Abstract

To form a stable emulsion system, the water-soluble proteins (WSPs) of Sipunculus nudus were prepared as the sole effective stabilizer for the high internal phase emulsion (HIPEs), of which the influence of the WSPs concentration and environmental stability was investigated. The HIPEs were fabricated using a simple one-pot homogenization process (10,000 rpm/min, 3 min) that involved blending the WSPs (0.1, 1, 2, 3, 4, and 5 wt%) with soybean oil (60, 65, 70, 75, 80, 85, and 90%). The microstructure and properties of stable HIPEs were characterized by particle size, ζ-potential, visual observations, optical microscopy, and dynamic rheology property measurements. As the concentration of WSPs increases, the mean particle diameter of HIPEs decreases, on the contrary, the apparent viscosity and storage modulus gradually increase. At a given emulsifier concentration (3 wt%), the stable and gel-like HIPEs were formed at the oil internal phase (ϕ) values of 70–75%, all the pH range in values from 3 to 9, and the ionic strength from 100 to 500 mM. Furthermore, the HIPEs that were stabilized formed a gel-like state that was relatively stable to heat and storage (30 days). And there was a new phenomenon that the destabilized HIPE of the freeze-thaw treatments could still return to a gel-like state again after homogenizing. The study results suggest that the WSPs of S. nudus as a natural emulsifier could be widely used in the food industry.

Highlights

  • High internal phase emulsions are potentially applied in food products and industries [1,2,3,4,5,6,7] because it has relatively high stability to droplet aggregation and creaming [8, 9]

  • Formation and Characteristics of high internal phase emulsion (HIPEs) Stabilized by water-soluble proteins (WSPs)

  • Similar results have been reported for the HIPEs stabilized by protein/polysaccharide hybrid particles [39] and assembled block copolymer [3]

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Summary

INTRODUCTION

High internal phase emulsions are potentially applied in food products and industries [1,2,3,4,5,6,7] because it has relatively high stability to droplet aggregation and creaming [8, 9]. Cha et al [32] found that the Emulsifying Activity Index (EAI), Emulsifying Stability Index (EsI), apparent viscosity, and zeta absolute potential of mussel myofibrillar protein (MMP) and lecithin stabilized emulsion increased and were in a state of good dispersion after a high-pressure homogenization treatment. These results will contribute to improving the formulation of emulsions and their properties, and provide a new understanding of MMP as a natural emulsifier in the food industry. This study uses WSPs as the sole stabilizer to prepare stable gel-like HIPEs, which provides a theoretical basis and technical support for studying the structural characteristics of food-grade emulsifiers and the formation mechanism of stable emulsion systems

MATERIALS AND METHODS
RESULTS AND DISCUSSION
DATA AVAILABILITY STATEMENT
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