Thermal gelation properties of surimi-like material made fromsheep meat

Meat Science 52 (1999) 429±435

Thermal gelation properties of surimi-like material made from sheep meat R.E. Antonomanolaki a, K.P. Vareltzis a,*, S.A. Georgakis a, E. Kaldrymidou b a

Laboratory of Food Technology, Department of Hygiene and Technology of Food of Animal Origin, Faculty of Veterinary Medicine, Aristotle University of Thessaloniki, Thessaloniki 540 06, Greece b Laboratory of Pathology, Department of Infectious and Parasitic Diseases, Avian Medicine and Pathology, Faculty of Veterinary Medicine, Aristotle University of Thessaloniki, Thessaloniki 540 06, Greece Received 20 July 1998; received in revised form 9 February 1999; accepted 12 February 1999

Abstract Thermal gelation properties of surimi-like material made from sheep meat were investigated. The sheep meat was ground, washed 3 times at a meat to water ratio of 1:5 and dewatered by centrifugation. The e€ects of washing on the composition, functional properties and colour of the mince, were studied. The washing method resulted in a sharp reduction of the fat content and an increase of the water content and pH of the mince. Lightness (L*) and yellowness (b*) of the mince were improved by washing. A signi®cant reduction (p<0.001) of a* (redness) value and a decrease in the a*/b* ratios and saturation index value of the washed mince were recorded. Gels were prepared from washed and unwashed mince after being blended with 2% NaCl and heated at 75 C for 20 min. The washed mince produced excellent gels as measured by the fold test, elasticity modulus and the percentage recovery. The gels made of washed mince had lower expressible ¯uid compared to that of unwashed mince. A ®brous protein network structure was evidenced in the gel made from washed mince while observed under a transmission electron microscope. # 1999 Elsevier Science Ltd. All rights reserved.

1. Introduction Surimi manufacturing has been very successful in the ®sh industry. The high functionality and the variety of product applications of ®sh surimi have resulted in a world-wide popularity of seafood analogues made from ®sh surimi and hence, the production of surimi has been increased (Sonu, 1986; Gwinn, 1992). In recent years, there has been considerable interest in manufacturing surimi-like materials from the muscle of animal species other than ®sh. The characteristics of surimi-like material from poultry meat, beef, pork, sheep meat and also from meat by-products, such as, beef hearts have been studied (Burgen, Field, & McCormick, 1990; Kenney, Kastner, & Kropf, 1992; Liu & Xiong, 1996; McCormick, Burgen, Field, Rule, & Busboom, 1993; Park, Brewer, Novakosski, Bechtel, & McKeith, 1996; Srinivasan & Xiong, 1996; Yang & Froning, 1992). There has been limited research con* Corresponding author. Tel.: +30-31-999804; fax: +30-31999812. E-mail address: [email protected] (K.P. Vareltzis)

cerning the thermal gelation properties of surimi-like material made from sheep meat. Sheep farming in Greece is traditional and has slightly increased in the last decade. While the annual per capita consumption of sheep meat is relatively high in Greece (10 kg) compared to other EU countries (4 kg), it regards the meat mainly from very young animal (lamb meat). Sheep meat, especially meat from animals older than 5 years, has limited commercial use, due to its lesser acceptable qualities compared to lamb or other red meats, in the form of distinctive ¯avour, cooking odour, darker colour and tougher texture (Bushway, Lecomte, Work, & True, 1988). The high fat content of red meat, the more heme pigment and the high concentration of collagen, cause several problems when the red meat is used to produce surimi-like material (Park, et al., 1996). The process used for the production of surimi-like material from red meat involves repeated washing of minced meat with aqueous solution to remove fat, pigments, and other water soluble substances and to produce a crude myosin extract (Varnam & Sutherland, 1995). The application of the surimi technology in the production of a surimi-like material from sheep meat could

0309-1740/99/$ - see front matter # 1999 Elsevier Science Ltd. All rights reserved. PII: S0309-1740(99)00026-1

