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: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
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
This paper aimed to evaluate the effects of the structure and gel properties of myofibrillar protein (MP) on 300-days-old chicken breast quality treated with ultrasound (300 W) and low addition (4 mg/mL) of potassium alginate (UPA). The results showed that UPA group exhibited lower liquid loss and optimized texture correlated with the formed water barrier and damaged myofibrils. UPA reduced the MP size and increased its solubility, and the decreased myosin thermostability and dissociated actomyosin reduced heating time for improved texture. UPA improved the gel strength, elastic modulus and ordered-arrangement of network. During gelation, the aggregation of myosin head was weakened and cross-linking of myosin tail and PA molecules was enhanced by hydrophobic interactions. UPA further inhibited the formation of disulfide bonds of myosin head and increased gel firmness. The lower myosin gelling temperature thus accelerated gel formation, and enhanced protein association with PA molecules facilitated the better gel performance.
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Source |
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http://dx.doi.org/10.1016/j.foodchem.2021.129873 | DOI Listing |
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