Effect of added μ-calpain and post-mortem storage on the mechanical properties of bovine single muscle fibres extended to fracture

被引:10
作者
Christensen, M [1 ]
Young, RD
Lawson, MA
Larsen, LM
Purslow, PP
机构
[1] Royal Vet & Agr Univ, Dept Dairy & Food Sci, DK-1871 Frederiksberg C, Denmark
[2] Royal Vet & Agr Univ, Dept Chem, DK-1958 Frederiksberg, Denmark
[3] Univ Wales Coll Cardiff, Sch BioSci, Cardiff CF10 3TL, S Glam, Wales
[4] Univ Guelph, Dept Food Sci, Guelph, ON N1G 2W1, Canada
关键词
beef; proteolysis; mu-calpain; post-mortem storage; mechanical properties; tensile test; single muscle fibres;
D O I
10.1016/S0309-1740(03)00025-1
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effects of p-calpain and post-mortem storage on the strength of single muscle fibres were investigated. During the 10 min of incubation at pH 7.5, mu-calpain became evenly distributed throughout the fibre. mu-Calpain-incubation resulted in thinner (P<0.001) Z-lines and reduced (P<0.001) the strength of the fibres compared to controls. These results demonstrate that mu-calpain is capable of mechanically weakening the muscle fibres. Post-mortem storage of meat for 10 days at 2degreesC weakened (P<0.001) the muscle fibres compared to 24-h fibres. The presence or absence of Ca2+ affected fibre stiffness. Fibres incubated at pH 7.5 in 100 muM Ca2+ were less stiff than fibres incubated in 200 muM EGTA. Breaking stress and strain were not affected by Ca2+. We hypothesise that Ca2+ causes conformational changes in some of the load-bearing proteins, which alters their initial resistance to extension, but does not affect the breaking strength of the fibres. (C) 2003 Elsevier Ltd. All rights reserved.
引用
收藏
页码:105 / 112
页数:8
相关论文
共 27 条
[1]   CA2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL-MUSCLE [J].
BUSCH, WA ;
SUZUKI, A ;
STROMER, MH ;
GOLL, DE .
JOURNAL OF CELL BIOLOGY, 1972, 52 (02) :367-&
[2]   The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue [J].
Christensen, M ;
Purslow, PP ;
Larsen, LM .
MEAT SCIENCE, 2000, 55 (03) :301-307
[3]   STUDIES IN MEAT TENDERNESS .7. CHANGES IN FINE STRUCTURE OF MEAT DURING AGING [J].
DAVEY, CL ;
GILBERT, KV .
JOURNAL OF FOOD SCIENCE, 1969, 34 (01) :69-&
[4]   Calpains from thaw rigor muscle [J].
Dransfield, E .
MEAT SCIENCE, 1996, 43 (3-4) :311-320
[5]   MODELING POSTMORTEM TENDERIZATION .4. ROLE OF CALPAINS AND CALPASTATIN IN CONDITIONING [J].
DRANSFIELD, E .
MEAT SCIENCE, 1993, 34 (02) :217-234
[6]  
Ertbjerg P, 1999, J ANIM SCI, V77, P2428
[7]  
Gann G L, 1978, Meat Sci, V2, P129, DOI 10.1016/0309-1740(78)90013-X
[8]   Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat [J].
Hopkins, DL ;
Thompson, JM .
AUSTRALIAN JOURNAL OF AGRICULTURAL RESEARCH, 2002, 53 (02) :149-166
[9]   Inhibition of protease activity 2. Degradation of myofibrillar proteins, myofibril examination and determination of free calcium levels [J].
Hopkins, DL ;
Thompson, JM .
MEAT SCIENCE, 2001, 59 (02) :199-209
[10]  
HuffLonergan E, 1996, J ANIM SCI, V74, P993