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provide a new approach towards increasing its value and utilization. The objectives of this study were to develop a technique for the production of a surimi-like material from sheep meat and to determine the e€ects of washing on the composition, functional properties and colour of the surimi-like material. Further studies will follow in order to evaluate the characteristics of the surimi-like material from sheep meat and to explore its potential applications in new product formulations. 2. Materials and methods 2.1. Preparation of water washed mince Fresh meat (24±48 h post mortem) from >6 year old sheep was purchased from a local commercial source (Industrial Abattoir, Veria, GR.). The meat was separated from the vertebral column, ribs and sternum bones, while all visible loose fat was not removed prior to processing. All samples were processed immediately after arriving at the laboratory. The boneless meat was ground through the 4 mm plate of a Toledo table model grinder (Strommer 410.100-12, Denmark) and then the mince was divided into 2 batches weighing 1000 g each. The ®rst one (unwashed mince) was examined immediately or held in a 3 C refrigerator for less than 18 h until the end of the tests and the other was washed by the following procedure. A ¯ow diagram on the washing procedure is given in Fig. 1. The mince (1000 g) was mixed with ®ve volumes of cold tap water (T=3±4 C, pH=7.8‹0.01) in a plastic container. In the ®rst washing cycle, the mixture was stirred using an electric stirrer with two blade metal propellers for 5 min and then allowed to settle for 5 min. The mixture was stirred in the same manner for another 5 min and settled again for 5 min. After settling, the fat layer on the top of the mixture was stripped. The washed mince was strained through a 4 mm metal mesh screen (20 cm diameter, stainless steel) into another container. The washing process was repeated. After the second washing, the mince was blended with 5 volumes of cold water for 5 min at low speed. The resulting slurry was centrifuged at 1500g for 20 min at a constant temperature of 3 C. After the centrifugation, the supernatant was discarded and the washed mince was placed in the center of a bed of three layers thick cheesecloth. The cheesecloth was folded over the top of the mince in such a way that a secured package was achieved from which no mince could escape during the subsequent water extraction. Dewatering was accomplished by pressing the wrapped mince with a Wabash hydraulic press (Model 30-24-SM) for 15 min (Fig. 1). The dewatered mince was removed from the press and immediately manufactured into gels as follows.

Fig. 1. Flow diagram of the washing process.

2.2. Gel preparation Two di€erent gels were made, one from unwashed mince and another from washed mince. Gels were prepared using a cutter type machine (Ronik Food Processor, Model SFR 200) for chopping. The well chilled mince (150 g) was placed in the bowl of the food processor which had been previously chilled to ÿ25 C and was chopped at high speed for 2.5 min with sodium chloride (2% w/w) (Hennigar, Buck, Hultin, Peley, & Vareltzis, 1989; Vareltzis and Buck, 1987). During chopping, the temperature of the paste was maintained below 15 C. The resulting pastes were immediately stu€ed into plastic cylinders (2 cm diameter13 cm height) by a hand sausage stu€er (The Sausages Maker, Bu€alo, N.Y.). The ends were stopped with cork and the cylinders were heated at 75 C for 20 min in a water bath (Park, et al., 1996). The core temperature of the samples was monitored with a thermocouple (Ellab CMC 821). After heating the cylinders were removed from the water bath and cooled in iced water until their internal temperature dropped to <10 C. The gels were then removed from the cylinders, patted dry with paper toweling and wrapped in aluminum foil for overnight storage

R.E. Antonomanolaki et al. / Meat Science 52 (1999) 429±435

in a 3 C refrigerator, prior to subsequent testing. Fifteen experiments were carried out.

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Proximate composition of unwashed and washed mince was analyzed according to AOAC (1990). All determinations were made in duplicate. Collagen was determined by the hydroxyproline colorimetric method (AOAC, 1990), using a spectrophotometer (Bausch and Lomb Spectronic 70) at 560 nm. All analyses were performed in duplicate. The pH of the unwashed and washed mince was determined using standard methods (Korkeala, 1986). Ten grams of each sample were blended at high speed for 1 min with 90 ml of distilled water. An electrode was placed into the resultant slurry, and the meter was allowed to equilibrate for 20 s. Duplicate samples were read.

of the slice of gel was then expressed as a per cent of the original weight. Values reported were the average of six measurements. The mechanical texture measurements of stress, strain, elasticity modulus and percentage recovery were performed by Shimadzu Computer Controlled Universal Testing Machine (model AG-5kNA). Test samples (2 cm in length, 1.9 cm in diameter) were cut perpendicular to the long axis of each cylindrical gel. The single compression test with a 500 kgf compression load cell and 50 mm/min test speed were selected. The gels were subjected to 60% deformation since beyond this level specimens were fractured. The deformation recovery was also determined from compression±decompression cycle using a deformation rate of 50 mm/min in both directions. The recovery is expressed as the ratio between recovered and total deformation multiplied by one hundred (Peleg, 1983; Vareltzis & Buck, 1987). Values reported were the mean of six measurements.

