Effects of injection of hydrolysis plasma protein solution on the antioxidant properties in porcine M. Longissimus Lumborum
© The Author(s). 2016
Received: 24 November 2015
Accepted: 22 July 2016
Published: 17 August 2016
Plasma protein hydrolysates have been shown to possess antioxidant activity. However, no report has yet to examine the antioxidant effects of injection of plasma protein hydrolysates on meat quality. Therefore, in this study, the effects of injection of hydrolysis plasma protein solution on meat quality and storability were investigated in porcine M. longissimus lumborum.
Twelve pigs were randomly selected at a commercial slaughter plant and harvested. Dissected loins were injected with one of five solutions: C- control (untreated), T1- 10 mM phosphate buffer solution (PBS), T2- 10 mM PBS with 0.01 % butylated hydroxytoluene, T3- 10 mM PBS with 5 % plasma proteins, and T4- 10 mM PBS with 5 % hydrolysis plasma proteins.
T3 and T4 induced greater reduction in protein content of the loin muscle than other treatments. T2 resulted in the lowest pH as well as highest cooking loss. After a storage period of 3-7 days, both lightness and redness of meat were unaffected by all injection treatments. However, yellowness was significantly elevated by treatment with T4 relative to the control. T4 also resulted in the lowest shear force (a measure of meat toughness), suggesting improvement of texture or tenderness. Further, T4 resulted in the most stable TBARS values during storage, indicating that this treatment might retard rancidity in meat.
Injection of porcine M. longissimus lumborum with hydrolysis plasma protein solution could improve overall pork quality, including tenderness and storability.
KeywordsHydrolysis plasma proteins Shear force Lipid peroxidation Meat quality
Addition of marinade solutions to pork and other meat products to enhance quality is a well-established practice in many countries [1, 2]. A combination of salt and phosphate is commonly used to induce synergistic effects in meat tissue [3–5]. This procedure not only improves juiciness and tenderness but also increases the weight of the saleable product, caused by the retention of added water. The concentration of the additive needs to be such that tenderness and juiciness are improved but flavor and color are not adversely affected and the meat is not over-tenderized. The mechanism responsible for increased tenderness and juiciness is linked to increased water retention, and consequent swelling, of myofibrils in the meat .
The relative efficiency of marination for improving juiciness and tenderness in meat has been established based on sensory evaluation . In a prior study, Killefer  injected pork loins 1 h after the animal was slaughtered with a solution of citrate, phosphate, and salt or a solution of only phosphate and salt (control). In their results, increased ultimate pH values, improved color, and decreased cooking loss and shear force values were reported for the treated meat compared to the controls. Sodium citrate has been used as a glycolytic inhibitor in beef muscle to improve tenderness . It has been hypothesized that the pH increase resulting from glycolytic inhibition creates an environment in which protein-denaturing calpains are likely more active. Phosphate injection was originally developed to reduce the the sodium content of processed meats such as ham but has been gradually incorporated into fresh meats as well in order to improve their tenderness and juiciness . Phosphate ‘enhancement’ is now commonly used in the pork industry to increase pH and improve pork quality attributes. Although phosphate injection may increase saltiness and decrease the shelf life of meat , routine use of this method in industry necessitates its inclusion in a study that compares various new technologies for improving pork quality.
The most common synthetic antioxidants, such as butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT), have been widely used for many years to delay lipid oxidation and extend shelf-life of meat . However, concerns about the long-term safety and negative consumer perception of synthetic antioxidants have led to an increasing demand for natural antioxidants in meat and meat products . It has been reported that some protein and enzymatic hydrolysates of meat and meat by-products exert antioxidant effects in food systems . For instance, plasma protein hydrolysates have been shown to possess antioxidant activity . However, no information on the effect of injection of antioxidants on meat quality has been published.
Therefore, the purpose of this study was to investigate the effects of plasma protein injection into pre-rigor porcine M. longissimus lumborum on ultimate pork quality characteristics such as color, muscle pH, shear force, protein solubility, and rancidity during cold storage.
Preparation of non-hydrolysis and hydrolysis bovine plasma protein
To prepare plasma proteins (PP), from cattle blood plasma, 0.5 N ethylenediaminetetraacetic acid (EDTA) as an anticoagulated was added to fresh cattle blood at a ratio 1:9 (v/v), mixed well, and placed immediately on ice for 30 min. Samples were centrifuged by a refrigeration centrifuge (SUPRA 25 K, Hanil Science, Korea) at 14,000 g for 15 min at 4 °C. The plasma powders were freeze-dried (Clean van 8B Freeze-Dryer, BioTron, Inc., Korea), pulverized, placed in sealed bags, and stored at 4 °C.
