Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling |
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Authors: | Mohammad Alrosan Thuan-Chew Tan Azhar Mat Easa Sana Gammoh Stan Kubow Muhammad H. Alu'datt |
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Affiliation: | 1. Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, Penang, 11800 USM Malaysia;2. Department of Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, P.O. Box 3. 3030, Irbid, 22110 Jordan;4. School of Human Nutrition, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste-Anne-De-Bellevue, QC, H9X 3V9 Canada |
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Abstract: | There has been a growing interest in plant proteins due to their beneficial health effects, low cost and variety of applications in food industries. The low solubility of lentil proteins (LPs) is one of the significant factors that limit their use in food applications. Quinoa proteins (QPs), which have high water solubility, were combined with LPs at pH 12 to generate LP-QP complexes to generate pH-based soluble protein compounds. The LP-QP complexes demonstrated a large surface charge with an increase solubilisation of the protein complexes by more than 85%, together with resistance to protein aggregation. The combination of LPs to QPs led to a significant increase (P < 0.05) in unique tertiary and secondary protein structures as determined by the protein–protein interaction (PPI) technique involving pH recycling. Interactions between LPs and QPs affected the surface morphology of the protein complexes formed. Electrostatic interactions, hydrophobic forces and hydrogen bonding were indicated to play key roles in the PPIs. The capacity of pH cycling to illustrate the above protein interactions shows that this is a robust approach for assessing the emulsion and foaming properties of food proteins. |
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Keywords: | Lentil proteins pH recycling protein complexes quinoa proteins solubility |
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