Washing and Cryoprotectant Effects on Frozen Storage of Spent Hen Surimi A. A. Nowsad,*,1 W. F. Huang,† S. Kanoh,† and E. Niwa† *Department of Fisheries Technology, Bangladesh Agricultural University, Mymensingh 2202, Bangladesh; and †Laboratory of Marine Biopolymer Chemistry, Faculty of Bioresources, Mie University, Tsu 514, Japan protein solubility, expressible moisture, cooking yield, folding test, drip-loss, and sensory scores) were decreased in both unwashed and washed mince, mostly during the early stages of storage. Washed mince showed significantly better textural properties than unwashed mince. Washing protected the gel quality of the hen mince from degradation during frozen storage. Cryoprotectants could not protect the gel strength or breaking strength, but deformation was slightly improved. Water-retention properties were protected, and folding test and sensory scores were well preserved in the mince with added CP. Cryoprotectants had a beneficial effect on frozen, stored spent hen surimi to protect the elasticity and cohesiveness of the gel.
ABSTRACT Mince of 98-wk-old spent hens was washed two times with 0.1% NaCl. Portions of unwashed and washed mince were mixed with a cryoprotectant (CP) composed of 4% sucrose, 4% sorbitol, and 0.2% Natripolyphosphate and were immediately frozen and stored at –20 C. Mince without CP was run as control. Textural properties of the stored mince and surimi were measured at 1-mo intervals for 6 mo, after being thawed at 4 C overnight, ground with 3% NaCl, and heated at 90 C for 15 min. For freeze-thaw stability study, minces were subjected to six freeze-thaw cycles. Each freeze-thaw cycle was carried out at 1 mo of storage. Textural quality parameters (gel strength, breaking strength, deformation,
(Key words: spent hen, water washing, surimi, frozen storage, cryoprotectants) 2000 Poultry Science 79:913–920
the functional properties of surimi protein, such as gelforming ability, water-retention properties, and protein solubility (Lanier, 1986; Lee, 1984, 1986). The loss of functionality is due to the denaturation of protein, because freezing increases solute concentration and favors dehydration, both of which contribute to protein denaturation (MacDonald and Lanier, 1991). To protect the functionality of fish surimi protein during frozen storage, various cryoprotectants (CP), such as sucrose, sorbitol, and polyphosphates, have been blended with surimi (Okada, 1985). Sucrose and sorbitol improve the gel-forming ability, increase protein solubility, and decrease cooking loss (Park et al., 1988; Yoon and Lee, 1990; Sych et al., 1991). Sorbitol is combined with sucrose to reduce sweetness of the products. In addition to its function to protect myosin from denaturation (Konno et al., 1997), sorbitol enhances the cohesiveness of thermo-induced gels by controlling the cross-linking reactions of myosin during setting (Kimura et al., 1991). Polyphosphate in meat and seafood increases textural strength and moisture retention during processing by increasing pH, ionic strength, and protein solubility (Okada, 1985; Chang and Regenstein, 1997a). Bend-
INTRODUCTION Utilization of various animal by-products as human food in the form of surimi has been increased due to its convenient food applications. Successful surimi like materials have been produced from beef and pork muscles (Park et al., 1996a,b), beef heart (Wan et al., 1993; Xiong et al., 1993; Wang et al., 1997; Wang and Xiong, 1998), and mechanically deboned chicken meat (MDCM), especially from the residual parts of the meat-producing broiler chicken (Ball, 1988; Dawson et al., 1989; Smyth and O’Neill, 1997). Recently, we prepared surimi from spent hen and investigated its thermal gelation properties (Nowsad et al., 2000). Spent hen mince is an underutilized by-product of the poultry industry. Objectionable toughness of hen mince due to a high amount of heat-stable collagen (Nakamura et al., 1975) prevents it from being used in whole-meat products and, hence, reduces its market value (Nurmahmudi and Sams, 1997). We found that spent hen surimi produced a harder gel than broiler surimi but had similarly high cooking yield and water-holding capacity. Frozen storage is an essential step in surimi manufacture. Frozen storage brings about detrimental changes in
Abbreviation Key: BS = breaking strength; CP = cryoprotectants; C/ R = chewiness/rubberiness; CY = cooking yield; De = deformation; EM = expressible moisture; FT = folding test; GS = gel strength; MDCM = mechanically deboned chicken meat; PS = protein solubility; S/F = softness/firmness, UM = unwashed mince.
