228: Moderate Ultrasonication Promotes Myofibrillar Protein-Chlorogenic Acid Interaction Under Non-Oxidative or Oxidative Environments and Thermal Gelation

Introduction

Incorporation of phytophenols into meat products has been widely explored for its potential to improve gelling performance. The interactions between meat proteins (primarily myofibrillar protein, MP) and phenolic compounds may involve both noncovalent and covalent bonding. Ultrasonication is known to influence these interactions, which in turn may alter the gelation behavior of meat proteins. The objective of this study was to elucidate the potential role of ultrasound treatment at varying power levels (0–600 W) on the interactions between MP and chlorogenic acid (CA) under both non-oxidative and oxidative environments, with particular emphasis on the structural alterations of MP and their subsequent effects on gelling properties.

Methods

MP samples with or without CA were subjected to ultrasound treatment (0–600 W) in the presence or absence of oxidative stress. Structural changes in MP were assessed by measuring tryptophan fluorescence, surface hydrophobicity, free amines, total sulfhydryls, and crosslinking patterns. The resultant gelling properties were characterized by rheological measurements, gel strength, water state, and gel microstructure analysis.

Results

Compared with untreated MP, the binding of CA, notably under oxidative stress, caused a remarkable reduction in fluorescence intensity, free amines, and total sulfhydryls, along with an increment in surface hydrophobicity. The inclusion of ultrasonication impelled more extensive structural changes, with the most pronounced effects observed at a moderate power level (100 W), insinuating enhanced interactions between MP and CA. Consequently, the gelling potential of MP was impressively improved upon CA binding, especially when assisted by moderate ultrasound (≤ 200 W) under oxidative stress, where up to 69.9% increases in G’ and 33.2% enhancements in gel strength relative to untreated MP were noted. Furthermore, the binding of CA, particularly under oxidative stress, effectively restricted water mobility within the gel network and facilitated the conversion of free water into immobilized water; yet, the sonochemical effects of ultrasound further amplified these changes, evincing a potential synergistic effect between ultrasound treatment and CA binding in ameliorating the gelling performance of MP.

Significance

The results provide a theoretical basis for the application of ultrasound-assisted phenolic treatments as an efficient strategy to enhance the gelling properties and overall quality of processed meat products.

Authors: Xi Sun, Weiqi Zhou, Jiayi Mo, Qingling Wang