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Volumn 19, Issue 1, 2008, Pages 74-97

Effect of hydrodynamic pressure processing and aging on the tenderness and myofibrillar proteins of beef strip loins

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EID: 38049108196     PISSN: 10460756     EISSN: 17454573     Source Type: Journal    
DOI: 10.1111/j.1745-4573.2007.00101.x     Document Type: Article
Times cited : (42)

References (54)
  • 2
    • 0002204426 scopus 로고
    • An immunological method to assess protein degradation in post-mortem muscle
    • BANDMAN, E. ZDANIS, D. 1988. An immunological method to assess protein degradation in post-mortem muscle. Meat Sci. 22, 1 19.
    • (1988) Meat Sci. , vol.22 , pp. 1-19
    • Bandman, E.1    Zdanis, D.2
  • 4
    • 33846510446 scopus 로고    scopus 로고
    • Effects of hydrodynamic pressure processing and blade tenderization on intramuscular collagen and tenderness-related protein characteristics of top rounds from Brahman cattle
    • BOWKER, B.C., LIU, M.N., SOLOMON, M.B., EASTRIDGE, J.S., FAHRENHOLZ, T.M. VINYARD, B. 2007. Effects of hydrodynamic pressure processing and blade tenderization on intramuscular collagen and tenderness-related protein characteristics of top rounds from Brahman cattle. J. Muscle Foods 18, 35 55.
    • (2007) J. Muscle Foods , vol.18 , pp. 35-55
    • Bowker, B.C.1    Liu, M.N.2    Solomon, M.B.3    Eastridge, J.S.4    Fahrenholz, T.M.5    Vinyard, B.6
  • 5
    • 0025329214 scopus 로고
    • Transitions from fetal to fast troponin-T isoforms in developing rabbit skeletal muscle
    • BRIGGS, M.M., MCGINNIS, H.D. SCHACHAT, F. 1990. Transitions from fetal to fast troponin-T isoforms in developing rabbit skeletal muscle. Dev. Biol. 140, 253 260.
    • (1990) Dev. Biol. , vol.140 , pp. 253-260
    • Briggs, M.M.1    McGinnis, H.D.2    Schachat, F.3
  • 7
    • 0035589779 scopus 로고    scopus 로고
    • Hydrodynamic shock wave tenderization effects using a cylinder processor on early deboned broiler breasts
    • CLAUS, J.R., SCHILLING, J.K., MARRIOTT, N.G., DUNCAN, S.E., SOLOMON, M.B. WANG, H. 2001. Hydrodynamic shock wave tenderization effects using a cylinder processor on early deboned broiler breasts. Meat Sci. 58, 287 292.
    • (2001) Meat Sci. , vol.58 , pp. 287-292
    • Claus, J.R.1    Schilling, J.K.2    Marriott, N.G.3    Duncan, S.E.4    Solomon, M.B.5    Wang, H.6
  • 8
    • 84985162754 scopus 로고
    • Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle
    • CULLER, R.D., PARRISH, F.C., SMITH, G.C. CROSS, H.R. 1978. Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle. J. Food Sci. 43, 1177 1180.
    • (1978) J. Food Sci. , vol.43 , pp. 1177-1180
    • Culler, R.D.1    Parrish, F.C.2    Smith, G.C.3    Cross, H.R.4
  • 9
    • 84986535324 scopus 로고
    • Studies in meat tenderness. 8. Ultra-structural changes in meat during aging
    • DAVEY, C.L. DICKSON, M.R. 1970. Studies in meat tenderness. 8. Ultra-structural changes in meat during aging. J. Food Sci. 35, 56 60.
    • (1970) J. Food Sci. , vol.35 , pp. 56-60
    • Davey, C.L.1    Dickson, M.R.2
  • 10
    • 0002565004 scopus 로고
    • Effect of high hydrostatic pressure on meat microstructure
    • ELGASIM, E.A. KENNICK, W.H. 1982. Effect of high hydrostatic pressure on meat microstructure. Food Microstructure 1, 75 82.
    • (1982) Food Microstructure , vol.1 , pp. 75-82
    • Elgasim, E.A.1    Kennick, W.H.2
  • 11
    • 84985294913 scopus 로고
    • Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy
    • FRITZ, J.D. GREASER, M.L. 1991. Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy. J. Food Sci. 56, 607 610.
    • (1991) J. Food Sci. , vol.56 , pp. 607-610
    • Fritz, J.D.1    Greaser, M.L.2
  • 12
    • 0001741477 scopus 로고
    • Separation of subcellular organelles in differential and density gradient centrifugation
    • In. pp., American Meat Science Association, Chicago, IL.
