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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...
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Published in: | International journal of biological macromolecules 2024-10, Vol.277 (Pt 4), p.134422, Article 134422 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | 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.
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ISSN: | 0141-8130 1879-0003 1879-0003 |
DOI: | 10.1016/j.ijbiomac.2024.134422 |