Received for publication March 29, 1999. Accepted for publication February 7, 2000. 1 To whom correspondence should be addressed:
[email protected].
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the functionality of spent hen surimi during long-term frozen storage.
MATERIALS AND METHODS Mince and Surimi
FIGURE 1. Scheme for the preparation of surimi and heat-induced gel from spent hen mince.
hall (1954) showed that phosphates (such as pyrophosphate) were able to dissociate actomyosin into actin and myosin, which increased the moisture retention of protein. Chang and Regenstein (1997b) reported that sodium tripolyphosphate was most effective in enhancing textural strength and moisture retention of frozen surimi. Cryoprotectants (CP) have been shown to have marked effect on the preservation of the functionality of various warm-blooded animal muscles, such as beef mince (Park et al., 1993), beef heart surimi (Wang and Xiong, 1998), and chicken myofibrillar protein isolates (Trziszka et al., 1991; Uijttenboogaart et al., 1993). Conversely, Park et al. (1996b) reported that addition of CP prior to freezing had no protective effect on the gel-forming ability and freezethaw stability of frozen stored pork and beef surimi. Earlier, Nowsad et al. (2000) found that CP greatly improved the gel quality of spent hen surimi before freezing, but had very little effect in protecting the gel strength during 4-wk storage at –20 C. Due to the discrimination of results among various studies, a question has arisen if CP are at all needed to protect the functionality of washed chicken mince during frozen storage. Another question that remains unresolved concerns whether water washing only is sufficient to preserve its functional properties. There is no published report concerning washing and CP effects on chicken surimi for long-term freezing preservation. Therefore, the objective of this study was to investigate the effects of washing and common CP (comprising 4% sucrose, 4% sorbitol, and 0.2% Na-tripolyphosphate) on
2
Waring Products Division, New Hartford, CT.
A scheme for the preparation of surimi and heat-induced gel from spent hen (98 wk) breast and thigh muscles is given in Figure 1. After exsanguinating the birds, the muscles were excised manually, minced by a mechanical mincer (2-mm orifice diameter), and passed twice more through a fine sieve (1-mm orifice diameter) (Nowsad et al., 2000). Batches of spent hen mince (100 g/batch) were washed with prechilled (4 C) 0.1% NaCl solution (400 mL) by stirring in a commercial blender (model 35BL64)2 at a low speed for 2 min and then were allowed to settle for 8 min. Floating fat was skimmed off. Washed meat was collected by centrifugation (8,000 × g, 15 min). Unwashed and washed mince were blended with 4% sucrose, 4% sorbitol, and 0.2% Na-tripolyphosphate CP. Mince without CP was run as the control. The mince and surimi were vacuum-packaged in plastic bags, quickfrozen at –40 C, and stored at –20 C until analysis.
pH and Protein Solubility Muscle and gel pH were measured by direct insertion of an electrode into the sample (Sakura et al., 1993). For the measurement of protein solubility, a 0.5-g sample was solubilized in 9.5 mL of 8 M urea, 2% 2-mercaptoethanol, 2% SDS, and 50 mM Tris-HCl (pH 8.0). An equal volume of 15% trichloroacetic acid was added to the mixture. The precipitate was collected by centrifugation (10,000 × g, 20
FIGURE 2. Effects of washing and cryoprotectants (CP) on the pH of spent hen surimi stored at –20 C. Error bars are standard errors of the means. UM = unwashed mince; WM = washed mince.
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FROZEN STORAGE OF SPENT HEN SURIMI TABLE 1. Correlation coefficient-(r) matrix of different textural quality attributes of spent hen surimi Correlations1
GS
BS
De
PS
CY
EM
FT
S/F
C/R
pH GS BS De PS CY EM FT S/F
0.6995**
0.8092** 0.8978**
0.2159 0.6715* 0.2998
0.8204** 0.7118** 0.6570* 0.5287*
0.7187** 0.4709 0.1335 0.3914 0.4826*
−0.7235** −0.6368* −0.5409* −0.5354* −0.9711** −0.8293**
0.5029* 0.3380 0.2091 0.4895* 0.7290** 0.8112** 0.7898**
0.4075 0.3329 0.1889 0.4939* 0.6494* 0.8210** −0.6876** 0.8755**
0.4572 0.4437 0.3194 0.5146* 0.6010* 0.7935** −0.6757* 0.8199** 0.9313**
GS = gel strength; BS = breaking strength; De = deformation; PS = protein solubility; CY = cooking yield; EM = expressible moisture; FT = folding test; S/F = softness/firmness; C/R = chewiness/rubberiness. *P < 0.01; **P < 0.001. 1
min) and was dissolved in 1N NaOH, and the protein in solution was measured by the Biuret method (Nishimoto et al., 1987).
