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Isolation and characterization of some oxidizing enzymes of the McFarlin cranberry

Due to the scarcity of information concerning the oxidase systems
in cranberries the peroxidase, catalase, and polyphenolase systems,
which are used as biochemical indexes of adequacy for enzyme inactivation
in other fruits and vegetables, were investigated.
Enzyme extracts were prepared from acetone powders with and
without phenol-binding agents such as polyethylene glycol and polyvinylpyrrolidone
(PVP) and buffered PVP. The acetone-PVP combination
was found to be the most effective in reducing the polyphenolic content
of the enzyme extract. Highest specific activity was obtained by using
a buffered PVP extract. The pH optimum of cranberry peroxidase
activity is 6.0. Heat inactivation of cranberry peroxidase was determined
to follow first order kinetics. There was 90% destruction at 70,
80, and 90°C requiring 9.40, 1.60, and 0.47 minutes of heat treatment,
respectively. The activation energy for the thermal inactivation of
cranberry peroxidase was found to be 37.2 kcal/mole. Guaicol,
o-phenylene diamine (OPDA), and pyrogallol were tested for their
sensitivity to cranberry peroxidase with OPDA determined as most
sensitive.
The pH optimum for catalase activity was found to range from 7.5 to
9.2. Kinetics for the heat inactivation of cranberry catalase was determined
not to be of the first order nor zero order. Approximately 50%
of the catalase activity is inactivated after heating for 17, 1.8, and
O.6 minutes at temperatures of 50, 60, and 70°C, respectively.
Cranberry polyphenolase activity was measured using catechol as a
substrate. The product of the reaction absorped maximally at 400 mu.
The pH optimum for cranberry polyphenolase activity was determined
to be 7.0. Heat inactivation of cranberry polyphenolase was found to
follow first order kinetics. There was 90% destruction at 50, 60, and
70°C requiring 15.85, 7.05, and 1.37 minutes of heat treatment, respectively.
The activation energy for the inactivation of cranberry
polyphenolase was found to be 27.7 kcal/mole. / Graduation date: 1969

Identiferoai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/26815
Date07 May 1969
CreatorsChan, Harvey T., 1940-
ContributorsYang, Ho-Ya, 1912-
Source SetsOregon State University
Languageen_US
Detected LanguageEnglish
TypeThesis/Dissertation

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