ArticleScientific reports2015
One-step biosynthesis of α-ketoisocaproate from L-leucine by an Escherichia coli whole-cell biocatalyst expressing an L-amino acid deaminase from Proteus vulgaris.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 37 citations in OpenAlex.
- Alpha-Ketoisocaproate Attenuates Muscle Atrophy in Cancer Cachexia Models.Journal of cachexia, sarcopenia and muscle · 2025Article
- Development of a Multienzyme Cascade for Salvianolic Acid A Synthesis from l-Tyrosine.ACS omega · 2025Article
- The modification of heme special importer to improve the production of active hemoglobins in Escherichia coli.Biotechnology letters · 2024Article
- Dual contribution of the mTOR pathway and of the metabolism of amino acids in prostate cancer.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- Production of Salvianic Acid A from l-DOPA via Biocatalytic Cascade Reactions.Molecules (Basel, Switzerland) · 2022Article
- Semi-rational engineering membrane binding domain of L-amino acid deaminase fromFrontiers in microbiology · 2022Article
- Efficient Synthesis of (Frontiers in bioengineering and biotechnology · 2022Article
- Engineering of L-amino acid deaminases for the production of α-keto acids from L-amino acids.Bioengineered · 2019Review
- Highly selective synthesis of d-amino acids from readily available l-amino acids by a one-pot biocatalytic stereoinversion cascade.RSC advances · 2019Article
- Membrane binding of the insertion sequence of Proteus vulgaris L-amino acid deaminase stabilizes protein structure and increases catalytic activity.Scientific reports · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This work aimed to develop a whole-cell biotransformation process for the production of α-ketoisocaproate from L-leucine. A recombinant Escherichia coli strain was constructed by expressing an L-amino acid deaminase from Proteus vulgaris. To enhance α-ketoisocaproate production, the reaction conditions were optimized as follows: whole-cell biocatalyst 0.8 g/L, leucine concentration 13.1 g/L, temperature 35 °C, pH 7.5, and reaction time 20 h. Under the above conditions, the α-ketoisocaproate titer reached 12.7 g/L with a leucine conversion rate of 97.8%. In addition, different leucine feeding strategies were examined to increase the α-ketoisocaproate titer. When 13.1 g/L leucine was added at 2-h intervals (from 0 to 22 h, 12 addition times), the α-ketoisocaproate titer reached 69.1 g/L, while the leucine conversion rate decreased to 50.3%. We have developed an effective process for the biotechnological production of α-ketoisocaproate that is more environmentally friendly than the traditional petrochemical synthesis approach.
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