2.4. Colour measurement

2.6. Electron microscopy

The L*, a* and b* colour co-ordinates of unwashed and washed samples were measured by a Hunter Lab Colour Meter (D25-DP9000) with an optical sensor which was standardized with a white colour standard (C20-1651) at the beginning of each measurement session. The samples were placed between two thin glass tiles and the colour of each sample was measured three times, ensuring that each sample was rotated approximately 120 between the di€erent measurements. Additional values (a/ b, Saturation Index) were calculated according to Francis (1975) and Park, et al. (1996).

Tissue specimens (washed mince and its gel) were ®xed in 2.5% glutaraldehyde solution in sodium phosphate bu€er (pH=7.3) and post ®xed in 1% osmic tetroxide with veronal acetate bu€er (pH=7.2). Subsequently, the specimens were dehydrated in acetone and propylene oxide and embedded in ``HEPON 812''. Sections were cut by a Reichert ultramicrotome (Om U2 GA D Austria). The thickness of the ®ne sections was 800 A and they were stained with uranil acetate and lead citrate. Sections were observed by a Zeiss EM- 95-2 electron microscope at 60 kV. All solvents and reagents used were of reagent grade (Merck, Darmstadt, Germany).

2.3. Analysis of proximate composition and pH

2.5. Functional properties of gels Five gels of each batch were examined at room temperature for their functional properties. The fold test procedure (Kudo, Okada, & Miyachi, 1973; Sonu, 1986) involved folding a 3 mm thick by 2 cm diameter slice of gel, ®rst in half and then in quarter, if possible. The evaluation of the gels was performed in accordance with a 5-point grading system reported by Sonu (1986). Values reported were the average of six slices per gel. A Warner±Bratzler Shear (Model 2000) equipped with a dial calibrated in 0.50 g increments to 25 kg was used to shear gel cylinders perpendicular to their long axis. Values (maximum force required to shear the gel) were the average of six measurements. Expressible ¯uid was determined according to Hennigar et al. (1989). A thin slice of gel (3 mm thick2 cm diameter) was placed on a double layer of Whatman ®lter paper No. 1, was covered with another double layer of Whatman ®lter paper and the pack was subjected to a weight of 10.8 kg for 1 min. The weight loss

2.7. Statistical analysis Data were analyzed by one-way analysis of variance (Giannacopoulos, 1996) and Duncan's multiple range test was used to separate means with signi®cant F-values (Steel & Torrie, 1980). 3. Results and discussion 3.1. Proximate composition and pH Proximate composition and pH values of unwashed and washed mince, are given in Table 1. The most obvious e€ect was that the washing reduced the fat content from 23.74‹4.03% to 2.45‹0.66%. This was expected since the repeated water washing, the centrifugation and the lower density of the fat resulted the fat to ¯oat o€ and be removed. The compositional characteristics of washed products were a€ected by the method of preparation. The washing procedure in our

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Table 1 Proximate composition and pH of unwashed and washed mincea,b Treatment

Moisture %

Fat % (wet wt basis)

Fat % (dry wt basis)

Total protein %

Ash %

Connective tissue %

pH

Unwashed Washed

59.60‹4.31a 82.67‹1.71b

23.74‹4.03a 2.45‹0.66b

56.58‹1.10a 14.38‹0.56b

16.62‹1.36a 14.34‹1.39a

0.83‹0.09a 0.40‹0.06b

2.50‹0.82a 3.18‹0.81a

6.05‹0.16a 7.06‹0.18b

a b

Values are expressed as mean‹standard error. Means with the di€erent superscripts within the same column are signi®cantly di€erent (p<0.001).

