Effect of oxidative enzymes on bulk rheological properties of wheat flour doughs

被引:51
作者
Dunnewind, B
van Vliet, T
Orsel, R
机构
[1] Wageningen Univ Agr, Dept Agrotechnol & Food Sci, Food Phys Grp, NL-6700 EV Wageningen, Netherlands
[2] TNO, Nutr & Food Res Inst, Dept Food Sci & Technol, NL-3700 AJ Zeist, Netherlands
[3] Quest Int BV, NL-1400 CA Naarden, Netherlands
关键词
dough rheology; relaxation; peroxidase; glucose oxidase;
D O I
10.1006/jcrs.2002.0471
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The use of enzymes such as peroxidases or glucose oxidase instead of chemical oxidants is a very interesting option for improving breadmaking performance of doughs. In this study the effect of such enzymes on bulk rheological properties of dough was quantified and their influence on the polymer network in dough deduced. Small deformation oscillation and relaxation tests (strain 0.001) are not suitable for discriminating between doughs prepared in the presence of the different enzymes. Flow relaxation tests at high deformation and long relaxation times showed a clear distinction between the effect of peroxidase and glucose oxidase. Peroxidase increases only the number or lifetime of transient bonds, whereas glucose oxidase additionally produced cross-links that were permanent on time scales up to 3 h. Peroxidase probably introduced a second, more transient structure (arabinoxylan network) through the gluten network, whereas glucose oxidase may also have strengthened the gluten network. A higher water addition could not compensate for the effect of peroxidase; on longer time scalds the stress remained at a higher level. Similar results were obtained in large deformation biaxial and uniaxial extension tests. Peroxidases only increased stress levels. The addition of glucose oxidase resulted in a higher stress and more intense strain hardening. Only in biaxial extension was an influence of pH observed. An increase in stress level was accompanied by a decrease in fracture strain, making predictions of the effects on bread structure complicated. (C) 2002 Published by Elsevier Science Ltd.
引用
收藏
页码:357 / 366
页数:10
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