To prepare plasma protein hydrolysate (PPH), PP solution [5 % w/v 10 mM sodium phosphate buffer (pH 7.0)] was heat-pretreated (90 °C, 5 min) and then hydrolyzed with Alcalase. The enzyme to substrate ratio (E/S) was 2:100 (g/g). The pH of PP solution was adjusted to the optimal value for Alcalase (pH 8.32) before hydrolysis and was readjusted to the optimal value with 1 M NaOH every 15 min during hydrolysis. Hydrolysates were produced by varying the hydrolyzed time to 338 min and hydrolyzed temperature 54 °C. After hydrolysis, the pH of the solution was brought to 7.0 and the solution was then heated at 95 °C for 5 min to inactivate the enzyme. Degree hydrolysis (DH) was determined by assaying free amino groups with 2, 4, 6-trinitrobenzenesulfonic acid (TNBS) according to Alder-Nissen . The DH of hydrolyzed PP was 18.8 %.
Preparation of samples
Approximately 50 min post-mortem, dissected loins were assigned to injection treatments as follows: C- control (untreated), T1- 10 mM phosphate buffer solution (PBS) (pH 7.0), T2- 10 mM PBS with 0.01 % butylated hydroxytoluene (BHT), T3- 10 mM PBS with 5 % plasma proteins, and T4 10 mM PBS with 5 % hydrolysis plasma proteins. Before injection, skin was sliced perpendicular to the length of the loin, at approximately 3-cm intervals, in order to allow the injection needle to penetrate the muscle. Solutions were injected at room temperature. A hand-held injector and 10-cm needles were used to inject the experimental solutions. After injection, pump percentage was calculated. It was assumed that the loin constituted 10 % of the total weight of the side, and absorbed all of the injected solution. Pigs were stunned by using both an electric stunning wand and a captive bolt stunner. after stunning, pigs were exsanguinated and harvested according to normal procedures; the procedure was approved by the institutional Animal Care and Use Committee. After the carcasses and washed, each side was weighed.
Proximate chemical composition analysis
The proximate chemical compositions of the marinated samples were determined following standard procedures prescribed by the Association of Official Analytical Chemists . Moisture, crude protein, fat, and ash contents were determined using the oven, Folch et al. , Kjedahl, and dry ashing methods, respectively.
Approximately 3 g of each meat sample were weighed out, and distilled water was added. A slurry was made out of the meat and distilled water using a homogenizer (Ultra Turrax T25D, IKA, Germany). The pH of each slurry sample was measured, in triplicate, using a digital pH meter (MP230, Mettler Toledo, Switzerland).
Loss due to cooking was determined.
The internal color (International Commission on Illumination L* (lightness), a* (redness), and b* (yellowness)) of the injected porcine M. longissimus lumborum samples were measured using a Minolta Chromameter (Minolta CR 301, Tokyo, Japan) and standardized with a white calibration plate (Y = 93.5; x = 0.3132; y = 0.3198). Internal color was measured at three random locations of the sample surface, and the mean of these values was used in statistical analyses.
Myoglobin content measurement
Protein solubility measurement
In order to determine the solubility of sarcoplasmic and total (sarcoplasmic + myofibrillar) proteins, two extractions were conducted. First, sarcoplasmic proteins were extracted with 10 mL of ice-cold 25 mM potassium phosphate buffer (pH = 7.2), which was added to each of the quadruplicate 1-g muscle samples . The samples were then cut up with scissors, homogenized on ice using a Polytron on the lowest setting (3 × 4-second bursts to minimize protein denaturation through heating), and left on a shaker at 4 °C overnight. Next, the samples were centrifuged at 1,500 × g for 20 min and the protein concentrations of the supernatants were determined by the biuret method, using bovine serum albumin as the standard. Second, total protein was extracted with 20 mL of ice-cold 1.1 M potassium iodide solution in a 0.1 M phosphate buffer (pH = 7.2) which was added to duplicate 1 g samples. Homogenization, shaking, centrifugation, and protein determination of the samples were performed as described for sarcoplasmic proteins. Myofibrillar protein concentration was calculated as the difference between total and sarcoplasmic protein concentrations.
