Thermal inactivation kinetics of quality-related enzymes in cauliflower (Brassica oleracea var. botrytis)

Thermal inactivation of quality-related enzymes in both cauliflower crude enzyme extracts and fresh tissue samples was studied in temperature range 50–100 °C. For crude enzyme extracts, several parameters, reaction rate constants ( k ) and activation energy ( E a ) as well as decimal reduction time...

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Published inEuropean food research & technology Vol. 232; no. 2; pp. 319 - 326
Main Authors Rayan, Ahmed M. M., Gab-Alla, Amal A., Shatta, Adel A., El-Shamei, Zakarya A. S.
Format Journal Article
LanguageEnglish
German
Published Berlin/Heidelberg Springer-Verlag 01.02.2011
Springer
Springer Nature B.V
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Summary:Thermal inactivation of quality-related enzymes in both cauliflower crude enzyme extracts and fresh tissue samples was studied in temperature range 50–100 °C. For crude enzyme extracts, several parameters, reaction rate constants ( k ) and activation energy ( E a ) as well as decimal reduction time ( D ) and ( z ) values, were used to characterize the thermal stability. The rates of inactivation were found to follow first-order inactivation kinetics. Activation energies varied between 101.18 and 208.42 kJ mol −1 with z values of 10.59–24.09 °C. The examined kinetics indicated that lipoxygenase was the most heat resistant followed by peroxidase, polyphenol oxidase, pectin methyl esterase and ascorbic acid oxidase. Furthermore, the obtained results from the blanched fresh tissues indicated that inactivation of lipoxygenase secured disappearing of any other enzyme activities. Therefore, this study recommends using lipoxygenase as an indicator enzyme to optimize the thermal treatments of cauliflower products.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1438-2377
1438-2385
DOI:10.1007/s00217-010-1391-7