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Effects of pepsin hydrolysis on the soy β-conglycinin aggregates formed by heat treatment at different pH

Authors

  • Xiu-Ting He,

    1. Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology, Guangzhou, China
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  • Xiao-Quan Yang,

    Corresponding author
    1. Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology, Guangzhou, China
    2. State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou, China
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  • Jin-Bo Zhang

    1. Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology, Guangzhou, China
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Summary

The effects of pepsin hydrolysis on the β-conglycinin aggregates formed by heat treatment at different pH were investigated. Results showed that fibrils were still observed, whereas the random aggregates were easily to be digested in the simulated gastric fluid. Electrophoresis and molecular weight analysis indicated that large aggregates still existed after pepsin treatment for fibrils. Hydrolysis resulted in changes in the apparent viscosity (ηapp) of 6% fibril solutions. The ηapp at the shear rate range (0–30 s−1) increased in the order of fibrils < fibrils with pepsin for 60 min < fibrils with pepsin for 30 min. Smaller peptide/fibril fragments were generated, and additional aggregates were reformed during the hydrolysis process, as evidenced by thioflavin T and atomic force microscopy images. The native β-conglycinin hydrolysates comprised a mixture of polypeptides enriched in about 47 kDa. These findings would provide valuable information about effects of enzymatic hydrolysis on plant oligometric globulin aggregates.

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