Browse > Article
http://dx.doi.org/10.5851/kosfa.2007.27.3.267

Effect of Cryoprotectants on the Physico-chemical Characteristics of Chicken Breast Surimi Manufactured by pH Adjustment during Freezing Storage  

Jin, Sang-Keun (Department of Animal Resources Technology, Jinju National University)
Kim, Il-Suk (Department of Animal Resources Technology, Jinju National University)
Kim, Su-Jung (Department of Animal Resources Technology, Jinju National University)
Jeong, Ki-Jong (Department of Animal Resources Technology, Jinju National University)
Lee, Jae-Ryong (Department of Animal Resources Technology, Jinju National University)
Choi, Yeung-Joon (Division of Marine Bioscience, Gyeongsang National University)
Publication Information
Food Science of Animal Resources / v.27, no.3, 2007 , pp. 267-276 More about this Journal
Abstract
This study was conducted to determine the effect of cryoprotectants (sugar, sorbitol, polyphosphate) on the physico-chemical characteristics of chicken breast surimi manufactured by pH adjustment (pH 11.0) during freezing storage. The final surimi was divided into experimental units to which the following treatments were randomly assigned: C (Alaska pollack surimi: two washings, 4% sugar +5% sorbitol ${\pounds} 0.3% polyphosphate additive): T1 (chicken breast surimi: pH 11.0 adjusted, 0.3% polyphosphate additive): T2 (chicken breast surimi pH 11.0 adjusted, 5% sorbitol +0.3% polyphosphate additive); T3 (chicken breast surimi: pH 11.0 adjusted, 4% sugar +5% sorbitol +0.3% polyphosphate additive). The crude protein content of the control was higher than all treated samples, however the moisture, crude fat and crude ash of T3 were higher than the control (p<0.05). The pH, WHC and collagen content of the control were higher than all of the treated samples, and these values decreased with storage time for all treatments and the control (p<0.05). The cholesterol content of the control was lower than all treated samples, but the myofibrillar protein contents of all treated samples were higher than the control (p<0.05). The cooking loss of T2 was lower than the control and the other two treatments (p<0.05). The $L^*,\;a^*\;and\;b^*$ values of all treated samples were higher than those of the control during freezing storage (p<0.05). The W value of T3 at 1.5 and 3 months of freezing storage was higher than the control and T1 (p<0.05). The myoglobin and met-Mb contents of the control were similar to all treated samples, and the met-Mb content of the control and all treated samples increased with storage time (p<0.05). Immediately after freezing, the hardness of the control was higher than all treated samples, however it was lower after 1.5 and 3 months of frozen storage (p<0.05). The cohesiveness and gumminess of the control were higher than all treated samples immediately after freezing, however the values for T3 were higher than those of the control and the other two treatments during frozen storage for 1.5 and 3 months (p<0.05).
