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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Preparation, structural characterization and properties of feruloyl oligosaccharide-rice protein hydrolysate
Fenghong Deng1, Shunjing Luo1, Xiuting Hu1
1The State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, Jiangxi, China; International Institute of Food Innovation Co. Ltd, Nanchang 330200, Jiangxi, China.
Abstract:
Rice protein hydrolysate (RPH) and feruloyl oligosaccharides (FOs) were conjugated under the catalysis of laccase and free radical, and the structure and properties of the resultant conjugates were studied. Electrophoresis analysis demonstrated that conjugation with FOs increased the molecular weight of some fractions in RPH, which confirmed the formation of both conjugates. The conjugation degree of laccase-induced conjugate and radical-induced conjugate was 60.45% and 22.70%, respectively. Laccase-catalyzed conjugation decreased the tyrosine residue content of RPH but had no significant effect on the free amino group content, which suggested that tyrosine residues were the conjugation site in the laccase-induced conjugate. However, radical-catalyzed conjugation decreased both the free amino group content and the tyrosine residue content, which indicated that both free amino groups and tyrosine residues were the conjugation site in the radical-induced conjugate. The ultraviolet, fluorescence and circular dichroism spectroscopy analysis revealed that conjugation with FOs significantly altered the secondary and tertiary structure of RPH. In addition, conjugation with FOs increased the solubility and antioxidant activity of RPH but decreased the emulsifying activity and stability. Particularly, the radical-induced conjugate had greater anti-aggregation capacity and antioxidant activity but lower emulsifying activity and stability than the laccase-induced conjugate, which might be due to that their conjugation site and degree were different.
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