biostudies-literatureUnknown62(30)Gallifuoco AThis 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 (<i>R</i>² = 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 networIndustrial & engineering chemistry research11805-11813https://www.ebi.ac.uk/biostudies/studies/S-EPMC10401700biostudies-literatureAn Exploratory Study of Hydrochar as a Matrix for Biotechnological Applications.PMC10401700Spera APapa AATaglieri LDi Carlo AGallifuoco APassucci MfalseAn Exploratory Study of Hydrochar as a Matrix for Biotechnological Applications.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 (<i>R</i>² = 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 networ2023-01-01T00:00:00Z2023 Aug2025-04-20T03:16:56.018Z2025-02-19T01:58:08.482ZS-EPMC104017003754618410.1021/acs.iecr.3c00765