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Titolo:
Evidence against the non-enzymatic calcium theory of tenderization
Autore:
Geesink, GH; Taylor, RG; Bekhit, AED; Bickerstaffe, R;
Indirizzi:
Lincoln Univ, Anim & Food Sci Div, Mol Biotechnol Grp, Canterbury, New Zealand Lincoln Univ Canterbury New Zealand echnol Grp, Canterbury, New Zealand INRA, Rech Viande Stn, F-63122 Ceyrat, France INRA Ceyrat France F-63122INRA, Rech Viande Stn, F-63122 Ceyrat, France
Titolo Testata:
MEAT SCIENCE
fascicolo: 4, volume: 59, anno: 2001,
pagine: 417 - 422
SICI:
0309-1740(200112)59:4<417:EATNCT>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONGISSIMUS MUSCLE; MEAT TENDERIZATION; BEEF TENDERNESS; POSTMORTEM PROTEOLYSIS; MYOFIBRILLAR PROTEINS; DEGRADATION; CALPASTATIN; MECHANISM; LAMB; IONS;
Keywords:
calcium; tenderness; sarcomere length; proteolysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Geesink, GH Inst Anim Sci & Hlth, ID Lelystad, POB 65, NL-8200 AB Lelystad, Netherlands Inst Anim Sci & Hlth POB 65 Lelystad Netherlands NL-8200 AB s
Citazione:
G.H. Geesink et al., "Evidence against the non-enzymatic calcium theory of tenderization", MEAT SCI, 59(4), 2001, pp. 417-422

Abstract

The objective of the present study was to determine whether variation in the tenderization of lamb longissimus could be attributed to variations in the rise in free calcium postmortem and sarcomere lengthening post rigor. The longissimus muscle of 10 crossbred lambs (Romney x Coopworth) was sampledat 1 and 7 days postmortem for determination of MIRINZ shear force, myofibrillar fragmentation index (MFI), sarcomere length, free calcium, and proteolysis of troponin-T. Despite considerable variation in tenderness and tenderization of the muscles, sarcomere lengthening was not observed. The concentration of free calcium at 7 days postmortem correlated significantly withthe MFI (r=0.640; P<0.05) and tended to correlate with the shear force (r=-0.596; P < 0.1) and degradation of troponin-T (r = 0.625; P < 0.1). Degradation of troponin-T was significantly correlated with tenderization (r = 0.664; P < 0.05). Troponin-T is a calpain substrate, but reportedly is not degraded through a direct effect from calcium. The present results, therefore, suggest that the variation in free calcium in postmortem muscle affects tenderization through an effect on the calpain system and not through a direct effect of calcium on myofibrillar proteins. Consequently, the results ofthis study do not support the (calcium) theory that calcium directly affects tenderization. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:36:07