Structural characteristics of Sheldrake meat and secondary structure of myofibrillar protein: effects of oxidation

Figures & data

Table 1. L*, a*, and b* value of non-oxidized and oxidized Sheldrake breast muscle.

	H2O2 concentration n(mM)	0	5	10	15	20	25	30
Instrumental	L*	51.15 ± 1.1^a	48.21 ± 0.2^b	46.49 ± 0.57^c	43.39 ± 0.03^e	42.63 ± 1.19^ed	43.96 ± 2.17^ed	45.63 ± 1.1^d
	a*	9.24 ± 0.21^a	10.53 ± 0.4^b	11.23 ± 0.21^c	12.99 ± 0.5^d	12.38 ± 0.2^d	11.27 ± 0.39^c	11.05 ± 0.4^bc
	b*	14.86 ± 0.34^a	14.64 ± 0.41^ab	14.45 ± 0.29^abc	14.24 ± 0.31^bc	13.95 ± 0.25^c	14.11 ± 0.17^bc	14.32 ± 0.04^bc

Values in a row followed by different letters are significantly different (p < 0.05).

Figure 1. WHC (a), shear force (b), and TBARS value (c) of non-oxidized and oxidized Sheldrake breast muscle.

Figure 2. Protein carbonyls (a), sulfhydryl group contents (b), and the surface hydrophobicity (c) of non-oxidized and oxidized MP.

Figure 3. WHC (a) and textural properties (b) of non-oxidized and oxidized MP gels.

Figure 4. Raman spectra (500–550 cm^–1 region) of non-oxidized (a) and oxidized MP gels treated with different HRGS (5 mM H₂O₂ (b); 10 mM H₂O₂ (c); 15 mM H₂O₂ (d); 20 mM H₂O₂ (e); 25 mM H₂O₂ (f); 30 mM H₂O₂ (g)).

Figure 5. Deconvoluted and curve-fitted Raman bands of amide I of (a) and oxidized MP gels treated with different HRGS (5 mM H₂O₂ (b); 10 mM H₂O₂ (c); 15 mM H₂O₂ (d); 20 mM H₂O₂ (e); 25 mM H₂O₂ (f); 30 mM H₂O₂ (g)).

Figure 6. Relative content of the protein secondary structures (a) and normalized bands intensity (760 and 1340 cm^–1) and I₈₅₀/I₈₃₀ intensity ratio (b) of non-oxidized and oxidized MP gel.