Improving the Functionality of Lentil–Casein Protein Complexes through Structural Interactions and Water Kefir-Assisted Fermentation

Author:

Alrosan Mohammad12ORCID,Tan Thuan-Chew13ORCID,Easa Azhar Mat1ORCID,Alu’datt Muhammad H.4,Tranchant Carole C.5ORCID,Almajwal Ali Madi6,Gammoh Sana4,Maghaydah Sofyan47ORCID,Dheyab Mohammed Ali8,Jameel Mahmood S.8,Al-Qaisi Ali9

Affiliation:

1. Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, USM 11800, Penang, Malaysia

2. Applied Science Research Center, Applied Science Private University, Amman 11937, Jordan

3. Renewable Biomass Transformation Cluster, School of Industrial Technology, Universiti Sains Malaysia, USM 11800, Penang, Malaysia

4. Department of Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, Irbid 22110, Jordan

5. School of Food Science, Nutrition and Family Studies, Faculty of Health Sciences and Community Services, Université de Moncton, Moncton, NB E1A 3E9, Canada

6. Department of Community Health Sciences, College of Applied Medical Sciences, King Saud University, P.O. Box 10219, Riyadh 11433, Saudi Arabia

7. Department of Human Nutrition and Dietetics, College of Health Sciences, Abu Dhabi University, Zayed City, Abu Dhabi P.O. Box 59911, United Arab Emirates

8. School of Physics, Universiti Sains Malaysia, USM 11800, Penang, Malaysia

9. Department of Agricultural Biotechnology, Faculty of Agricultural Sciences and Technology, Palestine Technical University-Kadoorie (PTUK), Jaffa Street, Tulkarm P.O. Box 7, Palestine

Abstract

Highly nutritious lentil proteins (LP) have recently attracted interest in the food industry. However, due to their low solubility, extensive application of LP is severely limited. This study describes a new and successful method for overcoming this challenge by improving the nutritional–functional properties of LP, particularly their solubility and protein quality. By combining protein complexation with water kefir-assisted fermentation, the water solubility of native LP (~58%) increases to over 86% upon the formation of lentil–casein protein complexes (LCPC). Meanwhile, the surface charge increases to over −40 mV, accompanied by alterations in secondary and tertiary structures, as shown by Fourier-transform infrared and UV-vis spectra, respectively. In addition, subjecting the novel LCPC to fermentation increases the protein digestibility from 76% to over 86%, due to the reduction in micronutrients that have some degree of restriction with respect to protein digestibility. This approach could be an effective and practical way of altering plant-based proteins.

Funder

Malaysia’s Fundamental Research Grant Scheme

King Saud University, Riyadh, Saudi Arabia

Publisher

MDPI AG

Subject

Plant Science,Biochemistry, Genetics and Molecular Biology (miscellaneous),Food Science

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