Shear force analysis
Cooked meat samples were allowed to cool to 25 °C, after which three 1.27 cm core samples, oriented parallel to the muscle fiber structure of the meat, were excised. Warner-Braztler shear force, perpendicular to the muscle fiber orientation, was determined for each core using an Instron Universal Testing Machine (Model 1000) with a load cell of 50 kg and a chart speed of 100 mm/min.
The thiobarbituric acid-reactive substance (TBARS) contents of the samples, from each treatment, were determined using the TBA distillation procedure modified by Burge and Aust . Five-gram samples were weighed and homogenized using a homogenizer (Ultra Turrax T25D, IKA, Germany). The homogenate of the samples was transferred to a disposable test tube, into which 10 % butylated hydroxyanisole, and thiobarbituric acid/trichloroacetic acid (TBA/TCA) solution were added. The sample was mixed using a vortex mixer, and then incubated in a boiling water bath for the development of color. After cooling, supernatant solution was determined at 531 nm. The TBARS values were expressed as the number of milligrams of malondialdehyde per kilogram of sample.
Data were analyzed by ANOVA test and Duncan’s multiple comparison was applied to test the significance of differences between groups. Statistical Analysis Systems (SAS, ) was used for analyzing data.
Results and Discussion
Proximate chemical composition analysis
Effects of injection with plasma protein solution on proximate composition (%) in porcine longissimus muscle
71.82 ± 0.34C
4.85 ± 0.37
19.78 ± 0.10A
1.03 ± 0.01
74.22 ± 0.45B
4.37 ± 0.30
19.73 ± 0.10A
1.02 ± 0.04
75.35 ± 0.34A
4.95 ± 0.08
19.38 ± 0.32A
1.06 ± 0.04
73.95 ± 0.29B
4.91 ± 0.24
18.45 ± 0.21B
1.06 ± 0.02
75.17 ± 0.15A
4.81 ± 0.22
17.38 ± 0.01C
1.06 ± 0.02
pH and cooking loss
Effects of injection with plasma protein solution on pH and cooking loss (%) in porcine longissimus muscle, during cold storage
5.67 ± 0.02Aa
5.68 ± 0.02Aa
5.64 ± 0.01Ab
5.54 ± 0.04B
5.53 ± 0.03B
5.48 ± 0.02B
5.45 ± 0.02C
5.47 ± 0.01C
5.42 ± 0.05C
5.54 ± 0.01Ba
5.45 ± 0.01Cb
5.46 ± 0.01BCb
5.69 ± 0.03Aa
5.71 ± 0.02Aa
5.63 ± 0.01Ab
Cooking loss (%)
40.21 ± 0.26Ca
38.22 ± 0.14Bc
38.95 ± 0.82Bab
46.91 ± 1.64A
43.65 ± 0.48A
41.72 ± 2.26AB
45.96 ± 1.64AB
44.13 ± 0.35A
44.00 ± 0.86A
41.75 ± 2.17BC
39.25 ± 2.64B
40.95 ± 0.26AB
41.89 ± 2.68BC
43.41 ± 1.67A
42.19 ± 0.91AB
Quantification of expressible moisture (EM), a measure of the water-holding capacity (WHC) of meat, involves the use of force to expel water from the meat [26, 27]. Therefore, lower EM values coincide with increased breaking force values . Myofibrillar proteins, myosin, actin, and, to some extent, tropomyosin are the main water-binding components of muscular tissue . Denatured or precipitated sarcoplasmic proteins bound to myofibrils play an important role in decreasing the WHC of meat [27, 28].
Cooking loss of samples treated with the experimental solutions was significantly (p < 0.05) higher than those of samples treated with the control, during cold storage (Table 2). Improvements in WHC, observed in meat treated with sodium bicarbonate, may be attributed to increases in muscle pH and ionic strength . Ionic strength may be related to the amount of ions in solution; sodium bicarbonate increases the number of ions, which react with proteins, as well as hydration. However, the treatments in this study failed to improve the WHC of the meat samples. During cold storage, cooking loss of samples injected with the hydrolysis and non-hydrolysis plasma protein solutions was lower than those of samples treated with BHT solution.
