Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 197
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 197
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 271
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3165
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 597
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 511
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 317
Function: require_once
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In the food industry, the emulsifying process alters both the stability and quality of the emulsified products prepared by bovine bone high-temperature hydrolysate (BBHH). The microstructure and interactions of BBHH emulsion were characterized by cryo-scanning electron microscopy (Cryo-SEM) and Raman spectroscopy during emulsification. Notably, BBHH emulsion exhibited the best properties under emulsifying for 120 s, attributed to its interfacial adsorption characteristics. In terms of microstructure, the droplets were small and uniform, and the cross-linking and network structure between the droplet surfaces were obvious at 120 s. Raman spectroscopy indicated that the adsorption of BBHH at the oil-water interface mainly involved an increase of the β-sheet at the expense of the α-helix region. In addition, protein adsorption and structural development at the interface were driven by hydrophobic interactions, while further rearrangement and polymerization were mediated by disulfide bonds. Furthermore, the stability and particle size distribution of the emulsion also supported the results. This study provided a theoretical basis for the behavior of BBHH emulsion formation, which expanded valuable insights into the mechanisms by which liquid food emulsification systems mediated by animal-derived proteins and how they behave under a variety of external conditions.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.137667 | DOI Listing |