ArticleJournal of industrial microbiology & biotechnology2011
Overexpression of a recombinant amidase in a complex auto-inducing culture: purification, biochemical characterization, and regio- and stereoselectivity.
Article in Journal of industrial microbiology & biotechnology, 2011. 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, 27 citations in OpenAlex.
- Enzymatic Cascades for Stereoselective and Regioselective Amide Bond Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Recombinant Amidases: Recent Insights and its Applications in the Production of Industrially Important Fine Chemicals.Molecular biotechnology · 2025Review
- Machine learning-assisted amidase-catalytic enantioselectivity prediction and rational design of variants for improving enantioselectivity.Nature communications · 2024Article
- A new concept of biocatalytic synthesis of acrylic monomers for obtaining water-soluble acrylic heteropolymers.Metabolic engineering communications · 2024Article
- A novel amidase from Brevibacterium epidermidis ZJB-07021: gene cloning, refolding and application in butyrylhydroxamic acid synthesis.Journal of industrial microbiology & biotechnology · 2016Article
- Molecular dynamic analysis of mutant Y195I α-cyclodextrin glycosyltransferase with switched product specificity from α-cyclodextrin to γ-cyclodextrin.Journal of molecular modeling · 2015Article
- Purification and characterization of a novel thermo-active amidase from Geobacillus subterraneus RL-2a.Extremophiles : life under extreme conditions · 2013Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodococcus erythropolis AJ270 metabolizes a wide range of nitriles via the two-step nitrile hydratase/amidase pathway. In this study, an amidase gene from R. erythropolis AJ270 was cloned and expressed in Escherichia coli BL21 (DE3). The activity reached the highest level of 22.04 U/ml in a complex auto-inducing medium using a simplified process of fermentation operation. The recombinant amidase was purified to more than 95% from the crude lysate using Ni-NTA affinity chromatography and Superose S10-300 gel filtration. The V(max) and K(m) values of the purified enzyme with acetamide (50 mM) were 6.89 μmol/min/mg protein and 4.12 mM, respectively, which are similar to those of the enzyme from the wild-type cell. The enzyme converted racemic α-substituted amides, O-benzylated β-hydroxy amides, and N-benzylated β-amino amides to the corresponding (S)-acids with remarkably high enantioselectivity. The ionic liquid [BMIm][PF₆] (1-butyl-3-methylimidazolium hexafluorophosphate) enhanced the activity by 1.5-fold compared with water. The adequate expression of the enzyme and excellent enantioselectivity of the recombinant amidase to a broad spectrum of amides suggest that the enzyme has prospective industrial-scale practical applications in pharmaceutical chemistry.
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