Abstract
ABSTRACTPolyphenoloxidase (PPO) was isolated from two varieties of grapes grown in the northeastern United States and its characteristics were studied. The temperature and pH optima for both enzymes were 25°C and 5.5, respectively. The thermal inactivation of PPO followed first‐order kinetics; with the Niagara enzyme being more heat stable than Ravat PPO. The substrate specificity of the grape PPO clearly showed high affinity toward the o‐diphenolic compounds, with a high affinity toward caffeic acid. Inhibition studies indicated that L‐cysteine and sodium diethyldithiocarbamate were the most potent.
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.
