ArticleApplied microbiology and biotechnology2009
A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli.
Article in Applied microbiology and biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Skin microbiota in atopic dermatitis: victim or executioner?Clinical microbiology reviews · 2025Review
- Dual function of the O-antigen WaaL ligase of Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2023Article
- Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation.Biotechnology for biofuels and bioproducts · 2022Article
- Biochemical characterisation of a collagenase from Bacillus cereus strain Q1.Scientific reports · 2021Article
- Enhanced efficiency in isolation and expansion of hAMSCs via dual enzyme digestion and micro-carrier.Cell & bioscience · 2020Article
- Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.Journal of proteomics · 2014Article
- Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T.The Journal of biological chemistry · 2013Article
- Enhancement of the structural stability of full-length clostridial collagenase by calcium ions.Applied and environmental microbiology · 2012Article
- Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.Nature structural & molecular biology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Clostridial collagenases are foe and friend: on the one hand, these enzymes enable host infiltration and colonization by pathogenic clostridia, and on the other hand, they are valuable biotechnological tools due to their capacity to degrade various types of collagen and gelatine. However, the demand for high-grade preparations exceeds supply due to their pathogenic origin and the intricate purification of homogeneous isoforms. We present the establishment of an Escherichia coli expression system for a variety of constructs of collagenase G (ColG) and H (ColH) from Clostridium histolyticum and collagenase T (ColT) from Clostridium tetani, mimicking the isoforms in vivo. Based on a setup of five different expression strains and two expression vectors, 12 different constructs were expressed, and a flexible purification platform was established, consisting of various orthogonal chromatography steps adaptable to the individual needs of the respective variant. This fast, cost-effective, and easy-to-establish platform enabled us to obtain at least 10 mg of highly pure mono-isoformic protein per liter of culture, ideally suited for numerous sophisticated downstream applications. This production and purification platform paves the way for systematic screenings of recombinant collagenases to enlighten the biochemical function and to identify key residues and motifs in collagenolysis.
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Registered trials
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