Effects of ultrasound treatment on the structure, function properties and in vitro digestion of Sipunculus nudus protein.

Sipunculus nudus (S. nudus), an edible marine invertebrate, is rich in myofibrillar proteins. However, its extremely low water solubility and relatively firm texture limit its practical applications. This study aimed to investigate the consequences of different ultrasound amplitude treatments on the structure, functional properties, and digestive characteristics of S. nudus salt soluble protein (SSP). The results showed that ultrasound treatment significantly reduced the particle size, surface tension, and the unordered structure of SSP, while having not impact the zeta potential. Additionally, the results of infrared spectroscopy and intrinsic fluorescence spectrum revealed that ultrasound treatment enhanced the hydrogen bonding and hydrophobic interaction within the components of SSP, leading to a more compact and uniformly distributed protein structure. These changes increased the solubility (increased from 12.07 % to 37.59 %) and optimized the functional properties of SSP (foamability and emulsifiability). Further, the results of in vitro digestion simulation revealed that the antioxidant proteopeptides of SSP were mainly produced in the small intestine, with the ABTS+ radical scavenging capacity ranging from 140 to 170 µg Trolox/mL. Additionally, the antioxidant activity of the digestive fluid was enhanced with increasing ultrasound amplitude. This work linked structural changes in denatured proteins to their functional properties and digestive characteristics. This study provided a new direction for developing easily digestible food ingredients.

The Effects of Pectin Structure on Emulsifying, Rheological, and In Vitro Digestion Properties of Emulsion.

Pectin, a complex hydrocolloid, attracts extensive attention and application stemming from its good emulsification. However, the source of emulsification remains a conundrum. In this experiment, the structures of six kinds of commercial pectin, including LM 101 AS (101), LM 104 AS (104), 121 SLOW SET (121), YM 150 H (150), LM 13 CG (13CG), and ß-PECTIN (ß-P) were determined, and the effects of pectin structure on emulsion emulsification, rheology and in vitro digestibility were studied. The results showed that the ß-P pectin contained a higher content of protein, ferulic acid, and acetyl and had a lower interfacial tension; this pectin-stabilized emulsion exhibited a smaller droplet size and superior centrifugal and storage stability. The results showed that ß-P pectin had higher contents of protein, ferulic acid, and acetyl and lower interfacial tension than other pectins, and its stabilized emulsion exhibited smaller droplet size and superior centrifugation and storage stability. Furthermore, the emulsion formed by the pectin with high molecular weight and degree of methoxylation (DM) had a higher viscosity, which can inhibit the aggregation of emulsion droplets to some extent. However, the DM of pectin affected the charge and digestion behavior of pectin emulsion to a great extent. The smaller the DM, the more negative charge the emulsion carried, and the higher the release rate of free fatty acids. The results provided a basis for the rational selection and structural design of the pectin emulsifier.