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
Structural modification of protein prior to food application is an emergent approach to improve functionalization. The effectiveness of high-power ultrasound at varying amplitudes (0-100%) on the properties of pea protein powder was investigated in this study. The resulting modification was also tested with model gluten-free bread formulation and by screening the emulsion properties within vegetable oil. The 50% and beyond amplitude levels had significant impact on protein solubility, viscosity, Fourier Transform Infrared (FTIR) spectra, emulsion activity and stability. Foaming capacity and stability were enhanced with 75 and 100% amplitudes while the 25% amplitude exhibited the highest absolute zeta-potential. There was a concomitant increase in ultrasound amplitude and oil-binding capacity (2.83-6.43 g/g) where the water-holding capacity gradually decreased (5.78-3.61 g/g) with the increase in ultrasound power. The increase in ultrasound power led to decrease in L* values but progressively increased the total color difference (ΔE). Sonication (50% amplitude) also promoted the in-vitro digestibility of proteins by 22% as compared to the untreated sample. Scanning electron microscopy (SEM) fairly depictured the structural modification and FTIR spectra clearly demonstrated conformational changes in protein powders. The fortification with restructured pea protein powder significantly affected the volume and adhesiveness of glutenfree bread.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1007/s11130-023-01087-1 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!