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
Pumpkin seeds are rich source of nutritionally well-balanced proteins. The biochemical, nutritional, and functional properties of the protein isolate (PPI) and protein fractions from pumpkin seed were evaluated. Extraction method for PPI was optimized by varying NaCl (0, 0.5, 1 M) and flour-to-solution ratio (1:5, 1:10, 1:25), at pH 9.0. Proteins were extracted by Osborne procedure and the alkali fraction (AF, 45.82%) was found to be the predominant fraction. SDS-PAGE profile of PPI revealed major bands ranging from 50 to 7 kDa. AF contained all the essential amino acids (EAA) except lysine and threonine, as required by pre-school children (FAO/WHO). PPI and AF showed better protein efficiency ratio and EAA/TAA (total) %, indicating the presence of good quality proteins. Functional properties were found to be comparable with soybean protein isolate. Circular dichroism studies showed that water fraction comprised of α-helix and random coils, while salt and alkali fractions contained β-strand and coils.
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Source |
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http://dx.doi.org/10.1016/j.foodchem.2020.128177 | DOI Listing |
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