    • GOLL, D.E., YOUNG, R.B. STROMER, M.H. 1974. Separation of subcellular organelles in differential and density gradient centrifugation. In Proceedings of 27th Reciprocal Meat Conference, pp. 250 290, American Meat Science Association, Chicago, IL.
    • (1974) Proceedings of 27th Reciprocal Meat Conference , pp. 250-290
    • Goll, D.E.1    Young, R.B.2    Stromer, M.H.3
  • 13
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • GORNALL, A.G., BARDAWILL, C.J. DAVID, M.M. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751 766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 14
    • 0028126638 scopus 로고
    • Identification of the 30 kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T
    • HO, C.Y., STROMER, M.H. ROBSON, R.M. 1994. Identification of the 30 kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T. Biochimie 76, 369 375.
    • (1994) Biochimie , vol.76 , pp. 369-375
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 15
    • 0030183591 scopus 로고    scopus 로고
    • Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle
    • HO, C.Y., STROMER, M.H. ROBSON, R.M. 1996. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. J. Anim. Sci. 74, 1563 1575.
    • (1996) J. Anim. Sci. , vol.74 , pp. 1563-1575
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 16
    • 21844495511 scopus 로고
    • Levels of calpain and calpastatin in meat subjected to high pressure
    • HOMMA, N., IKEUCHI, Y. SUZUKI, A. 1995. Levels of calpain and calpastatin in meat subjected to high pressure. Meat Sci. 41, 251 260.
    • (1995) Meat Sci. , vol.41 , pp. 251-260
    • Homma, N.1    Ikeuchi, Y.2    Suzuki, A.3
  • 17
    • 0034421985 scopus 로고    scopus 로고
    • A research note on factors affecting the determination of myofibrillar fragmentation
    • HOPKINS, D.L., LITTLEFIELD, P.J. THOMPSON, J.M. 2000. A research note on factors affecting the determination of myofibrillar fragmentation. Meat Sci. 56, 19 22.
    • (2000) Meat Sci. , vol.56 , pp. 19-22
    • Hopkins, D.L.1    Littlefield, P.J.2    Thompson, J.M.3
  • 18
    • 0029285632 scopus 로고
    • Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle
    • HUFF-LONERGAN, E., PARRISH, F.C. ROBSON, R.M. 1995. Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Anim. Sci. 73, 1064 1073.
    • (1995) J. Anim. Sci. , vol.73 , pp. 1064-1073
    • Huff-Lonergan, E.1    Parrish, F.C.2    Robson, R.M.3
  • 19
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle
    • HUFF-LONERGAN, E., MITSUHASHI, T., BEEKMAN, D.D., PARRISH, F.C., OLSON, D.G. ROBSON, R.M. 1996. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci. 74, 993 1008.
    • (1996) J. Anim. Sci. , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish, F.C.4    Olson, D.G.5    Robson, R.M.6
  • 20
    • 0029692222 scopus 로고    scopus 로고
    • Effect of beef tenderness on consumer satisfaction with steaks consumed in the home and restaurant
    • HUFFMAN, K.L., MILLER, M.F., HOOVER, L.C., WU, C.K., BRITTIN, H.C. RAMSEY, C.B. 1996. Effect of beef tenderness on consumer satisfaction with steaks consumed in the home and restaurant. J. Anim. Sci. 74, 91 97.
    • (1996) J. Anim. Sci. , vol.74 , pp. 91-97
    • Huffman, K.L.1    Miller, M.F.2    Hoover, L.C.3    Wu, C.K.4    Brittin, H.C.5    Ramsey, C.B.6
  • 21
    • 84987369453 scopus 로고
    • Studies of desmin and α-actinin degradation in bovine semitendinosus muscle
    • HWAN, S. BANDMAN, E. 1989. Studies of desmin and α-actinin degradation in bovine semitendinosus muscle. J. Food Sci. 54, 1426 1430.
    • (1989) J. Food Sci. , vol.54 , pp. 1426-1430
    • Hwan, S.1    Bandman, E.2
  • 22
    • 84987286270 scopus 로고
    • A research note: Effect of postmortem storage on cold-shortened bovine muscle: Analysis by SDS-polyacrylamide gel electrophoresis
    • KOOHMARAIE, M., KENNICK, W.H., ANGLEMIER, A.F., ELGASIM, E.A. JONES, T.K. 1984a. A research note: Effect of postmortem storage on cold-shortened bovine muscle: Analysis by SDS-polyacrylamide gel electrophoresis. J. Food Sci. 49, 290 291.
