Abstract
1. 1. A membrane-bound alcohol dehydrogenase (alcohol:(acceptor) oxidoreductase, no EC number) has been solubilized from Pseudomonas aeruginosa by treatment with Triton X-100 and purified to homogeneity as judged by electrophoresis on polyacrylamide gels. (Spec. act. 6.4 units/mg protein for 1-octanol.) Aggregation of the enzyme takes place in the absence of detergent. This may be at least partly related to the lack of stability of the purified enzyme. 2. 2. The purified enzymes does not use pyridine nucleotides (NAD or NADP) as coenzymes. No spectral evidence of the involvement of a flavin as a prosthetic group has been found. Among the artificial electron acceptors tested, only phenazine methosulfate is utilized. The product of oxidation of an alcohol is the corresponding aldehyde. 3. 3. This alcohol dehydrogenase has a high affinity for long chain primary alcohols ( K m for 1-tetradecanol 4.5 μM). It is induced by growth on various hydrocarbons and especially by long-chain hydrocarbons ( n- hexadecane ). These properties clearly indicate its involvement in the degradation of long chain hydrocarbons in P. aeruginosa.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
