The traditional method of preparing dihydro-β-ionone has many drawbacks, which has restricted its industrial application. Therefore, it is necessary to find a biotechnological method to produce dihydro-β-ionone.
resultsIn this study, the enoate reductase with high conversion efficiency of β-ionone to dihydro-β-ionone, DBR1, was obtained by screening four genetically engineered bacteria. The product, dihydro-β-ionone, was analyzed by GC and GC-MS. The highest dihydro-β-ionone production with 308.3 mg/L was detected in the recombinant strain expressing DBR1 which was later on expressed and purified. Its optimal temperature and pH were 45 °C and 6.5, respectively. The greatest activity of the purified enzyme was 356.39 U/mg using β-ionone as substrate. In the enzymatic conversion system, 1 mM of β-ionone was transformed into 91.08 mg/L of dihydro-β-ionone with 93.80% of molar conversion.
conclusionDBR1 had high selectivity to hydrogenated the 10,11-unsaturated double bond of β-ionone as well as high catalytic efficiency for the conversion of β-ionone to dihydro-β-ionone. It is the first report on the bioconversion of β-ionone to dihydro-β-ionone by using enoate reductase.
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