Hostname: page-component-848d4c4894-jbqgn Total loading time: 0 Render date: 2024-07-04T05:33:21.498Z Has data issue: false hasContentIssue false

Different rates of glycolysis affect glycolytic activities and protein properties in turkey breast muscle

Published online by Cambridge University Press:  15 October 2008

S. Eadmusik
Affiliation:
INRA, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France Université de Toulouse, INPT-ENSAT, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France ENVT, UMR 1289 TANDEM, F-31076 Toulouse, France
C. Molette*
Affiliation:
INRA, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France Université de Toulouse, INPT-ENSAT, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France ENVT, UMR 1289 TANDEM, F-31076 Toulouse, France
H. Rémignon
Affiliation:
INRA, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France Université de Toulouse, INPT-ENSAT, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France ENVT, UMR 1289 TANDEM, F-31076 Toulouse, France
X. Fernandez
Affiliation:
INRA, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France Université de Toulouse, INPT-ENSAT, UMR 1289 TANDEM, F-31326 Castanet-Tolosan, France ENVT, UMR 1289 TANDEM, F-31076 Toulouse, France
*
Get access

Abstract

Protein alterations of turkey breast muscles (Pectoralis major) were investigated at 20 min and 24 h post mortem. Specific activities, quantities and kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and aldolase A were also determined at 20 min post mortem. Based on the pH values at 20 min post mortem, two groups of samples were classified as rapid glycolysis group (RG; pH20 min = 5.80 ± 0.07, n = 20) and normal glycolysis group (NG; pH20 min = 6.21 ± 0.01, n = 20). RG had lower specific activities of GAPDH and aldolase A than NG while Vm and Km values of both enzymes were not different between groups. RG showed lower high ionic strength (HIS) and pellet protein extractabilities at 20 min post mortem. It also had lower low ionic strength (LIS) and HIS protein extractabilities at 24 h post mortem. Besides pellet protein, muscular protein extractabilities at 24 h post mortem were higher than at 20 min post mortem. From SDS-PAGE of samples at 24 h post mortem, RG exhibited lower band intensities at 45 and 200 kDa, which were further identified as actin and myosin heavy chain (MHC), respectively. Western blots revealed that relative amounts of actin and MHC at 20 min post mortem were not different between groups. However, RG muscles had less relative amount of actin at 24 h post mortem. It also indicated that amounts of actin and MHC increased with regard to post mortem time.