Effects of injection with plasma protein solution on CIE L*, a*, and b* in porcine longissimus muscle, during cold storage
58.29 ± 3.02AB
57.84 ± 2.86
57.65 ± 1.54
58.39 ± 2.01AB
58.90 ± 3.56
58.42 ± 2.63
56.53 ± 3.11B
56.46 ± 3.86
56.91 ± 2.60
60.04 ± 0.87A
56.88 ± 3.22
57.22 ± 2.48
58.18 ± 2.32AB
59.89 ± 3.72
57.94 ± 4.95
7.77 ± 0.78BC
7.46 ± 0.54
7.32 ± 0.79
8.56 ± 0.46ABa
7.60 ± 1.12ab
6.93 ± 0.90b
8.95 ± 1.04Aa
7.25 ± 1.10b
7.20 ± 0.55b
7.33 ± 0.54C
7.07 ± 1.38
6.46 ± 0.89
8.40 ± 0.49AB
7.43 ± 0.93
7.44 ± 1.41
6.68 ± 1.20C
7.35 ± 0.68B
6.65 ± 0.65B
7.88 ± 0.38ABa
7.30 ± 0.77Bab
6.60 ± 0.50Bb
7.77 ± 0.27ABa
6.49 ± 0.36Cb
6.50 ± 0.40Bb
7.10 ± 0.64BCa
6.85 ± 0.42BCa
5.93 ± 0.60Bb
8.46 ± 0.18Aa
8.29 ± 0.34Aa
7.61 ± 0.54Ab
This color change in pork loin was expected based on a previously established strong positive relationship between color of pork and pH [30, 31]. PSE and DFD pork differ from normal pork in terms of physiological and biochemical characteristics. The unusual pH and WHC of the PSE and DFD muscles lead to unusual meat colors . In this study, the effects of hydrolysis plasma protein solution injection on muscle pH were dramatic. As the ultimate pH level of the plasma protein solution treated samples was not significantly different (Table 2), the higher a* and b* values can be directly attributed to the injection of hydrolysis plasma protein into pork.
Meat color is one of the most important factors influencing the quality and consumer preferences related to meat, and is considered as an indicator of meat freshness and ‘doneness’ (i.e., how well a meat is cooked) . In measuring bloom on the surface of muscles, Brewer et al.  reported that the L*, a*, and b* values were most correlated to the visual determination of muscle surface pinkness (r = -0.67 to -0.80). Lindahl et al.  reported that heme pigment and metmyoglobin contents are only slightly correlated with peak L* values (r = 0.35–0.45). Furthermore, heme pigment and metmyoglobin contents were less correlated with b* than with a* values (r = 0.40 and 0.50, respectively). Generally, changes in L* values (lightness) over the period of retail display were very subtle . The oxymyoglobin and myoglobin fractions in meat were found to be the most important factors related to variations in b* values . According to Lindahl et al.  observed decreases in b* suggest that the color of pork became less yellow because browning reactions (lower ratio of myoglobin to oxymyoglobin) in cooked meat were fewer.
Changes in metmyoglobin (MetMb)
Effects of injection with plasma protein solution on metmyoglobin percentage of porcine longissimus muscle, during cold storage
4.92 ± 0.04Ac
7.52 ± 0.04Ab
11.54 ± 0.07Aa
4.65 ± 0.07Bc
6.60 ± 0.02Bb
9.87 ± 0.03Ba
4.68 ± 0.05Bc
6.10 ± 0.03Cb
8.04 ± 0.01Ca
4.78 ± 0.02Bc
6.08 ± 0.01Cb
8.03 ± 0.02Ca
4.71 ± 0.03Bc
5.99 ± 0.03Db
7.31 ± 0.05Da
Effects of injection with plasma protein solution on protein solubility (mg/g) in porcine longissimus muscle
197.75 ± 10.87
67.52 ± 1.41B
130.23 ± 9.46AB
208.38 ± 10.82
65.93 ± 0.60B
142.45 ± 11.43AB
217.39 ± 13.52
63.15 ± 1.04C
154.23 ± 14.57A
201.21 ± 2.38
78.80 ± 0.73A
122.41 ± 1.65B
210.65 ± 4.51
67.83 ± 1.20B
142.81 ± 3.30AB
Kauffman et al.  suggested that the increase in protein solubility observed in their study was likely caused by a reduction of protein denaturation in muscles of halothane-sensitive pigs treated with sodium bicarbonate. The findings of Marta et al.  highlight the dependence of myofibrillar and sarcoplasmic protein solubilities on meat quality and NaCl concentration. Further, an increase in total protein solubility, including sarcoplasmic protein solubility, has been reported to decrease drip loss in pork .
