Abstract
A 2-alkenal reductase, which catalyzes the reduction of sorbaldehyde (trans-2, trans-4- hexadienal) to trans-4-hexenal, was purified from Mucor griseo-cyanus by dialysis against an acidic buffer solution (pH 5.2), salting-out fractionation with ammoniumsulfate, chromatography on DEAE-Sephadex, preparative disc electrophoresis, and gel filtration on Bio-Gel P-75. A 2-alkenal reductase of a microorganismwas purified for the first time. The molecular weight was estimated to be 2.6 x 104 by SDS-disc electrophoresis, and the optimum pH was found to be 6.5. The enzyme was dependent on both NADPHand NADH, and was specific for cis-2-heptenal and -octenal in a series of 2-alkenals, trans-2-alkenals (C4, C6-C10 and C12), cis-2-alkenals (C7 and C8), acrolein, and trans-2-cinnamaldehyde.
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.
