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The effect of lipoxygenase action on the mechanical development of wheat flour doughs
Author(s) -
Frazier P. J.,
LeighDugmore F. A.,
Daniels N. W. R.,
Eggitt P. W. Russell,
Coppock J. B. M.
Publication year - 1973
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740240411
Subject(s) - food science , chemistry , lipoxygenase , rheology , wheat flour , lipid oxidation , linoleic acid , emulsion , enzyme , biochemistry , materials science , antioxidant , fatty acid , composite material
Abstract The mechanical development of dough has been followed by measurement of the relaxation time of dough samples after mixing to various levels of work input. Parallel determinations of free and bound lipid have also been made. When doughs were mixed in air, addition of full‐fat, enzyme‐active soya bean flour (subsequently referred to as “soya flour”) resulted in an increase in relaxation time, particularly at higher work levels. The magnitude of this improvement increased with increasing work input and was dependent on the rate of work input. Addition of soya flour also enabled a higher level of mechanical work to be introduced before dough breakdown occurred. When doughs were mixed under nitrogen, or when the soya flour was heat denatured, no change in the rheological properties compared with the respective control doughs was found. The release of bound lipid, which occurred during dough development in air in the presence of soya flour, could also be induced by adding purified lipoxygenase to the dough, together with linoleic acid as a substrate. This resulted in rheological changes similar to those observed using soya flour. However addition of enzymically pre‐peroxidised lipid to doughs mixed in nitrogen was without effect on relaxation times. These findings suggest that lipid release is linked with structural changes in dough protein and provide further support for a mechanism of coupled oxidation of protein ‐SH groups by lipoxygenase.