1995
DOI: 10.1111/j.1365-2621.1995.tb09828.x
|View full text |Cite
|
Sign up to set email alerts
|

Postmortem Delay Time and Heating Rate Affect Tenderness and Ultrastructure of Prerigor Cooked Bovine Muscle

Abstract: The response of prerigor bovine muscle to different heating conditions was determined. Samples were fast-heated at six postmortem times or at five heating rates at four early postmortem times. All samples were heated to 70°C internally. Prerigor muscle cooked at progressively shorter postmortem times and faster heating rates had correspondingly lower shear values. In prerigor fast-heated samples, phase contrast microscopy revealed transverse bright stripes along the myofiber while scanning electron microscopy … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

1
2
0

Year Published

1996
1996
2021
2021

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 8 publications
(3 citation statements)
references
References 24 publications
1
2
0
Order By: Relevance
“…8) presented more fractures than the other three species. All samples showed Z-line and M-band degradation, in agreement with the reported by Wu et al [31] Nonetheless, Shimada and Takahashi [32] reported that the damage in Z-line is due to the liberation of phospholipids in pork and beef calcium-marinated samples, reducing the importance of calpains role in meat tenderisation. On the other hand, Ho et al [33] reported that changes in myofibrillar structure were mainly due to I-band degradation as reported by who described that myofibril structures in postmortem muscle are replaced by an amorphous, non-uniform bands adjacent to I-band ruptures, increasing intermyofibril gaps, as compared to premortem tissue.…”
Section: Structural Changessupporting
confidence: 90%
“…8) presented more fractures than the other three species. All samples showed Z-line and M-band degradation, in agreement with the reported by Wu et al [31] Nonetheless, Shimada and Takahashi [32] reported that the damage in Z-line is due to the liberation of phospholipids in pork and beef calcium-marinated samples, reducing the importance of calpains role in meat tenderisation. On the other hand, Ho et al [33] reported that changes in myofibrillar structure were mainly due to I-band degradation as reported by who described that myofibril structures in postmortem muscle are replaced by an amorphous, non-uniform bands adjacent to I-band ruptures, increasing intermyofibril gaps, as compared to premortem tissue.…”
Section: Structural Changessupporting
confidence: 90%
“… Wheeler and Koohmaraie (1994) reported that the WBSF of ovine longissimus muscle increased from 5.10 kg at 3 h postmortem (per-rigor) to 8.66 kg at 24 h postmortem (rigor mortis), and then decreased to 4.36 kg by 72 h postmortem (post-rigor). Wu et al (1995) found that pre-rigor bovine stemomandibularis muscle was more tender than post-rigor control muscle cooked to 70°C internally. The amount of free water increased during rigor mortis and resolution, which caused an accumulation of water on the cut surface and higher drip loss ( Devine et al, 2014 ).…”
Section: Introductionmentioning
confidence: 91%
“…However, a direct relationship between softening and chemical structure of myofibrillar proteins was demonstrated. [5] There are two types of calpains: calpain I or m, requiring 50 to 70 mM Ca 2þ for activation, and calpain II or m, requiring 1 to 5 mM Ca 2þ . [6] Softening of bovine meat activated by 1 to 5 mM Ca 2þ without notably altering other sensory characteristics was observed.…”
Section: Introductionmentioning
confidence: 99%