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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Accessory enzymes have been identified in lignin-degrading fungi and bacteria that can generate hydrogen peroxide, which is used as a co-substrate by lignin-oxidising peroxidases. This article describes a glycolate oxidase enzyme from lignin-degrading bacterium Rhodococcus jostii RHA1, which functions as an efficient accessory enzyme for degradation of polymeric lignin substrates by bacterial DyP-type peroxidases. The article describes: (1) enzyme purification; (2) assays for enzyme activity; (3) analysis of substrate specificity; (4) assays for enzyme combinations with bacterial DyP-type peroxidases; (5) analysis of low molecular weight products obtained using enzyme combinations.
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http://dx.doi.org/10.1016/bs.mie.2025.02.009 | DOI Listing |