Thermal inactivation of lipoxygenase and hydroperoxytrienoic acid lyase in tomatoes

Abstract Lipoxygenase (LOX) and hydroperoxytrienoic acid lyase (HPL) activities were determined in tomato juice from four cultivars of processing tomatoes. Large differences in total activity levels were found between different cultivars. Thermal inactivation kinetics of these two enzymes were determined for two cultivars used in cold break processing. LOX inactivation did not follow simple first order kinetics. The data could be fitted by assuming that three isoforms of LOX are present. HPL inactivation also indicated the presence of labile and resistant forms with the resistant form showing simple first order inactivation kinetics. The inactivation kinetics for both enzymes indicate that they would be rapidly inactivated at the cold break target temperature of 60 °C. It is questionable whether the activity of these two enzymes contributes to the superior flavour associated with products produced by the cold break process.

[1]  J. Vliegenthart,et al.  Purification, stabilization and characterization of tomato fatty acid hydroperoxide lyase. , 2000, Phytochemistry.

[2]  Kwan‐Hwa Park,et al.  Thermal inactivation kinetics of potato tuber lipoxygenase , 1988 .

[3]  E. Baldwin,et al.  Aroma perception of individual volatile compounds in fresh tomatoes (Lycopersicon esculentum, Mill.) as affected by the medium of evaluation. , 2000 .

[4]  P. G. Smith,et al.  The production and quality of tomato concentrates. , 1998, Critical reviews in food science and nutrition.

[5]  R. Linforth,et al.  Fruit-specific lipoxygenase suppression in antisense-transgenic tomatoes , 1999 .

[6]  Indrawati,et al.  Single, Combined, or Sequential Action of Pressure and Temperature on Lipoxygenase in Green Beans (Phaseolus vulgaris L.) : A Kinetic Inactivation Study , 1999, Biotechnology progress.

[7]  P. E. Nelson,et al.  Quality attributes of processed tomato products: A review , 1996 .

[8]  D. Barrett,et al.  Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes. , 2002, Journal of Agricultural and Food Chemistry.

[9]  T. Cheesbrough,et al.  [53] Lipoxygenase from soybeans: EC 1.13.11.12 Linoleate:oxygen oxidoreductase , 1981 .

[10]  T. Galliard,et al.  The enzymic breakdown of lipids to volatile and non‐volatile carbonyl fragments in disrupted tomato fruits , 1977 .

[11]  J. Joyard,et al.  Envelope Membranes from Spinach Chloroplasts Are a Site of Metabolism of Fatty Acid Hydroperoxides , 1996, Plant physiology.

[12]  E. Helmerhorst,et al.  Microcentrifuge desalting: a rapid, quantitative method for desalting small amounts of protein. , 1980, Analytical biochemistry.

[13]  G. Griffiths,et al.  Lipid hydroperoxide levels in plant tissues. , 2000, Journal of experimental botany.

[14]  S. Svensson,et al.  Thermal inactivation of lipoxygenase from peas (Pisum Sativum L.) : 1. Time-temperature relationships and pH-dependence , 1972 .

[15]  J. Vliegenthart,et al.  Purification, product characterization and kinetic properties of soluble tomato lipoxygenase , 1998 .

[16]  R. Buttery,et al.  Fresh tomato aroma volatiles: a quantitative study , 1987 .

[17]  Robert L. Shewfelt,et al.  Absence of a clear relationship between lipid pathway enzymes and volatile compounds in fresh tomatoes , 2001 .

[18]  R. Linforth,et al.  Soluble lipoxygenase isoforms from tomato fruit , 1997 .

[19]  A. Hatanaka.  The biogeneration of green odour by green leaves , 1993 .

[20]  P. Vandenberg,et al.  Product yield in oxygenation of linoleate by soybean lipoxygenase: the value of the molar extinction coefficient in the spectrophotometric assay. , 1987, Analytical biochemistry.