Effect of Glucose Oxidase on Moisture Status and Protein Structure of Dough
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Abstract:
Nuclear Magnetic Resonance (NMR) and Fourier transform infrared spectroscopy (FT-IR) were used to study the effect of glucose oxidase (GOD) (0~0.5%) on moisture distribution and parameter changes of protein structures in dough. A correlation analysis of each experimental indicator was conducted based on the thermodynamic properties of dough and the changes in disulfide bond content. The results showed that the addition of GOD could reduce the relaxation times (T2) for water in dough. In the range of 0~0.5%, the T21 and T22 values decreased first and then increased, whereas when the dose was 0.4%, the measured T21 and T22 values were the lowest; thus, GOD concentration had a significant negative correlation (p < 0.05) with T21 and T22. The amount of β-pleated sheet, β-sheet, α-helix, unordered structure, and β-turn increased first and then decreased, and a significant positive correlation (p < 0.01) was found between GOD concentration and r values. GOD could increase the gelatinization temperature and thermal stability of the dough, promote sulfhydryl groups (-SH) to be converted to disulfide groups (S-S), and significantly affect changes in disulfide groups (S-S). The moisture migration in dough showed significant correlation (p < 0.05) with the gelatinization temperature of dough, disulfide (S-S) content, α-helix, β-turn, and unordered structure. The gelatinization peak temperature (Tp) had significant positive correlation with disulfide groups (S-S), α-helix, and β-turn (p < 0.05).
