Abstract
The enzymes for shortening the phenylpropanoid side chain were partially purified by ion exchange and gel filtration column chromatographies after (NH4)2SO4 precipitation. The enzyme activities of each fraction were dependent on the presence of dithiothreitol (DTT). The optimum pH and the molecular weight of the enzyme in one fraction were approximately 7.0 and 17,000, respectively. The enzyme activity of ferulic acid toward 4-coumaric acid in the same fraction was about 16%. The enzyme activity was activated by the addition of 0.5mM Fe2+. We propose that 2,3-dioxygenase catalyzes the reaction from ferulic acid to vanillin in Vanilla planifolia.
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.