study did not result in reduction of fat to levels of <1% as reported by McCormick et al. (1993). Nevertheless, the washing procedure reduced the fat content greatly (75% on dry weight basis). The water content of washed mince was 82.67‹1.7%. This water content would result in a ``C-grade'' quality of raw surimi according to the quality standards of the Japan Surimi Association (Sonu, 1986), but it was lower than the results reported by McCormick et al. (1993) due to the dewatering procedure. The ash content was signi®cantly reduced (p<0.001) during the washing procedure. The majority of the water-soluble components, including sarcoplasmic proteins and inorganic salts, were removed during the leaching, while the concentration of the myo®brillar proteins increased. These results are in agreement with those reported by Toyoda, Kimura, Fujita, Noguchi, and Lee (1992). Percentage protein content of the washed mince was not signi®cantly di€erent (p>0.001) from that of the unwashed mince. The washing procedures, using aqueous solutions of NaCl or NaHCO3 were shown to be equally e€ective on removing both fat and water soluble proteins (Bonifer & Froning, 1996). In our study, aqueous washing with tap water (pH=7.8) resulted in the removal of fat and water-soluble proteins. McCormick et al. (1993) reported that the sarcoplasmic proteins were removed during washing of mutton. Lin, Park, and Morrissey (1995) suggested that the ®rst washing in surimi production removed mainly sarcoplasmic proteins. Sarcoplasmic proteins interfere with the functional properties of the contractile proteins (Lanier, 1986). Percent connective tissue content did not signi®cantly increase (p>0.001) in washed mince. Several studies, however, (McCormick et al., 1993; Yang & Froning, 1992) have reported increased collagen content following the washing of meat, most likely due to the insolubility of collagen in water. The high connective tissue content in the washed meat may be undesirable

since collagen could disrupt the continuous protein structure (Yang & Froning, 1992). The pH of the washed mince was signi®cantly increased (p<0.001). The minced meat was washed with tap water having high pH (pH=7.8). Investigations (Dawson, Sheldon, & Ball, 1988; Hernandez, Baker, & Hotchkiss, 1986; Yang & Froning, 1992) have shown that a washing solution of elevated pH resulted in better lipid and pigment reduction. The high pH of the washing solution raises the pH of the meat slurry, making the pigments and blood more soluble and, therefore, easier to be removed, while it may also allow for easier extraction of myoglobin (Dawson, Sheldon, & Ball, 1989). 3.2. Colour The colour values of the unwashed and washed mince are given in Table 2. The lightness (L*) and yellowness (b*) values of the unwashed mince were signi®cantly lower (p<0.001) than those of the washed mince. The increase in the L* values in the washed mince indicates the production of a lighter product. This was probably related to the increase of the moisture content. Reppond and Babbitt (1997) reported that L* value increased linearly with increased moisture content of pollock (Theragra chalcogramma). Hernandez et al. (1986) reported that the higher the pH of the washing medium for mechanically deboned turkey meat, the lighter and less red the resulting product. The high pH of the tap water and the washing procedures we used, resulted in a dramatic reduction of a* (redness) values from 17.65‹1.81 in unwashed mince to 0.17‹0.007 in washed mince, apparently due to the removal of the muscle blood and other pigments. The a*/b* ratio, as an indicator of the colour change in meat, was signi®cantly (p<0.001) lower in the washed mince. Decrease in the a*/b* ratios was also reported by Park et al. (1996), after washing beef and pork to produce a water-washed

Table 2 Average Gardner colour re¯ectance values of unwashed and washed mincea,b L* Unwashed mince Washed mince a b

a* a

45.87‹3.40 74.99‹2.23b

b* a

17.65‹1.81 0.17‹0.007b

SI a

15.79‹0.98 12.78‹0.73b

Values are expressed as mean‹standard error. Means with the di€erent superscripts within the same column are signi®cantly di€erent (p<0.001).

