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
The use of the laccase enzyme from the fungus , coupled with the mediator 1-hydroxybenzotriazole (1-HBT) has been shown to be effective for the biocatalytic conversion of a hexameric lignin model compound containing three of the most common linkages found in native lignin. Cleavage of the model takes place over a 24 hours period predominantly at the β-O-4 ether linkage to give a previously known β-5 dimer intermediate which in turn was rapidly consumed to further degradation products. There is also mass spectrometric evidence of repolymerisation of the β-5 dimer and other degradation intermediates to form higher oligomers. Mechanistic pathways to account for the major catalytic processes are proposed.
Download full-text PDF |
Source |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11516409 | PMC |
http://dx.doi.org/10.1039/d4gc01720j | DOI Listing |
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