Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

Catalysts

Artur Jędrzak¹  Jakub Zdarta¹  Łukasz Klapiszewski¹  Teofil Jesionowski¹ 

[1] Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, PL-60965 Poznan, Poland;

关键词: enzyme immobilization;    cellulases;    titania-lignin hybrid;    immobilized cellulase stability;    cellulose hydrolysis;   

DOI  :  10.3390/catal7120374

来源: DOAJ

【 摘 要 】

Cellulase from Aspergillus niger was immobilized on a synthesized TiO2–lignin hybrid support. The enzyme was effectively deposited on the inorganic–organic hybrid matrix, mainly via physical interactions. The optimal initial immobilization parameters, selected for the highest relative activity, were pH 5.0, 6 h process duration, and an enzyme solution concentration of 5 mg/mL. Moreover, the effects of pH, temperature, and number of consecutive catalytic cycles and the storage stability of free and immobilized cellulase were evaluated and compared. Thermal and chemical stability were significantly improved, while after 3 h at a temperature of 50 °C and pH 6.0, the immobilized cellulase retained over 80% of its initial activity. In addition, the half-life of the immobilized cellulase (307 min) was five times that of the free enzyme (63 min). After ten repeated catalytic cycles, the immobilized biocatalyst retained over 90% of its initial catalytic properties. This study presents a protocol for the production of highly stable and reusable biocatalytic systems for practical application in the hydrolysis of cellulose.

【 授权许可】

Unknown