Effects of Soy Protein Isolate and Inulin Conjugate on Gel Properties and Molecular Conformation of Spanish Mackerel Myofibrillar Protein.

ABSTRACT

The gel properties and molecular conformation of Spanish mackerel myofibrillar protein (MP) induced by soy protein isolate-inulin conjugates (SPI-inulin conjugates) were investigated. The addition of SPI-inulin conjugates significantly enhanced the quality of the protein gel. An analysis of different additives was conducted to assess their impact on the gel strength, texture, water-holding capacity (WHC), water distribution, intermolecular force, dynamic rheology, Raman spectrum, fluorescence spectrum, and microstructure of MP. The results demonstrated a substantial improvement in the strength and water retention of the MP gel with the addition of the conjugate. Compared with the control group (MP), the gel strength increased from 35.18 g·cm to 41.90 g·cm, and WHC increased from 36.80% to 52.67% with the inclusion of SPI-inulin conjugates. The hydrogen bond content was notably higher than that of other groups, and hydrophobic interaction increased from 29.30% to 36.85% with the addition of SPI-inulin conjugates. Furthermore, the addition of the conjugate altered the secondary structure of the myofibrillar gel, with a decrease in α-helix content from 62.91% to 48.42% and an increase in ß-sheet content from 13.40% to 24.65%. Additionally, the SPI-inulin conjugates led to a significant reduction in the endogenous fluorescence intensity of MP. Atomic force microscopy (AFM) results revealed a substantial increase in the Rq value from 8.21 nm to 20.21 nm. Adding SPI and inulin in the form of conjugates is an effective method to improve the gel properties of proteins, which provides important guidance for the study of adding conjugates to surimi products. It has potential application prospects in commercial surimi products.