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
Special enzymes are necessary for producing gluten-free foods, and specific proteolytic enzymes with gluten-degrading activity may be used as oral treatments for celiac disease. Enzymes of the kind were sought, identified, and preliminarily characterized in two strains of the alkaliphilic microscopic fungi Sodiomyces alkalinus and S. magadiensis. Post-glutamine cleaving activity was for the first time observed in the strains along with proline-cleaving activities of dipeptidyl peptidase 4 (DPP4) and proline aminopeptidase (PAP), allowing efficient hydrolysis of both proline/glutamine-rich gluten peptides and whole gluten. The optimal pH and pH-dependent stability were determined for the peptidases in question. All of the enzymes shown to cleave the prolyne/glutamine-containing bonds were assigned to the serine peptidase group and were found to be stable in moderately acidic and alkaline conditions. Owing to their activities, the peptidases are promising as tools to produce gluten-free foods and to design diets for gluten-intolerant patients.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1134/S0012496622700144 | DOI Listing |
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