Submitted to: Cereal Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/21/2002
Publication Date: 8/21/2002
Citation: ROSELL, C.M., WANG, J., AJA, S., BEAN, S., LOOKHART, G.L. WHEAT FLOUR PROTEINS AS AFFECTED BY TRANSGLUTAMINASE AND GLUCOSE OXIDASE. CEREAL CHEMISTRY. 2002. Interpretive Summary: Wheat is one of the major cereals used in food around the world. The storage proteins of wheat play a fundamental role in the breadmaking process. They have the ability to form gluten, a necessary network to amalgamate the other wheat components, mainly carbohydrates, and the gas produced during proofing. Several factors affect the final gluten quality such as cultivar, environment, insect infestation, and post harvest conditions. Chemical dough conditioners are often used to improve dough strength but enzymes are increasingly being used as they are generally recognized as safe (GRAS). Transglutaminase (TG) and glucose oxidase (GO) are two enzymes that have dough strengthening properties. This study was designed to follow the effect of TG and GO on improving dough properties and gluten strength. GO was found to affect the storage proteins more than TG. This information is of interest to cereal chemists, millers and bakers. Addition of one or more enzymes to the water used in tempering the wheats prior to milling may condition the wheat and provide doughs with more desirable dough qualities.
Technical Abstract: Enzymes are good tools to modify wheat proteins by creating new bonds between the protein chains. In this study, the effect of the addition of glucose oxidase (GO) and transglutaminase (TG) on the wheat flour proteins is presented. The modification of wheat proteins was determined by analyzing the changes in gluten quality, alveograph parameters, and protein modifications. The amount of wet gluten increased with the addition of BO and TG, but the gluten quality was not improved in any case. Regarding the alveograph parameters, the effect of GO was readily evident obtaining wheat dough with higher tenacity and lower extensibility than the control, while TG led to doughs with lower tenacity and that were also less extensible. The protein modifications were characterized by free-zone capillary electrophoresis (FZCE). FZCE data indicated that TG polymerizes mainly glutenins and, of those, the high molecular weight glutenin subunits were the most affected.