ArticleMolecular biotechnology2017
Medium Optimization for Improved Production of Dihydrolipohyl Dehydrogenase from Bacillus sphaericus PAD-91 in Escherichia coli.
Article in Molecular biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 13 citations in OpenAlex.
- Chemical Composition, Molecular Docking Analysis, and Biological Properties ofAdvanced biomedical research · 2025Article
- Optimizing recombinant mini proinsulin production via response surface method and microbioreactor screening.PloS one · 2025Article
- Media optimization for SHuffle T7 Escherichia coli expressing SUMO-Lispro proinsulin by response surface methodology.BMC biotechnology · 2022Article
- Human DT-diaphorase expression inVeterinary research forum : an international quarterly journal · 2022Article
- The Effective Control of Hyperuricemia in Cancer Patients: A New Recombinant Conjugated Variant of Urate Oxidase.Asian Pacific journal of cancer prevention : APJCP · 2021Article
- Enhanced (Journal of microbiology and biotechnology · 2020Article
- Enhanced L-methionine production by genetically engineered3 Biotech · 2019Article
- Genetic and physiological basis for antibody production by Kluyveromyces marxianus.AMB Express · 2018Article
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2 authors at 1 institution in 1 country.
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Abstract
Dihydrolipohyl dehydrogenase (DLD) is a FAD-dependent enzyme that catalyzes the reversible oxidation of dihydrolipoamide. Herein, we report medium optimization for the production of a recombinant DLD with NADH-dependent diaphorase activity from a strain of Bacillus sphaericus PAD-91. The DLD gene that consisted of 1413 bp was expressed in Escherichia coli BL21 (DE3), and its enzymatic properties were studied. The composition of production medium was optimized using one-variable-at-a-time method followed by response surface methodology (RSM). B. sphaericus DLD catalyzed the reduction of lipoamide by NAD
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