Browse > Article
http://dx.doi.org/10.5851/kosfa.2020.e21

Changes in Cathepsin Activity during Low-Temperature Storage and Sous Vide Processing of Beef Brisket  

Kaur, Lovedeep (School of Food and Advanced Technology, Massey University)
Hui, Seah Xin (School of Food and Advanced Technology, Massey University)
Boland, Mike (Riddet Institute, Massey University)
Publication Information
Food Science of Animal Resources / v.40, no.3, 2020 , pp. 415-425 More about this Journal
Abstract
It is believed that two main proteolytic systems are involved in the tenderization of meat: the cathepsins and the calpains. Many researchers consider the calpain system to be the major contributor to meat tenderness during post-mortem storage. However, the role and activity of cathepsins during post-mortem storage or low temperature meat processing is unclear, particularly for the tough meat cuts like brisket. Thus, the study was designed to investigate the effects of cold (refrigerated and frozen) storage and sous vide processing on the activities of cathepsin B, H, and L in beef brisket. There were no significant changes in pH and cathepsin H activity throughout the 18 d of storage at both temperatures. However, an increase in cathepsin B activity was observed during the first 4 d at both storage temperatures, but subsequently the activity remained unchanged. Cathepsins B and L were found to be more heat stable at sous vide temperatures (50℃ for 24 h, 55℃ for 5 h and at 60℃ and 70℃ for 1 h) compared to cathepsin H. Cathepsin B+L activity was found to increase after sous vide cooking at 50℃ for 1 h but decreased to about 47% relative to the uncooked control after 24 h of cooking. These results suggest that cathepsins B and L may contribute to the improved meat tenderness usually seen in sous vide cooked brisket meat.
Keywords
cathepsin; endogenous enzymes; meat; post-mortem storage; sous vide;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Laakkonen E, Wellington GH, Sherbon JN. 1970. Low-temperature, long-time heating of bovine muscle 1. Changes in tenderness, water-binding capacity, pH and amount of water-soluble components. J Food Sci 35:175-177.   DOI
2 Lana A, Zolla L. 2016. Proteolysis in meat tenderization from the point of view of each single protein: A proteomic perspective. J Proteom 147:85-97.   DOI
3 Matos EAD. 2013. Nutrition and farming practices as modulators of quality in gilthead seabream (Sparus aurata). Ph.D. dissertation, Universidade do Algarve, Faro, Portual.
4 Minitab. 2014. Minitab 17 statistical software. Minitab, State College, PA.
5 Ouali A, Gagaoua M, Boudida Y, Becila S, Boudjellal A, Herrera-Mendez CH, Sentandreu MA. 2013. Biomarkers of meat tenderness: Present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Sci 95:854-870.   DOI
6 Pomponio L, Ertbjerg P. 2012. The effect of temperature on the activity of ${\mu}$-and m-calpain and calpastatin during postmortem storage of porcine longissimus muscle. Meat Sci 91:50-55.   DOI
7 Rico E, Toldra F, Flores J. 1991. Problems associated with the assay of cathepsin D in meat and meat products. Food Chem 40:87-91.   DOI
8 Solvig H. 2014. The effect of proteolytic lysosomal enzymes and cathepsin B on collagen and connective tissue denaturation during long time low temperature cooking. M.S. thesis, Stavanger Univ., Stavanger, Norway.
9 Spanier AM, McMillin KW, Miller JA. 1990. Enzyme activity levels in beef: Effect of postmortem aging and end-point cooking temperature. J Food Sci 55:318-322.   DOI
10 Toldra F, Etherington DJ. 1988. Examination of cathepsins B, D, H and L activities in dry-cured hams. Meat Sci 23:1-7.   DOI
11 Bowker BC, Eastridge JS, Paroczay EW, Callahan JA, Solomon MB. 2010. Aging/tenderization mechanisms. In Handbook of meat processing. Toldra F (ed). Blackwell, Oxford, IA, USA. pp 87-104.
12 van Jaarsveld FP, Naude RJ, Oelofsen W. 1997. The effects of Ca ions, EGTA and storage time on myofibrillar protein degradation, levels of $Ca^{2+}$-dependent proteases and cathepsins B, H, L and D of ostrich skeletal muscle. Meat Sci 45:517-529.   DOI
13 Zhu X, Kaur L, Staincliffe M, Boland M. 2018. Actinidin pretreatment and sous vide cooking of beef brisket: Effects on meat microstructure, texture and in vitro protein digestibility. Meat Sci 145:256-265.   DOI
14 Agarwal SK. 1990. Proteases cathepsins: A view. Biochem Educ 18:67-72.   DOI
15 Allen RE, Goll DsE. 2003. Cellular and developmental biology of skeletal muscle as related to muscle growth. In Biology of growth of domestic animals. Scanes CG (ed). Iowa State Press, Ames, IA, USA. pp 148-169
16 Baldwin DE. 2012. Sous vide cooking: A review. Int J Gastr Food Sci 1:15-30.   DOI
17 Bandman E, Zdanis D. 1988. An immunological method to assess protein degradation in post-mortem muscle. Meat Sci 22:1-19.   DOI
18 Beltran, J, Bonnet M, Ouali A. 1992. Comparative action of cathepsins B and L on intramuscular collagen as assessed by differential scanning calorimetry. Meat Sci 32:299-306.   DOI
19 Burleigh MC, Barrett AJ, Lazarus GS. 1974. Cathepsin B1. A lysosomal enzyme that degrades native collagen. Biochem J 137:387-398.   DOI
20 Cheret R, Delbarre-Ladrat C, de Lamballerie-Anton M, Verrez-Bagnis V. 2007. Calpain and cathepsin activities in post mortem fish and meat muscles. Food Chem 101:1474-1479.   DOI
21 Dominguez-Hernandez E, Salaseviciene A, Ertbjerg P. 2018. Low-temperature long-time cooking of meat: Eating quality and underlying mechanisms. Meat Sci 143:104-113.   DOI
22 Christensen L, Ertbjerg P, Aaslyng MD, Christensen M. 2011. Effect of prolonged heat treatment from $48^{\circ}C$ to $63^{\circ}C $ on toughness, cooking loss and color of pork. Meat Sci 88:280-285.   DOI
23 Christensen L, Ertbjerg P, Loje H, Risbo J, van den Berg FWJ, Christensen M. 2013. Relationship between meat toughness and properties of connective tissue from cows and young bulls heat treated at low temperatures for prolonged times. Meat Sci 93:787-795.   DOI
24 Christian J, Stephen JJ. 2010. Freezing/thawing. In Handbook of meat processing. Toldra F (ed). Blackwell, Oxford, IA, USA. pp 105-124.
25 Ertbjerg P, Christiansen LS, Pedersen AB, Kristensen L. 2012. The effect of temperature and time on activity of calpain and lysosomal enzymes and degradation of desmin in porcine longissimus muscle. 58th International Congress of Meat Science and Technology, Montreal, QC, Canada.
26 Hamm R, Deatherage FE. 1960. Changes in hydration, solubility and charges of muscle proteins during heating of meat. J Food Sci 25:587-610.   DOI
27 Herrera-Mendez CH, Becila S, Boudjellal A, Ouali A. 2006. Meat ageing: Reconsideration of the current concept. Trends Food Sci Technol 17:394-405.   DOI
28 Koohmaraie M, Geesink GH. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 74:34-43.   DOI
29 Koohmaraie M, Seideman SC, Schollmeyer JE, Dutson TR, Babiker AS. 1988. Factors associated with the tenderness of three bovine muscles. J Food Sci 53:407-410.   DOI