Effects of injection with plasma protein solution on Warner-Bratzler shear force (kg/cm2) in porcine longissimus muscle, during cold storage
2.09 ± 0.28Aa
1.61 ± 0.22Cb
2.36 ± 0.42Ba
2.49 ± 0.61A
2.80 ± 0.25A
2.91 ± 0.48A
2.61 ± 0.49A
2.74 ± 0.19A
2.53 ± 0.45AB
2.25 ± 0.65A
2.38 ± 0.17B
2.39 ± 0.36B
1.46 ± 0.46B
1.16 ± 0.19D
1.15 ± 0.20C
Hydrolysis and non-hydrolysis plasma protein solutions showed increased antioxidant activities during cold storage. According to Faustman and Cassens , lipid oxidation and myoglobin oxidation are closely related in meat an increase in one result in a similar increase in the other. This pattern was thought to be related to the direct oxidation of Mb or the destruction of Mb-reducing systems by free radicals generated during lipid oxidation. Guo et al.  reported that, in their study, the low molecular weight fraction (<1 k) of protease N hydrolysate of royal jelly proteins had the greatest antioxidant activity. Further, Park et al.  reported strong antioxidant activity in hydrolysate from egg yolk protein.
Proximate composition of the injection of pre-rigor porcine longissimus lumborum muscle with non-hydrolysis and hydrolysis plasma protein showed higher moisture and lower protein contents than the control. The pH and lightness showed no differences between control and T4, whereas significantly higher redness and yellowness were found in T4. Hydrolysis plasma protein significantly decreased MetMb content during cold storage. Shear force was significantly lower in T4 than control and other treatments. The lower TBARS was observed in the porcine longissimus muscle injected with non-hydrolysis and hydrolysis plasma protein solutions compared to the control.
The main findings of our study are that (1) injection of pre-rigor porcine longissimus lumborum muscle with non-hydrolysis and hydrolysis plasma proteins improves pork quality and (2) longissimus lumborum muscle pH, meat color, tenderness, protein solubility, and lipid oxidation in pork loin are directly affected by the concentrations of injected non-hydrolysis and hydrolysis plasma proteins. Thus, our study clearly highlights the potential use of hydrolysis plasma proteins in improving the tenderness of pork and increasing storage life.
This research was supported (Project No.113027033) by High Value-added Food Technology Development Program, Ministry of Agriculture, Food and Rural Affairs.
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- Bjerklie S. Pumped pork: Palliate or parody?. Meat Processing 1998. p. 94.
- Rust RE. Marketing opportunities for enhanced fresh pork. Meat Int. 1998;8:36–9.Google Scholar
- Detienne NA, Wicker L. Sodium chloride and tripolyphosphate effects on physical and quality characteristics on injected pork loins. J Food Sci. 1999;64:1042–7.View ArticleGoogle Scholar
- Vote DJ, Platter WJ, Tatum JD, Schmidt GR, Belk KE, Smith GC, Speer NC. Injection of beef strip loins with solutions containing sodium tripolyphosphate, sodium lactate, and sodium chloride to enhance palatability. J Anim Sci. 2000;78:952–7.View ArticlePubMedGoogle Scholar
- Murphy MA, Zerby HN. Prerigor infusion of lamb with sodium chloride, phosphate and dextrose solutions to improve tenderness. Meat Sci. 2004;66:343–9.View ArticlePubMedGoogle Scholar
- Offer G, Trinick J. On the mechanism of water holding in meat; the swelling and shrinking of myofibrils. Meat Sci. 1983;8:245–81.View ArticlePubMedGoogle Scholar
- Sheard PR, Nute GR, Richardson RI, Perry A, Taylor AA. Injection of water and polyphosphate into pork to improve juiciness and tenderness after cooking. Meat Sci. 1999;51:371–6.View ArticlePubMedGoogle Scholar
- Killefer J. Effect of enhancement of pork and beef on post mortem events. Proceed. 59th Reciprocal Meats Conference, Lexington, KY;2004.
