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2016 | 72 | 07 |

Tytuł artykułu

Wpływ procesu poubojowego dojrzewania mięsa wieprzowego na zmiany profilu białek i kruchość

Warianty tytułu

EN
Impact of post mortem aging of pork on changes in the isoelectric point of the proteins and tenderness

Języki publikacji

PL

Abstrakty

EN
The aim of the study was to evaluate the post mortem proteolysis of centrifugal drip protein derived from pork. The varied course of the process of meat tenderization in muscles using the isoelectric focusing (IEF) technique was observed. The experimental material was the longissimus lumborum et thoracis muscle excised from 24 pigs of known origin, breeding and rearing conditions. Meat of normal quality (RFN) was examined in this study. On the basis of shear force values, the experimental muscles were divided into 4 groups of different courses of tenderization: A – meat remaining tough during the entire 6-day period of post-slaughter changes; B – meat characterized by a typical tenderization process, i.e. tough 48 h after slaughter and tender after 6 days of storage; C – tender or relatively tender meat on both dates of examination; D – meat which was the toughest 48 hours after slaughter and the most tender 144 hours after slaughter. Proteins for electrophoretic analysis on the agarose gel of the centrifugal drip fraction were submitted after 48 h and 144 h post mortem. The separation of the proteins was performed in a horizontal layout, using an FBE-3000 apparatus and an ECPS power pack (Pharmacia). On every path of the proteins separation, four ranges of pH value were evaluated, namely: 4.0 ÷ 6.0 pI, 6.1 ÷ 7.2 pI, 7.3 ÷ 7.7 pI and > 7.7 pI. Meat tenderness on the second day after slaughter was influenced by proteins, in which their pI was in the range of 6.1 ÷ 7.2 and 4.0 ÷ 6.0. From the evaluation which was carried out in the immunoblotting analysis of proteins using troponin T (9D) antibodies it was demonstrated that 48 h after slaughtering the most intense reactions were observed in the range of pI of 5.5 ÷ 5.9, which is the pH range corresponding to the isoelectric point of troponin T. However, after 144 h post mortem the most intense reaction was demonstrated in the range of pI of 6.1÷ 7.7. This indicates the breakdown of troponin T and an increase of the number of degradation products of this protein occurring while the meat tenderization process progresses. The degradation products of troponin T identified by IEF can be an indicator of meat tenderization.

Wydawca

-

Rocznik

Tom

72

Numer

07

Opis fizyczny

s.458-462,rys.,tab.,bibliogr.

Twórcy

autor
  • Instytut Technologii Mięsa, Wydział Nauk o Żywności i Żywieniu, Uniwersytet Przyrodniczy w Poznaniu, ul. Wojska Polskiego 31, 60-624 Poznań
  • Instytut Technologii Mięsa, Wydział Nauk o Żywności i Żywieniu, Uniwersytet Przyrodniczy w Poznaniu, ul. Wojska Polskiego 31, 60-624 Poznań
autor
  • Instytut Technologii Mięsa, Wydział Nauk o Żywności i Żywieniu, Uniwersytet Przyrodniczy w Poznaniu, ul. Wojska Polskiego 31, 60-624 Poznań
autor
  • Instytut Technologii Mięsa, Wydział Nauk o Żywności i Żywieniu, Uniwersytet Przyrodniczy w Poznaniu, ul. Wojska Polskiego 31, 60-624 Poznań

Bibliografia

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  • Crystall B. B., Culioli J., Demeyer D., Honikel K. O., Moller A. J., Purslow P., Schwagele F., Shorthose R. I., Uytterhaegen L.: Recommendation of reference methods for assessment of meat tenderness. 40-th ICoMST 1994. Dan Haag, Netherlands, Aug.28-Sept. 2 session v. 05, 1994.
  • Dransfield E.: Optimization of tenderization, ageing and tenderness. Meat Sci. 1994, 36, 105-121.
  • Fritz J. D., Greaser M. L.: Changes in titin and nebulin in postmortem bovine muscle reveled by gel electrophoresis, western blotting and immunofluorescence microscopy. J. Food Sci. 1991, 56, 607-610, 615.
  • Goll D. E., Kleese W. C., Okitani A., Kumamto T., Cong J., Kaprell H. P.: Historical background and current status of the Ca2+-dependent proteinases system in intracellular calcium-dependent proteolysis. Mallgren R. L., Murachi T. (eds) – CSR press, Boca Raton, FL 1990, s. 3-24.
  • Grześ B., Pospiech E., Koćwin-Podsiadła M., Łyczyński A., Zybert A., Mikołajczak B., Iwańska E.: Analysis of the causes of meat quality variations of pigs with the genotype. Pol. J. Food Nutr. Sci. 2005, 14/55, SI 1, 59-63.
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  • Koohmaraie M.: Muscle proteinases and meat aging. Meat Sci. 1994, 36, 93-104.
  • Koohmaraie M.: The role of Ca2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 1992, 74, 239-245.
  • Kołakowski E.: Protein Determination and Analysis in Food Systems, [w:] Sikorski Z. E. (red.): Chemical & Functional Properties of Food Proteins. Pennsylvania, Lancaster 2001.
  • Lee E.-J., Kim Y.-H., Lee N.-H., Hong S.-I., Yamamoto K., Kim Y.-J.: The role of sarcoplasmatic protein in hydrostatic pressure-induced myofibrillar protein degradation. Meat Sci. 2011, 87, 219-222.
  • Marino R., Albenzio M., Malva A., Carporese M., Santillo A., Sevi A.: Changes in meat quality traits and sarcoplasmatic proteins during aging in three different cattle breeds. Meat Sci. 2014, 98, 178-185.
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  • Penny I. F., Dransfield E.: Relationship between toughness and troponin T in conditioned beef. Meat Sci. 1979, 3, 135-141.
  • Pospiech E., Peltre G., Wąsowicz E., Jeleń H., Greaser M. L., Mikołajczak B., Bresińska A., Gorączka A.: Elektroforeza, [w:] Jankiewicz M., Kędzior Z. (red.): Metody pomiarów i kontroli jakości w przemyśle spożywczym i biotechnologii. Wydawnictwo AR Poznań, WTŻ 2003, s. 171-210.
  • Pospiech E., Greaser M. L., Peltre G., Mikołajczak B.: Electrophoretic isofocusing in studies on meat protein from various animal species and pork stored under different conditions. Pol. J. Food Nutr. Sci. 2005, 14/55, 299-302.
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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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