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
d-Xylonic acid (XA), derived from pentose sugar xylose, is a multifunctional high-value chemical with a wide range of applications in the fields of medicines, food, agriculture and is a valuable chemical reagent for the synthesis of other useful commodity chemicals. In the bacterial system, xylose dehydrogenase (XDH) catalyzes the oxidation of d-xylose into d-xylonolactone, consuming NAD or NADP as a cofactor. The d-xylonolactone then undergoes auto-oxidation into d-xylonic acid. Herein, the XDH enzyme overexpressed in is purified and immobilized on ferromagnetic nanoparticles, effectively converting xylose into xylonic acid. Parameters deciding the bioconversion were statistically optimized and obtained a maximum of 91% conversion rate. Kinetic parameters of immobilized xylose dehydrogenase showed a 2-fold increase in the maximum velocity of the reaction and catalytic efficiency compared to free enzyme. The operational stability test for the enzyme-nanoparticle conjugate retained 93% relative activity after 10 successive experiments, exhibiting the good recyclability of the biocatalyst for XA production.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1021/acs.bioconjchem.2c00159 | DOI Listing |
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