Wheat Flour Proteins as Affected by Transglutaminase and Glucose Oxidase
Влияние трансглутаминазы и глюкозооксидазы на белки пшеничной муки
2003-01-01
SCID: 54.1/2t8wnrqa
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free-zone capillary electrophoresisglucose oxidasegluten qualitytransglutaminasewheat flour proteins
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Abstract (AI)
ABSTRACT Enzymes are good tool 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 GO 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.
Key Findings
1
Free-zone capillary electrophoresis showed that transglutaminase primarily polymerized glutenins, especially high-molecular-weight glutenin subunits.
2
Glucose oxidase and transglutaminase increased the amount of wet gluten in wheat flour, but neither enzyme improved gluten quality.
3
Glucose oxidase produced dough with higher tenacity and lower extensibility than the control, whereas transglutaminase reduced both tenacity and extensibility.
4
The study demonstrates that enzyme-induced protein bonding alters wheat dough rheology and protein composition without necessarily improving functional gluten quality.
Research Object
wheat flour proteins modified with glucose oxidase and transglutaminase
Research Subject
enzyme-induced changes in gluten quality, dough alveograph parameters, and protein polymerization, particularly of high-molecular-weight glutenin subunits
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2003-01-01
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