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Effects of Transglutaminase on Rheology, Microstructure, and Baking Properties of Frozen Dough

May 2008 Volume 85 Number 3
Pages 301 — 306
W. N. Huang,1,2 Y. L. Yuan,1 Y. S. Kim,1 and O. K. Chung1

Professor, graduate research assistant, associate professor, and visiting professor, respectively. The State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University (former Southern Yangtze University), Wuxi, Jiangsu 214122, China. Corresponding author. Phone: 86-510-859-19139. Fax: 86-510-859-19139. E-mail: wnhuang@jiangnan.edu.cn


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Accepted October 4, 2007.
ABSTRACT

The improving effects of transglutaminase (TGase) were investigated on the frozen dough system and its breadmaking quality. Rheological properties and microstructure of fresh and frozen doughs were measured using a Rapid Visco-Analyser (RVA), dynamic rheometer, and scanning electron microscopy (SEM). The frozen doughs with three storage periods (1, 3, and 5 weeks at –18°C) were studied at three levels (0.5, 1.0, and 1.5%) of TGase. As the amount of TGase increased, hot pasting peak viscosity and final viscosity from the RVA decreased, but breakdown value increased. The TGase content showed a positive correlation with both storage modulus G′ (elastic modulus) and the loss modulus G″ (viscous modulus): G′ was higher than G″ at any given frequency. The SEM micrographs showed that TGase strengthened the gluten network of fresh, unfrozen dough. After five weeks of frozen storage at –18°C, the gluten structure in the control dough appeared less continuous, more disrupted, and separated from the starch granules, while the dough containing 0.5% TGase showed less fractured gluten network. Addition of TGase increased specific volume of bread significantly (P < 0.05) with softer bread texture. Even after the five weeks of frozen storage, bread volume from dough with 1.5% TGase was similar to that of the fresh control bread (P < 0.05). The improving effects of TGase on frozen dough were likely the result of the ability of TGase to polymerize proteins to stabilize the gluten structure embedded by starch granules in frozen doughs.



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