Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis.
Thermal stabilities of main enzymes involved in the biosynthesis of virgin olive oil (VOO) aroma through the lipoxygenase (LOX) pathway were studied in crude enzymatic preparations. Kinetic parameters of thermal inactivation for LOX were determined graphically and were shown to be compatible with the presence of two LOX isoenzymes (LOXlab and LOXres) having different thermal stabilities and displaying relative activities of 88 and 12% each. Data on hydroperoxide lyase (HPL) suggest the existence of just one HPL isoform. Thermal stabilities of LOX and HPL enzymatic activities in crude preparations seem to explain the observed decrease of volatile contents in VOO aroma as a consequence of heat treatments of olive fruit. Moreover, differences in thermal stability of LOXlab and LOXres would justify the distinct pattern of reduction of C6 and C5 compound contents observed in the aroma of these oils.
Luaces
Pilar
P
Department of Physiology and Technology of Plant Products, Instituto de la Grasa, C.S.I.C., Padre García Tejero 4, 41012-Seville, Spain.
Sanz
Carlos
C
Pérez
Ana G
AG
D000446:Aldehyde-Lyases / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004795:Enzyme Stability; D005638:Fruit / Q000201:enzymology*; D006358:Hot Temperature; D008084:Lipoxygenase / Q000378:metabolism*; D009812:Odorants / Q000032:analysis*; D031658:Olea / Q000201:enzymology*; D000069463:Olive Oil; D010938:Plant Oils / Q000737:chemistry*
D000069463:Olive Oil; D010938:Plant Oils; D003577:Cytochrome P-450 Enzyme System; D008084:Lipoxygenase; D000446:Aldehyde-Lyases; C054540:hydroperoxide lyase