Keywords
cryoprotectants; physico-chemical characteristics; pH adjustment; chicken breast; surimi;
Citations & Related Records
Times Cited By KSCI : 8  (Citation Analysis)
Times Cited By Web Of Science : 1  (Related Records In Web of Science)
Times Cited By SCOPUS : 1
연도 인용수 순위
1 AOAC (1969) Official methods of analysis, 17th ed, Association of Official Methods of Analysis of AOAC International, Ch. 45 pp. 82
2 Baron, C. P., Skibsted, L. H., and Andersen, H. J. (2002) Concentration effects in myoglobin-catalyzed peroxidation of linoleate. J. Agric. Food Chem. 50, 883-888   DOI   ScienceOn
3 Jung, C. H., Kim, J. S., Jin, S. K., Kim, I. S., Jung, K. J., and Choi, Y. J. (2004) Gelation properties and industrial application of functional protein from fish muscle-2. Properties of functional protein gel from fish, chicken breast and pork leg and optimum formulation. Kor. J. Soc. Food Sci. Nutr. 33, 1676-1684   과학기술학회마을   DOI   ScienceOn
4 Lee, S. K., Min, B. J., and Kang, C. G. (2001b) Effects of oleoresin spices on the quality of chicken surimi during frozen storage. Korean J. Food Sci. Ani. Resour. 21, 292-299   과학기술학회마을
5 Mansfield, B. (2003) Fish, factory trawlers, and imitation crab: the nature of quality in the seafood industry. J. Rural Studies 19, 9-21   DOI   ScienceOn
6 SAS (1999) SAS/STAT Software for PC. Release 6.11, SAS Institute Inc., Cary, NC, USA
7 Suzuki, T. (1981) Frozen minced meat (Surimi). In: Fish and Krill Protein; Processing Technology. Appl. Sci. Pub., Ltd., London, UK, pp. 115-147
8 Woessner, J. F. (1961) The determination of hydroxyproline in tissue and protein samples containing small proportions of this amino acid. 119 Arch. Biochem. Biophys. 93, 440-447   DOI   ScienceOn
9 Lee, S. K., Min, B. J., and Kang, C. G. (2001a) Influence of propyl gallate, sodium ascorbate, and sodium tripolyphosphate on quality change of chicken surimi during storage. Kor. J. Anim. Sci. Technol. 43, 525-534
10 Park, S., Brewer, M. S., Mckeith, F. K., Bechtel, P. J., and Novakofski, J. (1996) Composition of surimi-like material from beef or pork. J. Food Sci. 61, 717-726   DOI   ScienceOn
11 Sych, J., Lacroix, C., Adambounou, L. T., and Castaigne, F. (1990) Cryoprotective effects of some materials on codsurimi proteins during frozen storage. J. Food Sci. 55, 1222-1227   DOI
12 Ryu, H. S., Lee, K. W., and Lee, K. H. (1994) Effects of processing conditions on nutrition qualities of seafood. 2. Effects of cryoprotectants on the protein qualities of pollock surimi. Bull. Kor. Fish. Soc. 27, 335-343
13 Park, J. D., Yoon, S. S., Jung, C. H., Cho, M. S., and Choi, Y. J. (2003) Effect of sarcoplasmic protein and NaCl on heating gel from fish muscle surimi prepared by acid and alkaline processing. Kor. J. Soc. Food Sci. 32, 567-573   과학기술학회마을   DOI   ScienceOn
14 Lan, Y. H., Novakofski, J., McCusker, R. H., Brewer, M. S., Carr, T. R., and McKeith, F. K. (1995) Thermal gelation properties of myofibrillar protein from pork, beef, fish, chicken and turkey muscles. J. Food Sci. 60, 936-940   DOI   ScienceOn
15 Jeong, J. Y., Yang, H. S., Kang, G H., Lee, J. I., Park, G. B., and Joo, S. T. (2006) Effect of freeze-thaw process on myoglobin oxidation of pork loin during cold storage. Korean J. Food Sci. Ani. Resour. 26, 1-8   과학기술학회마을
16 Lee, C. M. (1984) Surimi process technology. Food Technol. 38, 69-80
17 Rhee, M. S., Lee, J. S., Lee, S., Kim, B. C., and Koh, K. C. (1995) Effects of additives and ionic strength in preblends on the binding of pre-cooked restructured pork roasts. Kor. J. Anim. Sci. Technol. 37, 427-437
