ArticleInternational journal of molecular sciences2021
Screening Collagenase Activity in Bacterial Lysate for Directed Enzyme Applications.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Dupuytren's disease cords are weakened ex vivo by injection of recombinant collagenase G - A proof-of-concept study.PloS one · 2026Article
- Discovering Skin Anti-Aging Potentials of the Most Abundant Flavone Phytochemical Compound Reported in Siam Violet Pearl, a Medicinal Plant from Thailand by In Silico and In Vitro Assessments.Antioxidants (Basel, Switzerland) · 2025Article
- Improving Tannery Wastewater Treatments Using an Additional Microbial Treatment with a Bacterial-Fungal Consortium.Biology · 2023Article
- A novel computationally engineered collagenase reduces the force required for tooth extraction in an ex-situ porcine jaw model.Journal of biological engineering · 2023Article
- Special Issue on "Enzymes as Biocatalysts: Current Research Trends and Applications".International journal of molecular sciences · 2022Article
- Collagenase Administration into Periodontal Ligament Reduces the Forces Required for Tooth Extraction in an Ex situ Porcine Jaw Model.Journal of functional biomaterials · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagenases are essential enzymes capable of digesting triple-helical collagen under physiological conditions. These enzymes play a key role in diverse physiological and pathophysiological processes. Collagenases are used for diverse biotechnological applications, and it is thus of major interest to identify new enzyme variants with improved characteristics such as expression yield, stability, or activity. The engineering of new enzyme variants often relies on either rational protein design or directed enzyme evolution. The latter includes screening of a large randomized or semirational genetic library, both of which require an assay that enables the identification of improved variants. Moreover, the assay should be tailored for microplates to allow the screening of hundreds or thousands of clones. Herein, we repurposed the previously reported fluorogenic assay using 3,4-dihydroxyphenylacetic acid for the quantitation of collagen, and applied it in the detection of bacterial collagenase activity in bacterial lysates. This enabled the screening of hundreds of
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