a/b a

24.00‹2.58 12.99‹0.8b

0.90‹0.02a 0.013‹0.0005b

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or a surimi-like product. Di€erences in saturation index between unwashed and washed mince were signi®cant (p<0.001). The washed mince had lower saturation values. Therefore, the purity of colour decreased with the washing procedure. Hernandez et al. (1986) suggested that meat samples which have a dominant red colour would achieve a higher saturation value than those with a more homogenous colour balance (e.g. white). Noticeable decrease in the saturation values due to washing was also reported by Elkhalifa, Graham, Marriot, and Phelps (1988). 3.3. Textural properties The textural properties of the gels made of unwashed and washed mince are given in Table 3. The addition of sodium chloride is essential in order to solubilize the myo®brillar proteins and to produce adequate gels of both washed and unwashed ®sh and red meat muscle (Hennigar et al., 1989). Gel hardness and water-holding capacity increase with the addition of NaCl (Park, Brewer, McKeith, Bechtel, & Novakofski, 1996b). Preliminary tests in our research, showed that the addition of 2% NaCl to both the unwashed and washed mince was essential for the production of good gels. The heatinduced gelation of myo®brillar proteins are considered as very important in the stability and textural aspects of comminuted and reformed meat products. Several studies have been made to asses the e€ect of di€erent temperatures on the gelation properties of surimi-like materials (Park et al., 1996b; Smyth & O'Neill, 1997). Park et al. (1996b) found that the ``setting'' phenomenon which occurred during thermal processing of ®sh surimi gels, did not occur in pork myo®brillar protein gels. The folding test showed signi®cant di€erences in gel strength (p<0.001) between the gels of unwashed and washed mince. Roussel and Cheftel (1988), Hastings, Keay, and Young (1990) and Hastings and Tavendale (1992) mentioned the folding test as very vital in industrial use that would provide a rapid and simple indication of the strength and elasticity of gels. The washed mince formed excellent gels, with the grade of 4.67‹0.47. The water-soluble components, present at the unwashed mince, seemed to a€ect the gel-forming ability of the myo®brillar proteins resulting in a poor quality gel (fold test grade 3.00‹0.64).

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The mechanical texture measurements of elasticity modulus and percentage recovery were also presented in Table 3. The compression testing is widely used to characterise the gelation properties of proteins. The application of the compression without failure (fracturing) provides information on the strength of the elastic elements or ®rmness of the protein gels while the failure compression test measures the degree and strength of protein cross-linkages and therefore, the cohesiveness of the gel (Lee et al., 1997). The elasticity modulus in the failure compression mode was determined automatically and was de®ned as true stress/true strain. It is obvious that the deformability modulus as described by Johnson, Segars, Kapsalis, Normand, and Peleg (1980), as a measure of resistance of the gel to deformation, coincides with the elasticity modulus. There was signi®cant di€erence (p<0.001) in the elasticity modulus between the gels of unwashed and washed mince. The gels made from the washed mince o€ered greater resistance to deformation compared to those from the unwashed mince (Table 3). The higher content of myo®brillar protein in the gels of washed mince should be considered while evaluating these ®ndings. Wimmer, Sebranek, and McKeith (1993) reported that the greater compression resistance by protein gels made from mechanically separated water-washed pork was due to greater protein density. The value for percentage recovery of the gels of washed meat was signi®cantly higher (p<0.001) than the gels of unwashed meat (Table 3). This indicates that the gels from the washed mince were more elastic, which also con®rms the ®ndings of fold test. Although preventive measures were taken to avoid potential errors during preparation of the test sample, the small variability of the results was probably due to various uncontrolled conditions, such as the incorporation of small quantities of air in the gels. Shear force values did not di€er signi®cantly (p>0.001) among the gels of unwashed and washed mince. Shear force data have been used to evaluate ®rmness and rubberiness of ®sh-surimi gels (Boer & Fennema 1989; Lee, Lee, Chung, & Lavery, 1992; Vareltzis & Buck, 1987). Vareltzis and Buck (1987) suggested that the shear test is appropriate for measuring the ®rmness of the gel but it should be combined with other ®ndings for the evaluation of the gel quality. Percentage expressible ¯uid values are shown in Table 3.

Table 3 Textural properties of gels made of unwashed and washed mincea,b Folding test Gels of unwashed mince Gels of washed mince a b

a

3.00‹0.64 4.67‹0.47b

Elasticity modulus kg cmÿ2 a

2.90‹0.88 3.86‹0.71b

Recovery % a

40.26‹3.70 54.82‹3.86b

Values are expressed as mean‹standard error. Means with the di€erent superscripts within the same column are signi®cantly di€erent (p<0.001).

