title: Enhancement of L-2-haloacid dehalogenase expression in Pseudomonas stutzeri DEH138 based on the different substrate specificity between dehalogenase-producing bacteria and their dehalogenases.
abstract: There was no direct correlation in substrate specificity between the metabolism of Pseudomonas stutzeri DEH138 and its corresponding dehalogenase. Dehalogenase substrates that could be dehalogenated might not be degraded by DEH138 or vice versa. Basing on this, different approaches to enhance L-2-haloacid dehalogenase (L-DEX) production in DEH138 via the combination of non-halogenated compounds with different inducers were applied. The optimum approach to obtain more L-DEX from DEH138 was the combination of DL-lactate and DL-2-chlorobutyrate, with 5.7-fold greater production and 11.7-fold greater productivity of the enzyme after optimization.
authors: Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
authors: Yayue
authors: Y
authors: Wang
authors: Yanjuan
authors: Y
authors: Xin
authors: Xupeng
authors: X
authors: Cao
authors: Song
authors: S
authors: Xue
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002087:Butyrates / Q000737:chemistry / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D019344:Lactic Acid / Q000737:chemistry / Q000378:metabolism; D044223:Pseudomonas stutzeri / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D002087:Butyrates; D019344:Lactic Acid; D006867:Hydrolases; C034507:2-haloacid dehalogenase