Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline
dc.contributor.author | Mohrhauser, D. | |
dc.contributor.author | Lonergan, Steven | |
dc.contributor.author | Huff-Lonergan, Elisabeth | |
dc.contributor.author | Underwood, K. | |
dc.contributor.author | Weaver, A. | |
dc.contributor.department | Animal Science | |
dc.date | 2018-02-13T23:51:25.000 | |
dc.date.accessioned | 2020-06-29T23:40:41Z | |
dc.date.available | 2020-06-29T23:40:41Z | |
dc.date.copyright | Wed Jan 01 00:00:00 UTC 2014 | |
dc.date.embargo | 2014-04-09 | |
dc.date.issued | 2014-03-01 | |
dc.description.abstract | <p>The objectives of this study were to 1) determine the conditions (temperature and pH) that exist in early postmortem muscle of normally chilled and delay chilled beef carcasses to provide a model for in vitro work and 2) determine the mechanism by which early postmortem temperature/pH conditions found in beef muscle influence the enzymes that regulate the aging process in vitro. For objective 1, 7 finished beef animals (HCW 385 ± 8 kg) were harvested with the right sides subjected to normal chilling (2.3°C) approximately 1.25 h postmortem and the left sides subjected to ambient temperature (delay chilling; 22.6°C) for an additional 4.75 h postmortem and then allowed to chill at 2.3°C. Delay chilled carcasses had a more rapid pH decline (<em>P</em> < 0.05) and a slower rate of carcass cooling (<em>P</em> < 0.05). No differences were observed between normally chilled and delay chilled samples for sarcomere length or postmortem proteolysis of troponin T (TnT; <em>P</em> > 0.10). Warner-Bratzler shear force (WBSF) was reduced in steaks from normally chilled carcasses at 14 d (<em>P</em> < 0.05), while results indicated a strong, positive correlation between 14-d WBSF and 3-h longissimus dorsi muscle (LM) temperature (<em>r</em> = 0.67, <em>P</em> < 0.01) as well as a strong, negative correlation between 14-d WBSF and 6-h LM pH (<em>r</em> = –0.65, <em>P</em> < 0.02). These results were used to design the methodology for objective 2, where isolated myofibrils were subjected to μ-calpain digestion at 4 or 22°C with either a fast or slow initial pH decline. As expected, digestions with a fast initial pH decline had lower pH values in the early time points of the incubation (<em>P</em> < 0.05). No differences were detected in μ-calpain activity or in the degradation of intact TnT between the fast and slow pH decline treatments (<em>P</em> > 0.10); however, warmer digestions resulted in a tendency for increased activation of μ-calpain (<em>P</em> < 0.10) and a significant reduction in intact TnT (<em>P</em> < 0.05). Additionally, a temperature × time interaction was revealed in μ-calpain activity and in the degradation of intact TnT (<em>P</em> < 0.05). Specifically, assayed calpain activity was lower at 0.17, 0.33, 1, and 3 h and greater at 72 h in warmer digestions, while intact TnT disappearance was greater as both time and digestion temperature increased. Meat aging and μ-calpain activity are influenced by both temperature and pH, but more research is necessary to fully realize their relationships.</p> | |
dc.description.comments | <p>This article is from <em>Journal of Animal Science</em> 92 (2014): 1261–1270, doi:<a href="http://dx.doi.org/10.2527/jas.2013-7270" target="_blank">10.2527/jas.2013-7270</a>. Posted with permission.</p> | |
dc.format.mimetype | application/pdf | |
dc.identifier | archive/lib.dr.iastate.edu/ans_pubs/42/ | |
dc.identifier.articleid | 1036 | |
dc.identifier.contextkey | 5463669 | |
dc.identifier.s3bucket | isulib-bepress-aws-west | |
dc.identifier.submissionpath | ans_pubs/42 | |
dc.identifier.uri | https://dr.lib.iastate.edu/handle/20.500.12876/9846 | |
dc.language.iso | en | |
dc.source.bitstream | archive/lib.dr.iastate.edu/ans_pubs/42/2014_MohrhauserDA_Calpain1ActivityBovine.pdf|||Sat Jan 15 00:12:05 UTC 2022 | |
dc.source.uri | 10.2527/jas.2013-7270 | |
dc.subject.disciplines | Agriculture | |
dc.subject.disciplines | Animal Sciences | |
dc.subject.disciplines | Meat Science | |
dc.subject.keywords | beef | |
dc.subject.keywords | chilling | |
dc.subject.keywords | μ-calpain | |
dc.subject.keywords | proteolysis | |
dc.title | Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline | |
dc.type | article | |
dc.type.genre | article | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | 8e04bc80-6e32-476c-a184-b0311cebe213 | |
relation.isAuthorOfPublication | 6a8e1178-0f76-46eb-bf7a-9f871232456b | |
relation.isOrgUnitOfPublication | 85ecce08-311a-441b-9c4d-ee2a3569506f |
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