Shear force Kg a

1.35‹0.48 1.27‹0.38a

Expressible ¯uid % 14.28‹2.17a 4.98‹0.24b

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The gels made of washed samples had signi®cant lower values (p<0.001) than the gels made of unwashed mince, although the initial moisture content of the washed mince was comparatively higher. According to Lanier (1985); Ching (1994) and Montero (1994) gelation of the meat proteins gives rise to polymerization of the myo®brillar proteins into a network structure in which, liquid and solid components are entrapped. The high concentration of myo®brillar proteins (Park, Brewer, McKeith, Bechtel, & Novekofski, 1996a) with high pH values are most likely responsible for increasing the water binding capacity in the gel of washed mince (Hennigar et al., 1989). 3.4. Microstructure Transmission electron microscopy was used to examine washed mince and its gel. The washed mince was composed of a mixture of muscle cell structure. The myo®brils ruptured on Z- line or on I- band and the remnants of the membrane structures (mitochondria, sarcoplasmic reticulum) were distended because of the remaining water in the mince. The clear spaces among the cellular structures showed that some water remained in the mince. The washing procedure increased the water content of the mince as it was also shown by the proximate composition of the mince. In some other areas with less myo®brillar rupture, there was distortion on Z-line, because of an unequal contraction (Fig. 2). In the gels, the architecture of the myo®brils disappeared and it was observed a ®lamentous network with darker and lighter areas (Fig. 3). It has been considered that the darker areas contain fragments of actomyocin from A-band and the lighter areas with less myo®brillar rupture contain fragments of actin from Iband (Montero, 1994). The ®lamentous structure constitute of a ®brous network, which gave the gel very

Fig. 2. Transmission electron photomicrograph of washed mince of sheep meat. Mf. myo®brils (arrows), transverse section of myo®brils. Membrane structure (Head arrows). Z, distortion on Z-line. Bar=0.5 mm.

Fig. 3. Transmission electron photomicrograph of gel made from washed mince of sheep meat. Filamentous network with darker (A) and lighter (I) areas. Bar=0.5 mm.

good textural properties. The same observations have also been made by Yang and Froning (1992) who examined washed chicken meat gels by scanning electron microscopy. Moreover, the di€used small clear spaces within the ®brous network showed the greater water holding capacity of the gel. This also explains the low expressible ¯uid values of the gel of washed mince. Collagen did not appear to be in¯uenced by the whole processing. References AOAC. (1990). Ocial methods of analysis (15th ed.). Washington, DC: Association of Ocial Analytical Chemists. Boer, G., & Fennema, O. (1989). E€ect of mixing and moisture modi®cation on toughening and dimethylamine formation in Alaska pollock mince during frozen storage at ÿ10 C. Journal of Food Science, 54(6), 1524±1529. Bonifer, L. B., & Froning, G. W. (1996). Chicken skin composition as a€ected by aqueous washing. Journal of Food Science, 61(5), 895± 898. Burgen, S., Field, R. A., & McCormick R. J. (1990). Development and characterization of surimi-like material from sheep. In 43rd Annual Reciprocal Meat Conference Proceedings (pp. 169). Bushway, A. A., Lecomte, N. B., Work, T. M., & True, R. H. (1988). Characteristics of frankfurters prepared from mutton and fowl. Journal of Food Science, 53(1), 67±69. Ching, H. L. (1994). Fish process for surimi production In Proceedings of Surimi and Minced Fish Products from Underutilised and Pelagic Fish. Athens, Greece, 1±4 November. Dawson, P. L., Sheldon, B. W., & Ball, H. R. (1988). Extraction of lipid and pigment components from mechanically deboned chicken meat. Journal of Food Science, 53(6), 1615±1617. Dawson, P. L., Sheldon, B. W., & Ball, H. R. (1989). Pilot-plant washing procedure to remove fat and color components from mechanically deboned chicken meat. Poultry Science, 68, 749±753. Elkhalifa, E. A., Graham, P. P., Marriot, N. G., & Phelps, S. K. (1988). Color characteristics and functional properties of ¯aked dark meat as in¯uenced by washing treatments. Journal of Food Science, 53(4), 1068±1071, 1080. Francis, F. J. (1975). The origin of tan a/b. Journal of Food Science, 40, 412.

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