Effect of ultrasound treatment on functional properties of reduced-salt chicken breast meat batter

Abstract

The effect of ultrasound treatments (40 kHz, 300 W) for different times (10, 20, 30 and 40 min) combined with different salt contents (1.0 %, 1.5 % and 2.0 %) on gel properties and water holding capacity (WHC) of chicken breast meat batter were investigated. Results showed salt level significantly (p < 0.05) affected the texture, storage modulus (G'), loss modulus (G″), cooking loss and WHC. Ultrasound treatments for 10 min and 20 min improved the texture and WHC, and had higher G' values. Compared with the controls (2 % salt), ultrasound treatment for 20 min with reduced-salt (1.5 %) had not significant effect (p > 0.05) on texture, cooking loss or WHC. However, longer ultrasound (40 min) treatment resulted in a decrease in hardness, G' value and WHC. Microstructural analysis revealed that gels treated with ultrasound for 20 min had a compact structure whereas those treated for 40 min contained more protein aggregations and more cavities. Low-field nuclear magnetic resonance (LF-NMR) indicated that ultrasound treatment for 20 min lowered the values of spin-spin relaxation time (T2) and increased the proportion of myofibillar water. Overall, high power ultrasound technology is a promising process which can improve the gelation properties and thereby allowing for a partial reduction in the salt levels in chicken meat gels.

Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

“…Gulseren et al (2007) also pointed out that structural changes in proteins under the influence of ultrasonic radiations are concomitant with the decrease in a-helicity of proteins. Our findings are in agreement with those of Li et al (2015) where ultrasound has been reported to cause decrease in ahelical content of proteins present in chicken meat batters.…”

“…The gels from control samples of myofibrils posses dense aggregates with minute pores. Variation in architecture of heat-induced gels of chicken meat batter due to ultrasonication was also reported by Li et al (2014Li et al ( , 2015. The gels of myofibrils sonicated for 5 min posses disordered structure with large number of dense aggregates having irregularly arranged large pores.…”

“…Protein gels with homogenous and fine arrangement had comparatively higher WHC than gels with non-homogenous structure (Samejima et al 1981). Moreover ultrasonication has been shown to optimise the gelation properties of chicken meat resulting in improved water holding capacity and structure of heat induced gels (Li et al 2014(Li et al , 2015Saleem and Ahmad 2016). Structural changes under ultrasonication, as indicated by CD spectra and hydrophobicity profile, leads to increased exposure of hydrophobic residues.…”

“…As demand for promising techniques to improve sensory and functional properties of meat are continuously growing (Petracci and Cavani 2012), therefore to understand the effect of ultrasonication on structural and functional properties of myofibrils is very important for obtaining desirable functional meat products and stable meat qualities. Li et al (2014Li et al ( , 2015 has successfully demonstrated the association between structural changes induced by ultrasound and gelation properties of chicken meat. However, these reports describe the application of ultrasound in structured whole muscle where influence of ultrasonication (in presence of various factors) on gelling properties of myofibrils is not clearly understood.…”

Effects of power ultrasound on oxidation and structure of beef proteins during curing processing

“…Furthermore, previous studies have confirmed that the structure and the function of proteins can be modified by applying PUS. Li et al [6] found that high-intensity PUS could be used to modify the functionality of PSE (Pale, soft and exudative)-like meat by changing the secondary structures of proteins, thereby improving the microstructure and rheological properties of gels. Hu et al [7] reported that PUS treatment of soy protein isolates led to an increase in the surface hydrophobicity and solubility of proteins, again affecting its microstructure and rheological properties.…”