    • (1984) J. Food Sci. , vol.49 , pp. 290-291
    • Koohmaraie, M.1    Kennick, W.H.2    Anglemier, A.F.3    Elgasim, E.A.4    Jones, T.K.5
  • 23
    • 84985264947 scopus 로고
    • Effect of prerigor pressurization on the activity of calcium-activated factor
    • KOOHMARAIE, M., KENNICK, W.H., ELGASIM, E.A. ANGLEMIER, A.F. 1984b. Effect of prerigor pressurization on the activity of calcium-activated factor. J. Food Sci. 49, 680 684.
    • (1984) J. Food Sci. , vol.49 , pp. 680-684
    • Koohmaraie, M.1    Kennick, W.H.2    Elgasim, E.A.3    Anglemier, A.F.4
  • 24
  • 25
    • 0030330032 scopus 로고    scopus 로고
    • Meat toughening does not occur when rigor shortening is prevented
    • KOOHMARAIE, M., DOUMIT, M.E. WHEELER, T.L. 1996. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci. 74, 2935 2942.
    • (1996) J. Anim. Sci. , vol.74 , pp. 2935-2942
    • Koohmaraie, M.1    Doumit, M.E.2    Wheeler, T.L.3
  • 26
    • 33645143089 scopus 로고    scopus 로고
    • Use of hydrodynamic pressure processing and blade tenderization to tenderize top rounds from Brahman cattle
    • LIU, M.N., SOLOMON, M.B., VINYARD, B., CALLAHAN, J.A., PATEL, J.R., WEST, R.L. CHASE, C.C. 2006. Use of hydrodynamic pressure processing and blade tenderization to tenderize top rounds from Brahman cattle. J. Muscle Foods 17, 79 91.
    • (2006) J. Muscle Foods , vol.17 , pp. 79-91
    • Liu, M.N.1    Solomon, M.B.2    Vinyard, B.3    Callahan, J.A.4    Patel, J.R.5    West, R.L.6    Chase, C.C.7
  • 27
    • 84982342895 scopus 로고    scopus 로고
    • Degree of muscular contraction as a factor in tenderness of beef
    • LOCKER, R.H. Degree of muscular contraction as a factor in tenderness of beef. Food Res. 25, 304 307.
    • Food Res. , vol.25 , pp. 304-307
    • Locker, R.H.1
  • 28
    • 84987313519 scopus 로고
    • The 30,000-dalton component of tender bovine longissimus muscle
    • MACBRIDE, M.A. PARRISH, F.C. 1977. The 30,000-dalton component of tender bovine longissimus muscle. J. Food Sci. 42, 1627 1629.
    • (1977) J. Food Sci. , vol.42 , pp. 1627-1629
    • MacBride, M.A.1    Parrish, F.C.2
  • 29
    • 84987333722 scopus 로고
    • Pressure-induced solubilization of meat proteins in saline solution
    • MACFARLANE, J.J. 1974. Pressure-induced solubilization of meat proteins in saline solution. J. Food Sci. 39, 542 547.
    • (1974) J. Food Sci. , vol.39 , pp. 542-547
    • MacFarlane, J.J.1
  • 30
    • 84985095067 scopus 로고
    • Pressure-induced solubilization of myofibrillar proteins
    • MACFARLANE, J.J. MCKENZIE, I.J. 1976. Pressure-induced solubilization of myofibrillar proteins. J. Food Sci. 41, 1442 1446.
    • (1976) J. Food Sci. , vol.41 , pp. 1442-1446
    • MacFarlane, J.J.1    McKenzie, I.J.2
  • 31
    • 0028075228 scopus 로고
    • Role of regulatory proteins (troponin-tropomyosin) in pathologic states
    • MALHOTRA, A. 1994. Role of regulatory proteins (troponin-tropomyosin) in pathologic states. Mol. Cell. Biochem. 135, 43 50.
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 43-50
    • Malhotra, A.1
  • 32
    • 0035535581 scopus 로고    scopus 로고
    • Studies of cow beef tenderness enhancement through supersonic- hydrodynamic shock wave treatment
    • MARRIOTT, N.G., WANG, H., SOLOMON, M.B. MOODY, W.G. 2001. Studies of cow beef tenderness enhancement through supersonic-hydrodynamic shock wave treatment. J. Muscle Foods 12, 207 218.
    • (2001) J. Muscle Foods , vol.12 , pp. 207-218
    • Marriott, N.G.1    Wang, H.2    Solomon, M.B.3    Moody, W.G.4
  • 33
    • 84981851390 scopus 로고
    • Studies in meat tenderness. III. the effects of cold shortening on tenderness
    • MARSH, B.B. LEET, N.G. 1966. Studies in meat tenderness. III. The effects of cold shortening on tenderness. J. Food Sci. 31, 450 459.