Thermally Induced Gel Frozen, stored mince and surimi were thawed at 4 C overnight, chopped for 1 min by a knife, and ground with 3% NaCl for 10 min in a mortar at 4 C. Final moisture content was adjusted to 80% with cold water. Ground paste was extruded with a hand sausage stuffer into a sausage casing (1.8-cm diameter, 35 cm long)3 and was heated in a 90 C water bath for 15 min to produce gel. After heat processing, gels were immediately cooled in ice water for 20 min and kept at room temperature for 2 h before the gel quality analysis.
Gel Quality A puncture test was carried out on the gel sample (2.5cm height) at a table speed of 6 cm/min using a food rheometer equipped with a spherical plunger (5-mm diameter)4. Gel strength (GS) was expressed as the product of breaking strength (g) and deformation (cm). A folding test (FT) was carried out by folding a 2 mm thick sample disc into halves and quarters. The scales for the FT were 4 = no cracks when folded into quarters; 3 = no cracks when folded in half, but cracked when folded into quarters; 2 = cracks when folded in half; 1 = broken and split into halves. Expressible moisture (EM) was determined by compressing a gel slice (about 1.0 g) between two double layers of filter paper (Advantec No. 3)5 at a pressure of 1 kg/cm2 for 3 min and was calculated from its weight before and after compression. The EM was expressed as the percentage of the total gel weight. Cooking yield (CY) was calculated from the ratio of the weight of cooked and uncooked samples as described by Amato et al. (1989).
3 Polyvinyledene chloride casing, Krehalon casing, Kureha Chemical Co. Ltd., 1-9-11 Nihonbashi, Chuoku, Tokyo 103-8552, Japan. 4 NRM-2010J-CW, Fudoh Kogyo Co. Ltd., 3-8-2 Hongo, Bunkyoku, Tokyo 113-0033, Japan. 5 Toyo Roshi Co. Ltd., Tokyo 111-0042, Japan. 6 Suzuran威, Nisshinbo, Tokyo 104-4552, Japan.
A nine-person trained panel of students and staff provided the sensory assessments (Nowsad et al., 2000). Softness/firmness (S/F) was defined as the amount of force required to bite through the sample with incisors, and chewiness/rubberiness (C/R) was defined as the amount of effort that panelists had to exert in chewing to prepare the sample for swallowing (Szczesniak et al., 1963). The quality was evaluated by numerical scores up to 10, where for S/F, 1 = very soft; and 10 = extremely firm, and for C/R, 1 = not chewy/rubbery; and 10 = extremely chewy/rubbery.
Freeze-Thaw Stability For the freeze-thaw study, unwashed and washed mince with CP added or without CP were vacuum-packaged in Ziploc威 bags and stored frozen as described before. Minces were subjected to six freeze-thaw cycles. Each freeze-thaw cycle was carried out at 1 mo of storage, and thawing was done at 4 C overnight. Freeze-thaw stability was determined by measuring gel strength and thaw-drip. To measure thaw-drip, preweighed frozen mince was thawed, blotted dry with paper towels,6 and reweighed. Percentage weight loss after thawing, based on initial frozen weight, was recorded as thaw-drip (DeFreitas et al., 1997).
Statistical Analysis The data for gel quality parameters were mean values from three replications. Here, replications refer to the experimental work for gel quality tests from different fresh and frozen-stored minces and surimis (unwashed mince, washed mince, surimi from unwashed mince, and surimi from washed mince; Figure 1). In each replication, triplicate gel samples were prepared and tested. One-way analysis of variance (Steel and Torrie, 1980) was used to compare the treatment effects. Least significant difference at P < 0.05 and a significant F-ratio were used to determine significant differences between mean values. Correlation coefficients (Steel and Torrie, 1980) were calculated to determine relationships between the textural parameters.
