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Published on: October 26, 2016
Mild-temperature conjugation of pea protein isolate with oxidized sodium alginate: structural, interfacial, and
Wenhao Liu1, Xiaoye Xu1, Caifeng Chen1
1Engineering Research Centre of Fujian-Taiwan Special Marine Food Processing and Nutrition (Ministry of Education), College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, PR China.
Abstract:
Pea protein isolate (PPI) has limited food applications because of poor aqueous solubility and emulsifying performance. Here, sodium alginate (SA) was oxidized to generate reactive aldehyde groups, enabling Schiff-base-mediated conjugation with PPI under mild conditions (40 °C, 90 min). By varying reaction parameters, conjugates with grafting degrees (GD) of 10.67-22.87% were obtained. Increasing GD was accompanied by increased β-sheet content (32.81-41.52%), tertiary structural reorganization, enhanced surface charge, a water contact angle of up to 79.35°, and a > 50% reduction in oil-water interfacial tension. The conjugates, particularly at GD >18%, stabilized high-internal-phase emulsions containing 75% oil at 4% protein, with good stability during heating, exposure to NaCl up to 200 mM, and 15 d storage. High-GD emulsions retained >85% of curcumin during storage, showed lower gastric curcumin release, and increased final bioaccessibility to >68% in the present in vitro digestion model. These findings demonstrate a mild, tunable strategy for improving PPI functionality and developing plant-protein-based delivery systems.