18 Park, K. H., Jin, S. K., Kim, I. S., Ha, J. H., Kang, S. M., Choi, Y. J., and Kim, J. S. (2005) Physico-chemical characteristics of surimi by washing method and pH control level of chopped chicken breast. Kor. J. Anim. Sci. Technol. 47, 1059-1066   DOI   ScienceOn
19 Sung, S. K., Yang, T. M., Kwon, Y. J., Choi, J. D., and Kim, D. G. (2000) The quality characteristics of Korean native chicken by the age. Kor. J. Anim. Sci. Technol. 42, 693-702
20 Park, J. W., Lanier, T. C., and Green, D. P. (1988) Cryoprotective effects of sugar, polyols, and/or phosphates on Alaska pollack surimi. J. Food Sci. 53, 1-3   DOI
21 Umemoto S. (1966) A modified methods for estimation of fish muscle protein by Biuret method. Bull. Jpn. Soc. Sci. Fish. 32, 427-435   DOI
22 AOAC (1990) Official method of analysis, 15th ed., Association of Official Analytical Chemists, Washington, DC
23 Chen, H. H. (2002) Decoloration and gel-forming ability of horse mackerel mince by air-flotation washing. J. Food Sci. 67, 2970-2975   DOI   ScienceOn
24 Livingston, D. J. and Brown, W. D. (1981) The chemistry of myoglobin and its reactions. Food Technol. 35, 244-250
25 Jin, S. K., Kim, I. S., Hur, S. J., Park, K. H., Ha, J. H., Kang, S. M., Choi, Y. J., and Kim, J. S. (2006) Effect of pH control on physico-chemical characteristics of chicken breast surimi. Korean J. Food Sci. Ani. Resour. 26, 64-69   과학기술학회마을
26 Ha, J. U. and Woo, D. K. (1997) Water holding capacity, cooking loss and gel characteristics of pork heart surimi prepared by washing under anti oxidative condition. Korean J. Food Sci. Ani. Resour. 17, 226-2317
27 Kawashima, T., Arai, K., and Saito, T. (1973) Studies on muscular proteins of fish. The amount of actomyosin in frozen 'surimi' from Alaska pollock. Bull. Jpn. Soc. Sci. Fish. 39, 525-532   DOI
28 Chae, H. S., Cho, S. H., Park, B. Y., Yoo, Y. M., Kim, J. H., Ahn, C. N., Lee, J. M., Kim, Y. K., and Choi, Y. I. (2002) Changes of the fatty acid, amino acid and collagen contents in domestic broiler chickens of different marketing standard. Korean J. Food Sci. Ani. Resour. 22, 1-7
29 Davis, G. W., Smith, G. C., Carpenter, Z. L., and Cross, H. R. (1974) Relationships of quality indicators to palatability attributes of pork loin. J. Anim. Sci. 41, 1305-1310
30 Park, J. W. and Laneir, T. C. (1987) Combined effects of phosphates and sugar or polyol on protein stabilization of fish myofibrils. J. Food Sci. 52, 1509-1513   DOI
31 Cho, H. J., Kang, S. G., Cha, Y. H., Kim, B. K., Woo, S. C., and Yeoh, Y. S. (2002) Effects of dietary ground, crumble and pellet of physico-chemical properties on broiler meat. Kor. J. Anim. Sci. Technol. 44, 585-592   DOI   ScienceOn
32 Sims, T. J. and Bailey, A. J. (1981) Connective tissue. In 'Development in meat science-2' ed. Lawrie R. A., Applied Sci. Pub
33 Livingston, D. J. and Brown, W. D. (1982) The chemistry of myoglobin and its reactions. Food Technol. 36, 240-252
34 Babbitt, J. K. and Reppond, K. D. (1988) Factors affecting the gel properties of surimi. J. Food Sci. 53, 965-972   DOI
35 Liu, H. P. (1970) Catalysts of lipid peroxidation in meats. 1. Linoleate peroxidation catalyzed by metmyoglobin or Fe(II)-EDTA. J. Food Sci. 35, 590-597
36 Yoon, K. S. and Lee, C. M. (1990) Cryoprotectant effects in surimi/mince-based extruded products. J. Food Sci. 55, 1210-1216   DOI
37 Antonomanolaki, R. E., Vareltzis, K. P., Georgakis, S. A., and Kaldrymidou, E. (1999) Thermal gelation properties of surimi-like material made from sheep meat. Meat Sci. 35, 429-435
38 Noguchi, S. and Matsumoto, J. J. (1970) Studies on the control of the denaturation of the fish muscle proteins during frozen storage-. Preventive effect of Na-glutamate. Bull. Jpn. Soc. Sci. Fish. 36, 1078-1087   DOI