ArticleThe protein journal2022
Molecular Cloning, Expression and Characterisation of a Bacterial Myrosinase from Citrobacter Wye1.
Article in The protein journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- Beyond defense: microbial modifications of plant specialized metabolites alter and expand their ecological functions.The New phytologist · 2025Review
- Insights into Osteogenesis Induced by CrudeNutrients · 2024Article
- Microorganisms-An Effective Tool to Intensify the Utilization of Sulforaphane.Foods (Basel, Switzerland) · 2022Review
- A new source of bacterial myrosinase isolated from endophytic Bacillus sp. NGB-B10, and its relevance in biological control activity.World journal of microbiology & biotechnology · 2022Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Glucosinolates are plant natural products which on degradation by myrosinases give rise to the beneficial bioactive isothiocyanates. Recently, a myrosinase activity was detected in a Citrobacter strain isolated from soil. This enzyme was purified enabling its amino acid sequence and gene sequence (cmyr) to be determined. In order to study this myrosinase it was necessary to establish an expression system that would enable future work such as a structural determination of the protein to be carried out. The myrosinase gene was amplified, cloned and expressed in Escherichia coli with a 6XHis-tag. The heterologous expression of cmyr enabled relatively large amounts of myrosinase to be produced (3.4 mg cmyr/100 ml culture). Myrosinase activity was determined by mixing substrate and enzyme and determining glucose release. Optimum pH and temperature were determined to be pH 6.0 and 25 °C for the Ni-NTA purified protein. The kinetic parameters of the purified myrosinase were determined using sinigrin as a substrate. K
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Registered trials
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