Affiliations 

  • 1 Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia; Applied Science Research Center, Applied Science Private University, Al-Arab St. 21, Amman 11931, Jordan; College of Health Science, QU Health, Qatar University, Doha P.O. Box 2713, Qatar; Department of Nutrition and Food Science, Faculty of Agriculture, Jerash University, Jerash, Jordan. Electronic address: [email protected]
  • 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 Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan; 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 Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan; Department of Food Science & Nutrition, College of Life Sciences, Kuwait University, P.O. Box. 5969, Safat 13060, Kuwait
  • 6 Department of Food Science, University of Guelph, Guelph, Ontario N1G 2W1, Canada
  • 7 Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia
  • 8 Department of Pharmaceutical Chemistry, College of Pharmacy, University of Baghdad, Baghdad, Bab-Al-Mouadam 10001, Iraq
  • 9 Water Technology Unit (WTU), Center for Advanced Materials (CAM), Qatar University, P.O. Box 2713, Doha, Qatar
Food Chem, 2024 Jul 30;447:138882.
PMID: 38452537 DOI: 10.1016/j.foodchem.2024.138882

Abstract

The two limiting factors for lentil protein utilization are water solubility and digestibility. In this study, we utilized two non-thermal techniques: (1) protein complexation of lentil and casein proteins using the pH-shifting method and (2) protein conjugation with trehalose to produce trehalose-conjugated lentil-casein protein complexes (T-CPs) with enhanced water solubility and digestibility. The protein structure of the T-CPs was analyzed for secondary protein structure, conformation protein, and tertiary protein structure using Fourier-transform infrared, UV, and fluorescence spectroscopies, respectively. The surface hydrophobicity and surface charge of T-CPs solution at pH 7.0 changed significantly (P 

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