- Streitel RH, Ockerman HW, Cahill VR. Maintenance of beef tenderness by inhibition of rigor mortis. J Food Sci. 1977;42:583–5.View ArticleGoogle Scholar
- Smith LA, Simmons SL, McKeith FK, Bechtel PJ, Brady PL. Effects of sodium tripolyphosphate on physical and sensory properties of beef and pork roasts. J Food Sci. 1984;49:1636–7.View ArticleGoogle Scholar
- Robbins K, Jensen J, Ryan KJ, Homco-Ryan C, McKeith FK, Brewer MS. Enhancement effects on sensory and retail display characteristics of beef rounds. J Muscle Foods. 2002;13:279–88.View ArticleGoogle Scholar
- de Gonzalez MT N, Boleman RM, Miller RK, Keeton JT, Rhee KS. Antioxidant properties of dried plum ingredients in raw and precooked pork sausage. J Food Sci. 2008;73:H63–71.View ArticleGoogle Scholar
- Ahn J, Gruen IU, Fernando LN. Antioxidant properties of natural plant extracts containing polyphenolic compounds in cooked ground beef. J Food Sci. 2002;67:1364–9.View ArticleGoogle Scholar
- Li B, Chen F, Wang X, Ji B, Wu Y. Isolation and identification of antioxidative peptides from porcine collagen hydrolysate by conseutive chromatography and electrospray ionization-mass spectrometry. Food Chem. 2007;102:1135–43.View ArticleGoogle Scholar
- Salgado PR, Fernández GB, Drago SR, Mauri AN. Addition of bovine plasma hydrolysates improves the antioxidant properties of soybean and sunflower protein-based films. Food Hydrocol. 2011;25:1433–40.View ArticleGoogle Scholar
- Alder-Nissen J. Some fundamental aspects of food protein hydrolysis. In: Enzymic hydrolysis of food proteins. New York: Elsevier Applied Science Publishers; 1986. p. 172–200.Google Scholar
- AOAC. Official methods of analysis. 17th ed. Gaithersburg, MD: Association of Official Analytical Chemists; 2000.Google Scholar
- Folch J, Lees M, Sloane-Stanley GH. A simple method for the isolation and purification of total lipid from animal tissues. J Biol Chem. 1957;26:497–509.Google Scholar
- Boles JA, Swan JE. Effect of post-slaughter processing and freezing on the functionality of hot-boned meat from young bull. Meat Sci. 1996;44:11–8.View ArticlePubMedGoogle Scholar
- Krzywicki K. The determination of haem pigments in meat. Meat Sci. 1982;7:29–36.View ArticlePubMedGoogle Scholar
- Helander EAS. Influence of exercise and restricted activity on the protein composition of skeletal muscle. Bochem J. 1961;78:478–82.View ArticleGoogle Scholar
- Buege JA, Aust SD. Microsomal lipid peroxidation. Methods Enzymol. 1978;52:302–10.View ArticlePubMedGoogle Scholar
- SAS 9.0. The SAS program for window. Cary, NC: The SAS Institute, Inc. 2009.
- Sindelar JJ, Prochaska F, Britt J, Smith GL, Miller RK, Templeman R, Osburn WN. Strategies to eliminate atypical flavours and aromas in sow loins. 1. Optimization of sodium tripolyphosphate, sodium bicarbonate, and injection level. Meat Sci. 2003;65:1211–22.View ArticlePubMedGoogle Scholar
- Wynveen EJ, Bowker AL, Grant AL, Lamkey JM, Fennewalk KJ, Henson L, Gerrard DE. Pork quality is affected by early postmortem phosphate and bicarbonate injection. J Food Sci. 2001;66:886–91.View ArticleGoogle Scholar
- Marcos B, Kerry JP, Mullen AM. High pressure induced changes on sarcoplasmic protein fraction and quality indicators. Meat Sci. 2010;85:115–20.View ArticlePubMedGoogle Scholar
- Owens CM, Hirschler EM, McKee SR, Martinez-Dawson R, Sams AR. The characterization and incidence of pale, soft, exudative turkey meat in a commercial plant. Poul Sci. 2000;79:553–8.View ArticleGoogle Scholar
- Chaijan M, Benjakul S, Visessanguan W, Faustman C. Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand. Food Res Int. 2004;37:1021–30.View ArticleGoogle Scholar
- Kauffman RG, van Laack RL, Russell RL, Pospiech E, Cornelius CA, Suckow CE, et al. Can pale, soft, exudative pork be prevented by postmortem sodium bicarbonate injection? J Anim Sci. 1998;76:3010–5.View ArticlePubMedGoogle Scholar