    • (1966) J. Food Sci. , vol.31 , pp. 450-459
    • Marsh, B.B.1    Leet, N.G.2
  • 35
    • 0033173501 scopus 로고    scopus 로고
    • Impact of the Hydrodyne process on tenderness, microbial load, and sensory characteristics of pork longissimus muscle
    • MOELLER, S., WULF, D., MEEKER, D., NDIFE, M., SUNDARARAJAN, N. SOLOMON, M.B. 1999. Impact of the Hydrodyne process on tenderness, microbial load, and sensory characteristics of pork longissimus muscle. J. Anim. Sci. 77, 2119 2123.
    • (1999) J. Anim. Sci. , vol.77 , pp. 2119-2123
    • Moeller, S.1    Wulf, D.2    Meeker, D.3    Ndife, M.4    Sundararajan, N.5    Solomon, M.B.6
  • 36
    • 0942300430 scopus 로고    scopus 로고
    • N-terminal amino acid sequences of troponin T fragments, including 30 kDa one, produced during postmortem aging of bovine longissimus muscle
    • MUROYA, S., KITAMURA, S., TANABE, S., NISHIMURA, T., NAKAJIMA, I. CHIKUNI, K. 2004. N-terminal amino acid sequences of troponin T fragments, including 30 kDa one, produced during postmortem aging of bovine longissimus muscle. Meat Sci. 67, 19 24.
    • (2004) Meat Sci. , vol.67 , pp. 19-24
    • Muroya, S.1    Kitamura, S.2    Tanabe, S.3    Nishimura, T.4    Nakajima, I.5    Chikuni, K.6
  • 37
    • 0031286262 scopus 로고    scopus 로고
    • The relationship between early postmortem pH and the tenderization of beef muscles
    • O'HALLORAN, G.R., TROY, D.J. BUCKLEY, D.J. 1997. The relationship between early postmortem pH and the tenderization of beef muscles. Meat Sci. 45, 239 251.
    • (1997) Meat Sci. , vol.45 , pp. 239-251
    • O'Halloran, G.R.1    Troy, D.J.2    Buckley, D.J.3
  • 38
    • 84985046283 scopus 로고
    • Effect of postmortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle
    • OLSON, D.G., PARRISH, F.C., DAYTON, W.R. GOLL, D.E. 1977. Effect of postmortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle. J. Food Sci. 42, 117 124.
    • (1977) J. Food Sci. , vol.42 , pp. 117-124
    • Olson, D.G.1    Parrish, F.C.2    Dayton, W.R.3    Goll, D.E.4
  • 39
    • 0000852182 scopus 로고
    • Relationship between toughness and troponin-T in conditioned beef
    • PENNY, I.F. DRANSFIELD, E. 1979. Relationship between toughness and troponin-T in conditioned beef. Meat Sci. 3, 135 141.
    • (1979) Meat Sci. , vol.3 , pp. 135-141
    • Penny, I.F.1    Dransfield, E.2
  • 41
    • 0012813607 scopus 로고
    • A research note: Comparison of methods for measuring pH in muscle tissue
    • SOLOMON, M.B. 1987. A research note: Comparison of methods for measuring pH in muscle tissue. J. Food Sci. 52, 1428 1429.
    • (1987) J. Food Sci. , vol.52 , pp. 1428-1429
    • Solomon, M.B.1
  • 42
    • 0031156957 scopus 로고    scopus 로고
    • The Hydrodyne: A new process to improve beef tenderness
    • SOLOMON, M.B., LONG, J.B. EASTRIDGE, J.S. 1997. The Hydrodyne: A new process to improve beef tenderness. J. Anim. Sci. 75, 1534 1537.
    • (1997) J. Anim. Sci. , vol.75 , pp. 1534-1537
    • Solomon, M.B.1    Long, J.B.2    Eastridge, J.S.3
  • 43
    • 0032222137 scopus 로고    scopus 로고
    • Tenderizing callipyge lamb with the Hydrodyne process and electrical stimulation
    • SOLOMON, M.B., CARPENTER, C.E., SNOWDER, G.D. COCKETT, N.E. 1998. Tenderizing callipyge lamb with the Hydrodyne process and electrical stimulation. J. Muscle Foods 9, 305 311.
