Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Background: Protein oxidation is widespread in biochemical systems. The objective of the study was to investigate the differences in protein oxidation, μ-calpain activity, desmin proteolysis and protein solubility of beef psoas major (PM) and semi-membranosus (SM) muscles under three packaging systems during postmortem ageing. At 24 h postmortem, beef muscles were packaged respectively in air-permeable film overwrap (AP), vacuum pack (VP) or modified atmosphere (MAP, 80% O + 20% CO ), and then displayed for 10 days at 4 °C.
Results: Carbonyl group values and thiol group content were significantly influenced by packaging type and storage time. The SM muscles from AP and MAP showed greater μ-calpain activity compared to VP. Desmin of PM and SM from AP and MAP samples showed decreased proteolysis compared with VP.
Conclusion: The results suggested that the inhibition of μ-calpain activity of beef samples from AP and MAP could be closely associated with protein oxidation which further lowered the level of desmin degradation compared to VP. © 2017 Society of Chemical Industry.
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Source |
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http://dx.doi.org/10.1002/jsfa.8316 | DOI Listing |
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