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
This paper explores the potentialities of hydrochar in protein separation and enzyme immobilization for non-energy biorefinery applications of hydrothermal carbonization. An innovative experimental procedure monitors soluble protein-hydrochar interactions and enzymatic reactions in a continuously stirred tank reactor. The hydrochar comes from hydrothermal carbonization of silver fir (200 °C, 30 min, 1/7 solid/water ratio) and standard activation (KOH, oven, 600 °C). Bovine serum albumin, a non-active, globular protein, was adsorbed at ≤3300 mg/g. Sip's isotherms fitted data well ( = 0.99999). The immobilization used a commercial β-glucosidase, which catalyzes the hydrolysis of cellobiose to glucose, a bottleneck of the cellulose to fermentable sugar bioconversion network due to the fast enzyme deactivation. The hydrochar adsorbed ≤26 w/w% of enzyme. The heterogeneous biocatalyst operational stability was 24 times that of the soluble one. The results encourage further investigations and foreshadow process schemes coupling hydrothermal carbonization and industrial bioconversions.
Download full-text PDF |
Source |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10401700 | PMC |
http://dx.doi.org/10.1021/acs.iecr.3c00765 | DOI Listing |
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