PROTEIN CHARACTERISTICS IN RELATION TO TEXTURAL AND PASTING PROPERTIES OF RICE AFTER STORAGE
Keywords:
Proteins, hydrophobic interaction, disulfide bonds, pasting properties, textural propertiesAbstract
The protein characteristics of fresh and aged rice were investigated to correlate with the textural and pasting properties. The alkaline extractable proteins of aged rice were lower than those of fresh rice and they were extensively decreased in cooked rice. However, an increase in extractable proteins was noticed when the extraction buffer contained 1% sodium dodecyl sulfate, indicating that the rice proteins were stabilized via hydrophobic interaction. The extracted proteins from raw and aged cooked rice showed higher surface hydrophobicity and more disulfide bonds than those of fresh rice, suggesting more protein unfolding and higher disulfide linkages. In addition, aged rice proteins revealed higher molecular weight formed via disulfide bonds and hydrophobic interactions, as observed by sulfate polyacrylamide gel electrophoresis (SDS-PAGE). After cooking, increased proglutelin and new aggregated protein (41 kDa) were observed. The harder texture and lower stickiness of aged cooked rice were noticed as compared with fresh cooked rice. Aged flour showed a lower breakdown, higher setback, and less paste viscosity, as monitored with a Rapid Visco Analyser. Removing protein from aged and fresh flour showed similar pasting curves, indicating that the proteins’ characteristics had an influence on the pasting characteristics and were related to the cooked rice’s texture.
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