Browse > Article

Effects of Hydrostatic Pressure Treatment on the Physicochemical, Morphological, and Textural Properties of Bovine Semitendinosus Muscle  

Kim, Yun-Ji (Division of Food Safety Research, Korea Food Research Institute)
Lee, Eun-Jung (Division of Food Safety Research, Korea Food Research Institute)
Lee, Nam-Hyouck (Division of Food Safety Research, Korea Food Research Institute)
Kim, Young-Ho (Division of Food Safety Research, Korea Food Research Institute)
Yamamoto, Katsuhiro (Department of Food Science, Rakuno Gakuen University)
Publication Information
Food Science and Biotechnology / v.16, no.1, 2007 , pp. 49-54 More about this Journal
Abstract
The effects of hydrostatic pressure (HP) treatment on the physicochemical, morphological, and textural properties of bovine semitendinosus (ST) muscle were assessed. Based on SDS-PAGE, the decrease in HP-treated ST muscle protein solubility in 0.1 M KCl buffer (pH 7.0) was attributable to a reduction in the levels of sarcoplasmic protein, and the protein solubility decrease observed in 0.6 M KCl buffer (PH 7.0) was attributable to a reduction in the levels of myosin heavy-chain and actin. Scanning electron microscope (SEM) observations showed that muscle fibers became finer and more compact with increasing pressures. The shear force and hardness of ST muscle pressurized to 300 MPa decreased significantly (p<0.05), however samples pressurized at 100 and 500 MPa exhibited a significant increase in both attributes relative to the control sample (p<0.05).
Keywords
hydrostatic pressure; bovine semitendinosus muscle; shear force; texture profile analysis; scanning electron microscope;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
Times Cited By Web Of Science : 8  (Related Records In Web of Science)
Times Cited By SCOPUS : 8
연도 인용수 순위
1 Davey CL, Kuttel H, Gibert KY. Shortening as a factor in meat aging. J. Food. Technol. 2: 53-56 (1967)   DOI
2 Koohmaraie M, Seideman SC, Schollmeyer JE, Dutson TR, Babiker AS. Factors associated with the tenderness of three bovine muscles. J. Food Sci. 53: 407-410 (1988)   DOI
3 Cheftel JC, Culioli J. Effects of high pressure on meat: a review. Meat Sci. 46: 211-236 (1997)   DOI   ScienceOn
4 Suzuki A, Suzuki N, lkeuchi Y, Saito M. Effects of high pressure treatment on the ultrastructure and solubilization of isolated myofibrils. Agr. Biol. Chem. Tokyo 55: 2467-2473 (1991)   DOI
5 Jung S, Ghoul M, De Lamballerie-Anton M. Changes in lysosoaml enzyme activities values of high pressure treared meat durong ageing. Meat Sci. 56: 239-246 (2000)   DOI   ScienceOn
6 Hong GP, Park SH, Kim JY, Lee SK, Min SG. Effects of time-dependent high pressure treatment on physico-chemical properties of pork. Food Sci. Biotechnol. 14: 808-812 (2005)
7 Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177: 751-766 (1949)
8 Jiang SZ, Hwang DC, Chen CS. Denaturation and change in SH group of actomyosin from milkfish (Chanos chanos) during storage at -$20^{\circ}C$. J. Agr. Food Chem. 36: 433-437 (1988)   DOI
9 Palka K. Roasting-induced changes in intramuscular connective tissue and tenderness of bovine semitendinosus muscle. Polish J. Food Nutr. Sci. 9/50: 41-45 (2000)
10 Bourne MC. Principles of objective texture measurement. pp 45-117. In: Food Texture and Viscosity: Concepts and Measurements. Stewart GF (ed). Academic Press, New York, NY, USA (1982)
11 Palka K, Daun H. Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating. Meat Sci. 51: 237-243 (1999)   DOI   ScienceOn