- Warner RD, Kauffman RG, Greaser ML. Muscle protein changes postmortem in relation to pork quality traits. Meat Sci. 1997;45:339–52.View ArticlePubMedGoogle Scholar
- Joo ST, Kauffman RG, Kim BC, Park GB. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci. 1999;52:291–7.View ArticlePubMedGoogle Scholar
- Faustman C, Cassens RG. The biochemical basis for discoloration in fresh meat: a review. J Muscle Foods. 1990;1:217–43.View ArticleGoogle Scholar
- Mancini RA, Hunt MC. Current research in meat color. Meat Sci. 2005;71:100–21.View ArticlePubMedGoogle Scholar
- Brewer MS, Zhu LG, Bidner B, Meisinger DJ, McKeith FK. Measuring pork color: effects of bloom time, muscle, pH and relationship to instrumental parameters. Meat Sci. 2001;57:169–76.View ArticlePubMedGoogle Scholar
- Lindahl G, Lundstrom K, Tornberg E. Contribution of pigment content, myoglobin forms and internal reflectance to the colour of pork loin and ham from pure breed pigs. Meat Sci. 2001;59:141–51.View ArticlePubMedGoogle Scholar
- McKenna DR, Mies PD, Baird BE, Pfeiffer KD, Ellebracht JW, Savell JW. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci. 2005;70:665–82.View ArticlePubMedGoogle Scholar
- Suman SP, Faustman C, Stamer SL, Liebler DC. Proteomics of lipid oxidation-induced oxidation of porcine and bovine oxymyoglobins. Proteomics. 2007;7:628–40.View ArticlePubMedGoogle Scholar
- Renerre M. Factors involved in the discoloration of beef meat. J Food Sci Technol. 1990;25:613–30.View ArticleGoogle Scholar
- Renerre M, Labas R. Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Sci. 1987;19:151–65.View ArticlePubMedGoogle Scholar
- Carlez A, Veciana-Nogues T, Cheftel JC. Changes in colour and myoglobin of minced beef meat due to high pressure processing. LWT-Food Sci Technol. 1995;28:528–38.View ArticleGoogle Scholar
- Choi YM, Ryu YC, Lee SH, Go GW, Shin HG, Kim KH, Rhee MS, Kim BC. Effects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle. LWT-Food Sci Technol. 2008;41:317–22.View ArticleGoogle Scholar
- Farouk MM, Wieliczko K, Lim R, Turnwald S, MacDonald GA. Cooked sausage batter cohesiveness as affected by sarcoplasmic proteins. Meat Sci. 2002;61:85–90.View ArticlePubMedGoogle Scholar
- Kim YS, Yongsawatdigul J, Park JW, Thawornchinsombut S. Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. J Food Biochem. 2005;29:517–32.View ArticleGoogle Scholar
- Marta G, Guerrero L, Sarraga C. The effect of meat quality, salt and ageing time on biochemical parameters of dry cured Longissimus dorsi muscle. Meat Sci. 1999;51:329–37.View ArticleGoogle Scholar
- Lawrence TE, Dikeman ME, Hunt MC, Kastner CL, Johnson DE. Effects of calcium salts on beef longissimus quality. Meat Sci. 2003;64:299–308.View ArticlePubMedGoogle Scholar
- Baublits RT, Pohlman FW, Brown Jr AH, Yancey EJ, Johnson ZB, Dias-Morse P. Solution enhancement and post-enhancement storage effects on the quality, sensory, and retail display characteristics of beef triceps brachii muscles. J Food Sci. 2006;71:S91–6.View ArticleGoogle Scholar
- Yasui T, Sakanishi M, Hashmoto Y. Phosphate effect on meat, effect of inorganic polyphosphates on solubility and extractability of myosin B. J Agri Food Chem. 1964;12:392–9.View ArticleGoogle Scholar
- Cornforth DP. West EM Evaluation of the antioxidant effects of milk mineral in cooked beef, pork, and turkey. J Food Sci. 2002;67:615–8.View ArticleGoogle Scholar
- Vasavada MN, Cornforth DP. Evaluation of milk mineral antioxidant activity in beef meatballs and nitrite-cured sausage. J Food Sci. 2005;70:C250–3.View ArticleGoogle Scholar
- Guo H, Kouzuma Y, Yonekura M. Structures and properties of antioxidative peptides derived from royal jelly protein. Food Chem. 2009;113:238–45.View ArticleGoogle Scholar
- Park PJ, Jung WK, Nam KS, Shahidi F, Kim SK. Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin free egg yolk. J Am Oil Chem Soc. 2001;78:651–6.View ArticleGoogle Scholar