    • (1998) J. Muscle Foods , vol.9 , pp. 305-311
    • Solomon, M.B.1    Carpenter, C.E.2    Snowder, G.D.3    Cockett, N.E.4
  • 45
    • 85010743671 scopus 로고    scopus 로고
    • Hydrodynamic pressure processing to improve meat quality and safety
    • In. L.M.L. Nollet. F. Toldra, eds.) pp.-219. CRC Press Taylor & Francis Group, Boca Raton, FL.
    • SOLOMON, M.B., LIU, M.N., PATEL, J.R., BOWKER, B.C. SHARMA, M. 2006. Hydrodynamic pressure processing to improve meat quality and safety. In Advanced Technologies for Meat Processing (L.M.L. Nollet F. Toldra, eds.) pp. 219 244, CRC Press Taylor & Francis Group, Boca Raton, FL.
    • (2006) Advanced Technologies for Meat Processing , pp. 244
    • Solomon, M.B.1    Liu, M.N.2    Patel, J.R.3    Bowker, B.C.4    Sharma, M.5
  • 46
    • 0034393490 scopus 로고    scopus 로고
    • A potential index for assessing the tenderness of hydrodynamic pressure (HDP)-treated beef strip loins
    • SPANIER, A.M. ROMANOWSKI, R.D. 2000. A potential index for assessing the tenderness of hydrodynamic pressure (HDP)-treated beef strip loins. Meat Sci. 56, 193 202.
    • (2000) Meat Sci. , vol.56 , pp. 193-202
    • Spanier, A.M.1    Romanowski, R.D.2
  • 47
    • 0000092392 scopus 로고
    • Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle
    • SUZUKI, A., WATANABE, M., IWAMURA, K., IKEUCHI, Y. SAITO, M. 1990. Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle. Agric. Biol. Chem. 54, 3085 3091.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 3085-3091
    • Suzuki, A.1    Watanabe, M.2    Iwamura, K.3    Ikeuchi, Y.4    Saito, M.5
  • 49
    • 0026550071 scopus 로고
    • The effect of electrical stimulation on beef tenderness, protease activity and myofibrillar protein fragmentation
    • UYTTERHAEGEN, L., CLAEYS, E. DEMEYER, D. 1992. The effect of electrical stimulation on beef tenderness, protease activity and myofibrillar protein fragmentation. Biochimie 74, 275 281.
    • (1992) Biochimie , vol.74 , pp. 275-281
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 50
    • 0028435234 scopus 로고
    • Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility
    • UYTTERHAEGEN, L., CLAEYS, E. DEMEYER, D. 1994. Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility. J. Anim. Sci. 72, 1209 1223.
    • (1994) J. Anim. Sci. , vol.72 , pp. 1209-1223
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 51
    • 0028432852 scopus 로고
    • Prerigor and postrigor changes in tenderness of bovine longissimus muscle
    • WHEELER, T.L. KOOHMARAIE, M. 1994. Prerigor and postrigor changes in tenderness of bovine longissimus muscle. J. Anim. Sci. 72, 1232 1238.
    • (1994) J. Anim. Sci. , vol.72 , pp. 1232-1238
    • Wheeler, T.L.1    Koohmaraie, M.2
  • 52
    • 0025654863 scopus 로고
    • Predicting beef-longissimus tenderness from various biochemical and histological muscle traits
    • WHIPPLE, G., KOOHMARAIE, M., DIKEMAN, M.E. CROUSE, J.D. 1990. Predicting beef-longissimus tenderness from various biochemical and histological muscle traits. J. Anim. Sci. 68, 4193 4199.
    • (1990) J. Anim. Sci. , vol.68 , pp. 4193-4199
    • Whipple, G.1    Koohmaraie, M.2    Dikeman, M.E.3    Crouse, J.D.4
  • 53
    • 0000231513 scopus 로고
    • Effect of temperature and pH on the postmortem degradation of myofibrillar proteins
    • YATES, L.D., DUTSON, T.R., CALDWELL, J. CARPENTER, Z.L. 1983. Effect of temperature and pH on the postmortem degradation of myofibrillar proteins. Meat Sci. 9, 157 179.
    • (1983) Meat Sci. , vol.9 , pp. 157-179
    • Yates, L.D.1    Dutson, T.R.2    Caldwell, J.3    Carpenter, Z.L.4
  • 54
    • 0032194918 scopus 로고    scopus 로고
    • Ultrastructural changes in bovine longissimus muscle caused by the Hydrodyne process
    • ZUCKERMAN, H. SOLOMON, M.B. 1998. Ultrastructural changes in bovine longissimus muscle caused by the Hydrodyne process. J. Muscle Foods 9, 419 426.
    • (1998) J. Muscle Foods , vol.9 , pp. 419-426
    • Zuckerman, H.1    Solomon, M.B.2


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