12 Suzuki A, Kim K, Homma N, Ikeuchi Y, Saito M. Acceleration of meat conditioning by high pressure treatment. pp. 219-227. In: High Pressure and Biotechnology. Balny C, Hayashi R, Heremans K, Masson P (eds). INSERM/John Libbey Eurotext Ltd., Montrouge, France (1992)
13 Macfarlane JJ, Mckenzie IJ, Turner RH. Pressure treatment of meat: effects on thermal transitions and shear values. Meat Sci. 5: 307-317 (1980)   DOI   ScienceOn
14 Fiske CH, Subbarow Y. The colorimetric determination of phosphorus. J. Biol, Chem. 66: 375-400 (1926)
15 Lee EJ, Kim YJ, Lee NH, Lin YH, Seo EJ, Yamamoto K. Effects of hydrostatic pressure on biochemical characteristics of myofibrillar protein extracted from bovine semitendinosus muscle. Food Sci. Biotechnol. 13: 632-635 (2004)
16 Lee RMKW. A critical appraisal of the effects f fixation dehydration and embedding on cell volume. pp. 61-70. In: Science of Biological Specimen Preparation. SEM Inc., AMF O'Hare, Chicago, IL, USA (1984)
17 Li-Chen E. Heat-induced changes in the proteins of whey protein concentrate. J. Food Sci. 48: 47-56 (1983)   DOI
18 Neuhoff V, Arold N, Taube D, Ehrhardt NM. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G250 and R-250. Electrophoresis 9: 255-262 (1988)   DOI   ScienceOn
19 Elgasim EA, Kennick WH. Effect of high pressure on meat microstructure. Food Microstruct. 1: 75-82 (1982)
20 Honikel KO. Reference methods for the assessment of physical characteristics of meat. Meat Sci. 49: 447-457 (1998)   DOI   ScienceOn
21 Hatae K, Yoshimatsu F, Matsumoto JJ. Discriminative characterization of different texture profiles of various cooked fish muscles. J. Food Sci. 49: 721-726 (1984)   DOI
22 Lee CM, Whiting RC, Jenkins RK. Texture and sensory evaluations of frankfurters made with different formulations and processes. J. Food Sci. 52: 896-900 (1987)   DOI
23 Yamamoto K, Hayashi S, Yasui T. Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCI at pH 6.0. Biosci. Biotech. Biochem. 57: 383-389 (1993)   DOI
24 SAS Institute, Inc. SAS User's Guide. Statistical Analysis Systems Institute, Cary, NC, USA (1996)
25 Queqiner C, Dumay E, Cavalier C, Cheftel JC. Reduction of Streptococcus thermophilus in a whey protein isolate by low moisture extrusion cooking without loss of functional properties. Int. J. Food Sci. Tech. 24: 601-602 (1989)   DOI   ScienceOn
26 Yamamoto K, Yoshida Y, Morita J, Yasui T. Morphological and physicochemical changes in the myosin molecules induced by hydrostatic pressure. J. Biochem. 116: 215-220 (1994)   DOI
27 Humphreys WJ, Spurlock BO, Johnson JS. Critical point drying of ethanol-infiltrated, cryofractured biological specimens for scanning electron microscopy. pp. 275-283. In: Scanning Electron Microscopy. Proceedings of the 7th Annual Scanning Electron Microscope Symposium. Johari O, Corbin I (ed). IIT Research Institute, Chicago, IL, USA (1974)
28 Takahashi K. Structural weakening of skeletal muscle tissue during post mortem ageing of meat: the non-emzymatic mechanism of meat tenderization. Meat Sci. 43: S67-S80 (1996)   DOI
29 Locker RH, Wild DJC. Tenderisation of meat by pressure-heat involves weakening of the gapfilament in the myofibril. Meat Sci. 10: 207-233 (1984)   DOI   ScienceOn
30 Lawmmli VK. Cleavage of structural proteins during the head of bacteriophage T4. Nature 227: 680-685 (1970)   DOI   ScienceOn
31 Bourne MC. Texture profile analysis. Food Technol.-Chicago 32: 62-66 (1978)