RESULTS AND DISCUSSION The unwashed spent hen mince used in this study had 76.22 + 0.92% (SE) moisture, 18.74 + 0.54% protein, 4.43
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+ 0.32% lipid, and 9.90 + 1.30 mg/g collagen. After washing, the composition was changed to 77.13 + 1.59% moisture, 21.20 + 0.67% protein, 0.94 + 0.03% lipid, and 14.83 + 0.92 mg/g collagen. Washing increased the pH of mince from 6.5 to 6.9 (Figure 2). The pH of unwashed and washed mince with CP added or without CP declined at 1 to 2 mo storage and then stabilized at a more or less constant value. Decrement of pH significantly correlated with the loss of textural qualities [GS, BS, protein solubility (PS), CY, EM, and FT] (Table 1) during storage. Cryoprotectants had no influence on pH of unwashed and washed mince. Various authors have found a positive correlation with tripolyphosphate and pH increment of surimi (Hamm, 1970; Okada, 1985). Chang and Regenstein (1997a), however, reported that sodium hexametaphosphate with sucrose and sorbitol partially inhibited the pH increase in frozen codfish mince. Washing increased the GS of fresh hen mince at 0 mo storage and, consequently, at all frozen storage periods (Figure 3). Cryoprotectants also greatly increased the GS in washed mince but hardly in unwashed mince at 0 mo storage. Gel strength and breaking strength (BS) sharply decreased at 1 mo storage, indicating a sudden deterioration of gel texture. After 1 mo storage, however, the quality parameters remained constant or increased slightly up to 6 mo. This result agrees with Hsieh and Regenstein (1989) and Jahncke et al. (1992), who reported that the texture deterioration in frozen stored fish mince occurred soon after freezing. Smyth and O’Neill (1997) found a progressive decrease in gel strength of surimi from MDCM up to 28 d of freezing and no decrease thereafter. In storage, GS and BS were higher in washed mince than in unwashed mince. No differences in GS and BS were, however, observed between the washed mince with CP added and that without CP or between the unwashed mince with CP added and that without CP. This finding indicated that washing alone could reduce GS loss in hen mince during storage, but CP had no such effect. Deformation (De) was slightly higher in the CP-incorporated washed mince than the other minces and increased during storage. Breaking strength expresses the hardness, and De reflects the stickiness or the elasticity of a gel (Lee, 1986; Niwa, 1995). Deformation is influenced mainly by protein quality and is considered to be an important measure of protein functionality (Hamann, 1988). Yamamoto (1986) found that De was more important than BS in explaining kamaboko gel texture. In our study, the product of the two parameters, GS, decreased in all minces during frozen storage. On the other hand, like De, FT, S/F, and C/R reflect the elasticity and cohesiveness of a gel (Niwa, 1995). In the present study, however, De failed to show any strong correlation with FT and sensory S/F and C/R tests (Table 1). The FT and sensory test were found to be key measures that reflect the protection of gel elasticity and cohesiveness by CP (Uijttenboogaart et al., 1993). Therefore, the puncture test results suggest that CP could not protect the gel hardness of hen mince during frozen storage, although the extent of textural
FIGURE 3. Effects of washing and cryoprotectants (CP) on the gel strength of spent hen surimi stored at –20 C. Gels were prepared by heating the pastes at 90 C for 15 min. UM = unwashed mince; WM = washed mince. Error bars are standard errors of the means.
deterioration in hen was not as severe as generally observed in piscine muscle. The freeze-thaw stability study showed a similar textural change (Table 2). Washed and unwashed mince lost 13 to 21% of the initial GS after 1 mo storage at –20 C. The loss of GS was not recovered even if CP was added to either unwashed or washed minces. Apparently, the percentage loss of GS was greater in CP-incorporated gels. This loss was due to the higher initial values of GS
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FROZEN STORAGE OF SPENT HEN SURIMI TABLE 2. Freeze-thaw stability of spent hen surimi Percentage gel strength
Thaw-drip
FTC1
UM
WM
UM+CP
WM+CP
UM (%)
WM (%)
UM+CP (%)
WM+CP (%)
0 1 2 3 4 5 6
100 79 79 81 75 77 80
100 87 82 79 80 80 77
100 71 70 74 72 75 76
100 65 65 70 71 70 69
— 10.0a 8.90a 8.84a 8.81a 8.82a 8.30a
— 9.08a 8.74a 8.68a 8.70a 8.72a 8.12a
— 2.02b 1.70b 1.70b 1.65b 1.67b 1.65b
— 1.23b 1.06b 1.11b 1.12b 1.05b 1.07b
Means within a column with no common superscript differ significantly (P < 0.05). FTC = freeze-thaw cycles; UM = unwashed mince; WM = washed mince; CP = cryoprotectants.
