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Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility

Alrosan M 1 , Madi Almajwal A 2 , Al-Qaisi A 3 , Gammoh S 4 , H Alu'datt M 4 , R Al Qudsi F 5 Show all authors , Tan TC 1 , A Razzak Mahmood A 6 , Maghaydah S 4

Affiliations 

  • 1 Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, 11800, USM, Penang, Malaysia
  • 2 Department of Community Health Sciences, College of Applied Medical Sciences, King Saud University, P.O. Box 10219, Riyadh, 11433, Saudi Arabia
  • 3 Department of Agricultural Biotechnology, Faculty of Agricultural Sciences and Technology, Palestine Technical University-Kadoorie (PTUK), Jaffa Street, Tulkarm P.O. Box 7, Palestine
  • 4 Department of Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, P.O. Box 3030, Irbid, 22110, Jordan
  • 5 Department of Food Science, University of Guelph, Guelph, Ontario, N1G 2W1, Canada
  • 6 Department of Pharmaceutical Chemistry, College of Pharmacy-University of Baghdad, Baghdad, Bab-Al-Mouadam, 10001, Iraq
Curr Res Struct Biol, 2024;7:100135.
PMID: 38516624 DOI: 10.1016/j.crstbi.2024.100135

Abstract

Plant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose conjugation on lentil and whey proteins. The protein structures after the modification were analysed using spectroscopic methods: Fourier-transform infrared, ultraviolet spectra, and fluorescence spectra. The amide group I, conformation protein, and tertiary structure of the trehalose-conjugated lentil-whey protein complexes (T-LWPs) showed significant changes (P < 0.05). Moreover, the surface properties (surface hydrophobicity and charges) of T-LWPs were significantly modified (P < 0.05), from 457 to 324 a.u and from 36 to -40 mV, respectively. Due to these modifications on the protein structures, the protein digestibility (80-86%) and water solubility (90-94.5%) of T-LWPs increased significantly (P 

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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