Yi Zhang , Laura Roman , Jacob Judas Kain Kirkensgaard , Milena Corredig
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引用次数: 0
Abstract
Salt plays a vital role in modulating protein solubility during plant protein extraction. This study investigated the effect of salt concentrations during extraction on the composition, structure, and thermal properties of pea protein extracts. Low concentrations (0.0–0.2 M) of NaCl resulted in higher ratio of convicilin and vicilin with higher molar mass. Salt concentration did not affect the molar mass of legumin. With 0.4 M NaCl, protein extractability peaked at 78 % and extracted protein had the highest legumin-to-vicilin ratio. With NaCl concentrations greater than 0.4 M, protein composition of extracts remained unchanged, but the extractability decreased. Salt enhanced the heat stability of all pea proteins, as measured by NanoDSC. This study demonstrated that varying NaCl concentrations during protein extraction resulted in pea proteins with different compositions, structures, and thermal properties, offering valuable insights for developing customized protein extraction. The findings can also be extended to other plant proteins.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.