a,b 1
in such mince. During repeated freezing and thawing, all minces, with or without CP, lost GS to the same degree. Thaw-drip decreased significantly (P < 0.05) in the mince with CP added. Decrement of thaw-drip, however, had no influence on the gel strength. Lesiak et al. (1997) found that the difference in thaw-drip in frozen, stored turkey breast muscles was not reflected in the shear force and water-holding capacity of cooked gels. Thaw-drip in both unwashed and washed mince with CP added and without CP decreased little (P > 0.05) in the freezethaw cycles. Both unwashed and washed mince without CP showed a gradual decrease in PS at –20 C (Figure 4). This decline was expected, because myofibrillar protein solubility decreases with the formation of insoluble high molecular weight protein aggregates during frozen storage (Xiong, 1997). In our study, PS decrement was more intense in unwashed mince than in washed mince. Higher PS in washed mince might be due to the concentration of myofibrillar proteins caused by washing. In the mince with CP added, PS suddenly decreased at 1 mo but soon stabilized
FIGURE 4. Effects of washing and cryoprotectants (CP) on the protein solubility of spent hen surimi stored at –20 C. Error bars are standard errors of the means. a–cMeans with different letters differ significantly (P < 0.05). UM = unwashed mince; WM = washed mince.
thereafter, and at 6 mo, the value still remained high in CP-treated and washed mince, which indicates a protective effect of both washing and CP on chicken myofibrillar protein. Cryoprotectants in a frozen meat system exert protecting and stabilizing effects on myofibrillar protein through reducing the quantity of frozen water in the protein matrix and modification of protein-protein interactions (Noguchi et al., 1975). Analysis of variance showed that washing significantly affected PS. Protein solubility was correlated with instrumental (P < 0.01) and sensory (P < 0.001) scores of the gel (Table 1). Expressible moisture (EM) was higher (P < 0.05) in unwashed mince than in washed mince (Figure 5). The EM progressively increased at –20 C, which was expected, because the texture deteriorates with the increment of free water during frozen storage (Samson and Regenstein, 1986). Increment of EM was significant (P < 0.05) at 1 mo but was not changed thereafter. Cryoprotectants lessened the amount of EM of the mince in storage. The effect of CP was greater in washed mince (P < 0.05) compared
FIGURE 5. Effects of washing and cryoprotectants (CP) on the expressible moisture (EM) of the gel from spent hen surimi stored at –20 C. Gels were prepared by heating the pastes at 90 C for 15 min. Error bars are standard errors of the means. a–dMeans with different letters differ significantly (P < 0.05). UM = unwashed mince; WM = washed mince.
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FIGURE 6. Effects of washing and cryoprotectants (CP) on the cooking yield of the gel from spent hen surimi stored at –20 C. Gels were prepared by heating the pastes at 90 C for 15 min. Error bars are standard errors of the means. a–fMeans with different letters differ significantly (P < 0.05). UM = unwashed mince; WM = washed mince.
