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

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.

Keywords

• casein proteins
• lentil proteins
• structural interaction
• protein quality
• solubility
• water kefir-assisted fermentation