FOOD SCIENCE ›› 2017, Vol. 38 ›› Issue (9): 143-148.doi: 10.7506/spkx1002-6630-201709023

• Basic Research • Previous Articles     Next Articles

Structural Modification of Oat Bran Globulin by Glycosylation and Change in Its Functional Properties

WANG Changyuan, QUAN Yue, LI Yuqiong, FENG Yuchao, CAO Longkui, ZHANG Dongjie   

  1. College of Food Science, Heilongjiang Bayi Agricultural University, Daqing 163319, China
  • Online:2017-05-15 Published:2017-05-22

Abstract: In the presence of glucosamine, oat bran globulin was subjected to glycosylation using transglutaminase (TG) for analyzing and correlating the structural and functional characteristics of the modified protein. The results showed that some properties of the glycosylated protein were improved when compared to the unmodified one, such as solubility, emulsion stability, foaming ability and foam stability. However, the surface hydrophobicity was significantly decreased. Additionally, the denaturation temperature and enthalpy change of the protein declined after glycosylation. The secondary structure contents changed, as indicated by an increase in α-helix, a decrease in β-sheet and β-turn and almost no change in random coil. The tyrosine residues of the glycosylated globulin were exposed, whereas the tryptophan residues were buried. Moreover, the disulfide stretching vibration mode was t-g-t. A comparison of functional properties and spatial conformation between the modified and unmodified globulin demonstrated that TG catalyzed the binding of glucose to oat bran globulin, further confirming the relationship between its functional characteristics and spatial conformation. The findings of this study may provide a theoretical basis for extending the minor grain industry chain, and offer basic data to study molecular design and intermolecular recombination for the production of special products based on oat bran protein.

Key words: oat bran, globulin, transglutaminase (TG), functional characteristics, structure

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