D
Dick B. Janssen
Researcher at University of Groningen
Publications - 387
Citations - 19823
Dick B. Janssen is an academic researcher from University of Groningen. The author has contributed to research in topics: Haloalkane dehalogenase & Dehalogenase. The author has an hindex of 76, co-authored 374 publications receiving 18485 citations. Previous affiliations of Dick B. Janssen include Radboud University Nijmegen & Codexis.
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Journal Article
Identification of Chloroacetaldehyde Dehydrogenase Involved in 1,2-Dichloroethane Degradation
TL;DR: The degradation of 1,2-dichloroethane and 2-chloroethanol by Xanthobacter autotrophicus GJ10 proceeds via chloroacetaldehyde, a reactive and potentially toxic intermediate as discussed by the authors.
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Genome Sequence of the Dichloromethane-Degrading Bacterium Hyphomicrobium sp. Strain GJ21.
Françoise Bringel,Christiaan P. Postema,Sophie Mangenot,Sabrina Bibi-Triki,Pauline Chaignaud,Muhammad Farhan Ul Haque,Christelle Gruffaz,Louis Hermon,Yousra Louhichi,Bruno Maucourt,Emilie E. L. Muller,Thierry Nadalig,Aurélie Lajus,Aurélie Lajus,Aurélie Lajus,Zoé Rouy,Zoé Rouy,Zoé Rouy,Claudine Médigue,Claudine Médigue,Claudine Médigue,Valérie Barbe,Dick B. Janssen,Stéphane Vuilleumier +23 more
TL;DR: The genome sequence of Hyphomicrobium sp.
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Lyophilization conditions for the storage of monooxygenases
TL;DR: Lyophilization in the presence of 2% (w/v) sucrose was found to be the best formulation to preserve activity and protect against inactivation when stored as lyophilizate at 50°C.
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Aminoacyl-coenzyme A synthesis catalyzed by a CoA ligase from Penicillium chrysogenum
TL;DR: The synthesis of aminoacyl‐coenzyme As (CoAs) catalyzed by a CoA ligase from Penicillium chrysogenum is described, and it is suggested that alanine 312 is part of the active site cavity, and mutagenesis (A312G) yielded a variant that has an enhanced catalytic efficiency with β‐phenylalanines and d‐α‐ phenylalanine.
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Adaptation of Pseudomonas sp. GJ1 to 2-bromoethanol caused by overexpression of an NAD-dependent aldehyde dehydrogenase with low affinity for halogenated aldehydes
TL;DR: To achieve growth with 2-bromoethanol, the high expression of the enzyme appears to be necessary in order to compensate for the high Km for bromoacetaldehyde and for inactivation of the enzymes by bromOacetaldehyde.