Type
Full Paper
Copyright
Copyright © The Animal Consortium 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Barbut, S 1993. Colour measurements for evaluating the pale soft exudative (PSE) occurrence in turkey meat. Food Research International 26, 3943.CrossRefGoogle Scholar
Barbut, S, Zhang, L, Marcone, M 2005. Effect of pale, normal and dark chicken breast meat on microstructure, extractable protein and cooking of marinated fillets. Poultry Science 84, 797802.CrossRefGoogle ScholarPubMed
Boles, JA, Parrish, FC Jr, Huiatt, TW, Robson, RM 1992. Effect of porcine stress syndrome on the solubility and degradation of myofibrillar/cytoskeletal proteins. Journal of Animal Science 70, 454464.CrossRefGoogle ScholarPubMed
Borderies, G, Jamet, E, Lafite, C, Rossignol, M, Jauneau, A, Boudart, G, Montsarrat, B, Esquerré-Tugayé, E, Boudet, A, Pont-Lezica, R 2003. Proteomics of loosely bound cell wall proteins of Arabidopsis thaliana cell suspension cultures: a critical analysis. Electrophoresis 24, 34213432.CrossRefGoogle ScholarPubMed
Bowker, BC, Grant, AL, Forrest, JC, Gerrard, DE 2000. Muscle metabolism and PSE pork. Journal of Animal Science 79, 18.CrossRefGoogle Scholar
Chiang, W, Allison, CP, Linz, JE, Strasburg, GM 2004. Identification of two RYR alleles and characterization of RYR transcript variants in turkey skeletal muscle. Gene 330, 177184.Google Scholar
Choi, YM, Ryu, YC, Kim, BC 2007. Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality. Meat Science 76, 281288.CrossRefGoogle ScholarPubMed
Crow, VL, Wittenberger, CL 1979. Separation and properties of NAD+ and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans. Journal of Biological Chemistry 254, 11341142.CrossRefGoogle ScholarPubMed
Dziewulska-Szwajkowska, D, Zmojdzian, M, Dobryszycki, P, Kochman, M, Dzugaj, A 2004. The interaction of FBPase with aldolase: a kinetic and fluorescence investigation on chicken muscle enzymes. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 137, 115129.CrossRefGoogle ScholarPubMed
Fujii, J, Otsu, K, Zorzato, F, de Leon, S, Khanna, VK, Weiler, JE, O’Brien, PJ, Mac Lennan, DH 1991. Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science 253, 448451.CrossRefGoogle ScholarPubMed
Gil, M, Hortos, M, Sarraga, C 1998. Calpain and cathepsin activities and protein extractability during ageing of longissimus porcine muscle from normal and PSE meat. Food Chemistry 63, 385390.CrossRefGoogle Scholar
Jeacocke, RE 1977. The temperature dependence of anaerobic glycolysis in beef muscle held in a linear temperature gradient. Journal of the Science of Food and Agriculture 28, 551556.CrossRefGoogle Scholar
Joo, ST, Kauffman, RJ, Kim, BC, Park, GB 1999. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Science 52, 291297.CrossRefGoogle ScholarPubMed
Kijowski, J 2001. Muscle proteins. In Chemical and functional properties of food proteins (ed. ZE Sikorski), pp. 233269. Technomic Publishing Company, Inc., Lancaster, PA, USA.Google Scholar
Koeck, T, Levison, B, Hazen, SL, Crabb, JW, STuehr, DJ, Aulak, KS 2004. Tyrosine nitration impairs mammalian aldolase A activity. Molecular and Cellular Proteomics 3, 548557.CrossRefGoogle ScholarPubMed
Laemmli, UK 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.CrossRefGoogle ScholarPubMed
Lametsch, R, Karisson, A, Rosenvold, K, Andersen, HJ, Roepstorff, P, Bendixen, E 2003. Postmortem proteome changes of porcine muscle related to tenderness. Journal of Agriculture and Food Chemistry 51, 69926997.CrossRefGoogle ScholarPubMed
Livisay, SA, Xiong, YL, Moody, WG 1996. Proteolytic activity and calcium effect in dark-firm-dry and pale-soft-exudative meat. Lebensmittel-Wissenschaft und-Technologie 29, 123128.CrossRefGoogle Scholar
Lovell, SJ, Knight, PJ, Harrington, WF 1981. Fraction of myosin heads bound to thin filaments in rigor myofibrils from insect flight and vertebrate muscles. Nature 293, 664666.CrossRefGoogle Scholar
Lyon, CE, Buhr, RJ 1999. Biochemical basis of meat texture. In Poultry meat science (ed. RI Richardson and CG Mead), pp. 99126. CAB International Publishing, London, UK.Google Scholar
Ma, RT-I, Addis, PB 1973. The association of struggle during exsanguination to glycolysis, protein solubility and shear in turkey Pectoralis muscle. Journal of Food Science 38, 995997.CrossRefGoogle Scholar
MacGregor, JS, Singh, VN, Davoust, S, Melloni, E, Pontremoli, S, Horecker, BL 1980. Evidence for formation of a rabbit liver aldolase-rabbit liver fructose 1,6 bisphosphatase complex. Proceedings of the National Academy of Sciences of the United States of America 77, 38893892.CrossRefGoogle ScholarPubMed
McKee, SR, Sams, AR 1997. The effect of seasonal heat stress on rigor development and the incidence of pale exudative turkey meat. Poultry Science 76, 16161620.CrossRefGoogle ScholarPubMed
Maurady, A, Zdanov, A, de Moissac, D, Beaudry, D, Sygusch, J 2002. A conserved glutamate residue exhibits multifunctional catalytic roles in d-fructose-1,6-bisphosphate aldolases. Journal of Biological Chemistry 277, 94749483.CrossRefGoogle ScholarPubMed
Molette, C, Rémignon, H, Babilé, R 2005. Modification of glycolyzing enzymes lowers meat quality. Poultry Science 84, 119127.CrossRefGoogle ScholarPubMed
Mullen, AM, Stapleton, PC, Corcoran, D, Hamill, RM, White, A 2006. Understanding meat quality through the application of genomic and proteomic approaches. Meat Science 74, 316.CrossRefGoogle ScholarPubMed
Offer, G 1991. Modelling of the formation of pale, soft and exudative meat: effect of chilling regime and rate and extent of glycolysis. Meat Science 30, 157184.CrossRefGoogle ScholarPubMed
O’Reilly, G, Clarke, F 1993. Identification of an actin binding region in aldolase. FEBS Letters 321, 6972.CrossRefGoogle ScholarPubMed
Owens, CM, Hirschler, EM, McKee, SR, Martinez-Dawson, R, Sams, AR 2000. The characterization and incidence of pale, soft, exudative turkey meat in a commercial plant. Poultry Science 79, 553558.CrossRefGoogle Scholar
Pietrzak, M, Greaser, ML, Sosnicki, AA 1997. Effect of rapid rigor mortis processes on protein functionality in Pectoralis major muscle of domestic turkeys. Journal of Animal Science 75, 21062116.CrossRefGoogle ScholarPubMed
Rakus, D, Mamczur, P, Gizak, A, Dus, D, Dzugaj, A 2003. Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line. Biochemical and Biophysical Research Communication 311, 294299.CrossRefGoogle ScholarPubMed
Rathgeber, BM, Boles, JA, Shand, PJ 1999a. Rapid post mortem pH decline and delayed chilling reduce quality of turkey breast meat. Poultry Science 78, 477484.CrossRefGoogle Scholar
Rathgeber, BM, Pato, MD, Boles, JA, Shand, PJ 1999b. Rapid post mortem glycolysis and delay chilling of turkey carcasses cause alterations to protein extractability and degradation of breast muscle proteins. Journal of Agriculture and Food Chemistry 47, 25292536.CrossRefGoogle ScholarPubMed
Rosenvold, K, Andersen, HJ 2003. Factors of significance for pork quality – a review. Meat Science 64, 219237.CrossRefGoogle ScholarPubMed
Ryu, YC, Choi, YM, Kim, BC 2005. Variations in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates. Meat Science 71, 522529.CrossRefGoogle ScholarPubMed
Statistical Analysis Systems Institute 1989. SAS user’s guide for personal computers, release 6.3. SAS Institute Inc., Cary, NC.Google Scholar
Scheffler, TL, Gerrard, DE 2007. Mechanisms controlling pork quality development: the biochemistry controlling postmortem energy metabolism. Meat Science 77, 716.CrossRefGoogle ScholarPubMed
Towbin, H, Staehelin, T, Gordon, J 1979. Electrophoresis transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 76, 43504354.CrossRefGoogle ScholarPubMed
Warner, RD, Kauffman, RG, Greaser, ML 1997. Muscle protein changes post mortem in relation to pork quality traits. Meat Science 45, 339352.CrossRefGoogle ScholarPubMed