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
Marigold-like tyrosinase-entrenched nanostructures were developed by a facile method using a metal cofactor to overcome the limitations of conventional enzyme immobilization techniques. The protein-copper complex promotes the hierarchical self-assembly of nanopetals into marigold-like microstructures through a sequential germination process. Nanopetals, which originated from bead-like tiny projections, showed budding over the surface and promoted the anisotropic growth of copper phosphate nanocrystals upon co-ordination with the active functional groups in protein. This organic-inorganic hybrid showed excellent re-usability, comparable catalytic efficiency, faster reaction rate, improved storage, and thermal stability without affecting the enzyme activity.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1039/d0dt02358b | DOI Listing |
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