Effects of NaCl-assisted regulation on the emulsifying properties of heat-induced type I collagen

Abstract

Although collagen is widely used as an emulsifier in the food industry, its emulsifying properties are strongly influenced by processing conditions. This research investigated the effects of NaCl on the emulsifying properties of type I collagen after heating. Before heating, the solubility, emulsifying activity index (EAI), emulsifying stability index (ESI), and viscosity of type I collagen initially increased after adding NaCl (0.2 M), after which decreased with increasing NaCl concentration (0.4 M and 0.6 M) due to salt-in effect and the salt-out effects of the protein. While after heating (90℃, 30 min), the collagen became more soluble, with improved EAI and ESI, viscosity, and reduced particle size in response to increasing NaCl concentrations. It was found that NaCl increased the EAI of type I collagen twice after heating, and the EAI reached its maximum at 0.6 M NaCl concentration. We concluded that the improved emulsifying properties may due to thermal denaturation of the protein, resulting in an unfolded and disordered structure with increase of hydrogen bonds with water, rupture of disulfide bonds, and exposure of hydrophobic groups, leading to the increase of adsorption at the oil/water interface. Meanwhile, the Raman spectra analysis and Atomic Force Microscope (AFM) images showed that unfolding of the collagen triple helix was gradually destroyed after NaCl addition and heating, with emulsifying properties improved. The specific outcomes of present study can be adapted towards the requirements to improve the quality of emulsified meat products in the food industry.