Title:
Immobilization of Cellulase Enzymes on Epoxy Sepabeads® for the Hydrolysis of Lignocellulosic Materials
Author(s):
De Bari, I., Verardi, A., Calabrò, V., Liuzzi, F., Ricca, E., Braccio, G.
Document(s):
Paper
Abstract:
For several years, international research has been performing the optimization of cellulose enzymatic hydrolysis to produce bioethanol. Enzymes low specific activity and fast deactivation are relevant problems in the development of this process and additional improvements are needed to make bioethanol comparable to traditional fuels. Enzymes immobilization facilitates biocatalyst recovery and reuse. Furthermore, enzymes immobilization avoids autolysis and increase enzyme stability allowing continuous operation for long periods, reducing processes costs and making this process more suitable to industrial scale up. In this paper, commercial cellulase enzymes (Celluclast 1.5 and Novozym 188) immobilization on epoxy Sepabeads® has been investigated. These supports ensure a mild physical adsorption of the enzymes followed by a very fast intramolecular covalent binding with the material epoxy groups. Data show that 60% of loaded Celluclast proteins were adsorbed by the support and that more than 90% of these proteins remained stably linked even after repeated washings. Similar results were obtained with Novozym. Novozym enzyme immobilized was used for ß-glucosidase activity test. The first analyses show that immobilized Novozym activity is comparable with free enzyme. The paper shows preliminary results about immobilized biocatalysts performances.
Keywords:
absorption, bioethanol, enzymatic hydrolysis, enzymatic process
Topic:
Biological conversion - Fermentation, enzymatic processes
Subtopic:
Biological conversion - fermentation, enzymatic processes
Event:
18th European Biomass Conference and Exhibition
Session:
VP2.6.40
Pages:
1440 - 1442
ISBN-13:
978-88-89407-56-1
ISBN-10:
88-89407-56-5
Paper DOI:
10.5071/18thEUBCE2010-VP2.6.40
Price:
FREE