with unwashed mince. Expressible moisture was found to be an effective measure to determine the textural change of hen mince in frozen storage. The usefulness of EM in monitoring the early changes of textural quality in frozen, stored fish surimi was also reported by other researchers (Hsieh and Regenstein, 1989; Jahncke et al., 1992). Expressible moisture values corresponded well with other textural and sensory parameters and showed a good correlation (P < 0.001) with pH, PS, CY, FT, and sensory scores but a moderate relation (P < 0.01) with instrumental GS, BS, and De (Table 1). At 0 mo storage, cooking yield (CY) was higher in washed mince than in unwashed mince, and addition of CP further increased CY value (Figure 6). The CY of either washed or unwashed mince with added CP or without CP sharply decreased (P < 0.05) at 1 to 2 mo storage
and then remained unchanged (P > 0.05). Cryoprotectants significantly (P < 0.05) lessened the decrement of CY at – 20 C in both unwashed and washed minces. Cooking yield maintained a significant correlation (P < 0.001) with the FT and sensory results (Table 1). Expressible moisture and CY are indices of water-retention properties of muscle foods. Increased water retention in the CP-incorporated hen mince might be due to huge functional OH groups of sucrose and sorbitol, through which they could bind to the proteins, resulting in increased protein hydration. Chang and Regenstein, (1997a) found that the amount of free water decreased in frozen-stored CP-incorporated fish mince, because polyols surrounded proteins and bound water through hydrogen bonds. Effects of washing and CP on the FT and sensory scores of the gel from stored mince are presented in Table 3. The FT scores were high in all fresh minces (0 mo storage) with or without added CP. In frozen storage, FT scores decreased in all minces except in washed mince with added CP. In washed mince with added CP, the value remained constant throughout the storage period, indicating a protecting effect of CP in such mince. The FT score in unwashed mince with CP added was also significantly better (P < 0.05) than that of the corresponding unwashed mince without CP. The FT reflects both gel cohesiveness and stickiness in instrumental measurements (Niwa, 1995), and can reflect gel degradation even if the hardness of the gel is high (Kinoshita et al., 1990). In our study, FT results were significantly related to De, PS, EM, CY, and sensory scores (Table 1). This result agrees with that of Uijttenboogaart et al. (1993), who found a significant increase of FT scores in the gel of myofibrillar protein isolate from MDCM with sucrose and sorbitol added. Sensory S/F and C/R values were significantly higher (P < 0.05) in the gels of washed mince compared to unwashed mince. The values decreased at 1 mo storage in the gels from all unwashed and washed minces with or without added CP. The values remained constant or slightly increased during successive storage up to 6 mo.
TABLE 3. Effects of washing and cryoprotectants on the folding test and sensory scores of the gel from frozen stored spent hen surimi1 Storage period Parameter
Treatment
0 mo
1 mo
2 mo
3 mo
4 mo
5 mo
6 mo
FT
UM WM UM+CP WM+CP UM WM UM+CP WM+CP UM WM UM+CP WM+CP
4a 4a 4a 4a 6.2b 6.8c 7.1cd 7.5d 6.2c 7.3d 7.3d 7.8e
2c 3b 3b 4a 5.0a 5.0a 6.0b 6.5bc 5.0b 4.1a 5.3b 7.0d
2c 1d 2c 4a 5.3ab 5.2a 6.1b 7.3cd 5.0b 4.5ab 5.2b 7.0d
2c 2c 3b 4a 5.2a 5.1a 6.0b 7.0c 5.0b 4.2a 5.0b 7.2d
1d 2c 3b 4a 5.2a 4.9a 6.2b 6.9c 4.7ab 4.9b 5.6bc 7.0d
1d 2c 3b 4a 5.3ab 4.8a 5.9b 7.0c 5.3b 5.0b 5.8bc 7.1d
1d 2c 3b 4a 5.5ab 5.2a 5.7b 7.3cd 5.5bc 5.2b 5.6bc 7.0d
S/F
C/R
Means within the same parameter with no common superscript differ significantly (P < 0.05). UM = unwashed mince; WM = washed mince; CP = cryoprotectants; FT = folding test; S/F = softness/ firmness; C/R = chewiness/rubberiness. Gels were prepared by heating the pastes at 90 C for 15 min. a−d 1
FROZEN STORAGE OF SPENT HEN SURIMI
The instrumental values of gel strength, along with PS and water-retention properties, showed a similar trend. Sensory scores, however, were markedly low (P < 0.05) in the mince without CP compared with those with added CP. Without CP, both unwashed and washed mince produced tougher gel, resulting in marked lower sensory scores than the CP-incorporated unwashed and washed minces. Conversely, an increased cohesiveness was evident in the gel from mince with CP added, as was also observed from their higher FT results. Kimura et al. (1991) reported that sorbitol enhanced the cohesiveness of fish surimi by controlling the protein cross-linking during setting. Washing and CP both affected FT and sensory results, suggesting that they protected hen mince during storage. Softness/firmness and C/R maintained a significant correlation with De, PS, CY, and FT scores (Table 1).
CONCLUSIONS Washed mince showed significantly better textural properties than unwashed mince in frozen storage. Gel quality was deteriorated mostly during the early stages of storage. Sucrose, sorbitol, and polyphosphate at 4, 4, and 0.2%, respectively, did not protect the GS of the stored mince but prevented the gel from becoming tough and rubbery by effectively protecting their water-binding properties. Cryoprotectants also maintained FT and sensory scores of the gel during storage.
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