Postmortem biochemical and textural changes in the Patinopecten yessoensis adductor muscle (PYAM) during iced storage

Figures & data

Figure 1. ATP and related endogenous degradation products of PYAM during iced storage

(A) The content of ATP, ADP, and IMP; (B) the content of AMP, Hx and Hxr. Data point is the mean of n = 3 for each sampling day. Bars represent the standard deviation. Different letters indicated significant differences from each other (p < .05).

Figure 2. Changes of K value in PYAM during iced storage

Data point is the mean of n = 3 for each sampling day. Bars represent the standard deviation. Different letters indicated significant differences (p< .05).

Figure 3. Changes of water-holding capacity (WHC), TVB-N and pH in PYAM during iced storage

Data point is the mean of n = 3 for each sampling day. Bars represent the standard deviation. Different letters indicated significant differences (p < .05).

Table 1. Changes of the hardness, chewiness, springiness, adhensiveness, shear force in PYAM during storage in ice

Storage time (d)	Hardness	Chewiness	Springiness	Adhensiveness	Shear Force
0	4676.9 ± 248.31^e	2407.2 ± 1006.86^a	0.85 ± 0.11^b	0.32 ± 0.02^b	775.3 ± 20.18^ab
1/3	5208.7 ± 358.83^c	2089.1 ± 572.99^b	0.82 ± 0.08^bc	0.35 ± 0.03^b	882.3 ± 69.44^a
1	5113.3 ± 383.63^d	1671.3 ± 204.01^c	0.95 ± 0.02^a	0.39 ± 0.01^a	865.8 ± 35.41^a
2	6684.1 ± 423.71^a	1566.3 ± 403.21^d	0.77 ± 0.07^cd	0.25 ± 0.06^cd	799.8 ± 22.73^ab
4	5396.5 ± 501.97^b	1201.4 ± 174.04^e	0.75 ± 0.02^d	0.26 ± 0.04^c	773.6 ± 22.56^ab
6	3795.3 ± 257.07^f	1144.0 ± 128.50^f	0.74 ± 0.11^d	0.23 ± 0.03^df	616.5 ± 19.29^bc
8	3549.6 ± 214.42^g	1003.8 ± 152.89^g	0.74 ± 0.07^d	0.24 ± 0.03^cd	540.1 ± 40.07^bc
10	3540.5 ± 358.80^g	920.9 ± 267.98^j	0.63 ± 0.12^e	0.25 ± 0.14^cd	561.3 ± 33.09^bc
12	3232.1 ± 352.27^h	947.4 ± 72.49^h	0.65 ± 0.06^e	0.20 ± 0.01^fj	530.5 ± 23.65^c
14	2284.8 ± 95.75^h	935.9 ± 174.76^i	0.59 ± 0.09^f	0.18 ± 0.01^j	534.7 ± 27.28^bc

Each point is presented with standard error, and different letters indicate significant differences between storage times within treatment.

Table 2. Changes in color parameters in PYAM during storage in ice

Storage time (d)	L*	a*	b*
0	64.12 ± 6.99^a	−2.31 ± 0.06^ab	3.52 ± 0.52^a
1/3	55.29 ± 1.49^ab	−2.20 ± 0.06^ab	2.92 ± 1.14^a
1	58.92 ± 0.82^ab	−2.17 ± 0.20^a	1.82 ± 0.25^a
2	54.75 ± 1.74^ab	−2.24 ± 0.17^ab	1.79 ± 0.48^a
4	55.38 ± 3.15^ab	−2.20 ± 0.22^ab	3.20 ± 0.47^a
6	55.96 ± 1.40^ab	−2.23 ± 0.40^ab	2.58 ± 0.66^a
8	55.77 ± 0.89^ab	−2.87 ± 0.36^ab	2.90 ± 0.67^a
10	55.77 ± 0.89^ab	−2.68 ± 0.10^ab	3.30 ± 1.13^a
12	55.45 ± 3.46^b	−2.61 ± 0.38^ab	3.12 ± 0.78^a
14	52.80 ± 2.10^b	−2.93 ± 0.51^b	2.45 ± 0.35^a

Data represent the mean and standard deviation of n = 6 for each sampling day. Bars represent the standard deviation. Different letters indicated significant differences (p < 0.05).

Figure 4. SDS-PAGE photographs of protein degradation in PYAM during iced storage

20 μg of each sample was loaded in 8% (w/v) SDS-PAGE gel. HM, High molecular Mark; LM, Low molecular Mark

Table 3. Cathepsin activities changes of PYAM during storage in ice

Storage time (d)	CB activity (U/mg protein)	CL activity (U/mg protein)
0	34.00 ± 1.13^a	34.60 ± 1.24^a
1/3	38.33 ± 1.60^b	34.23 ± 2.03^a
1	46.87 ± 1.14^c	35.70 ± 2.93^b
2	48.12 ± 1.66^cd	37.32 ± 2.06^b
4	49.83 ± 1.19^d	37.38 ± 1.14^b
6	59.08 ± 1.28^e	38.94 ± 1.88^c
8	70.82 ± 1.71^f	44.86 ± 1.86^d
10	95.31 ± 3.88^h	47.38 ± 1.33^e
12	80.25 ± 1.66^g	54.44 ± 2.56^f
14	68.46 ± 1.04^e	45.47 ± 2.36^d

Cathepsin activities were measured by a fluorospectrophotometer. Data point is the mean of n = 3 for each sampling day. Bars represent the standard deviation. Different letters indicated significant differences (p< 0.05).