alexa Reusability of Immobilized Cellulases with Highly Retained Enzyme Activity and their Application for the Hydrolysis of Model Substrates and Lignocellulosic Biomass | Abstract
ISSN: 2157-7544

Journal of Thermodynamics & Catalysis
Open Access

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Research Article

Reusability of Immobilized Cellulases with Highly Retained Enzyme Activity and their Application for the Hydrolysis of Model Substrates and Lignocellulosic Biomass

Yuko Ikeda, Archana Parashar, Michael Chae and David C Bressler*
Department of Agricultural, Food and Nutritional Science, University of Alberta, 410 Agriculture/Forestry Centre, Edmonton, AB, T6G 2P5, Canada
Corresponding Author : David C Bressler
Department of Agricultural
Food and Nutritional Science
University of Alberta, 410 Agriculture/Forestry Centre
Edmonton, AB, T6G 2P5, Canada
Tel: 17804924986
E-mail: [email protected]
Received July 21, 2015; Accepted August 10, 2015; Published August 22, 2015
Citation: Ikeda Y, Parashar A, Chae M, Bressler DC (2015) Reusability of Immobilized Cellulases with Highly Retained Enzyme Activity and their Application for the Hydrolysis of Model Substrates and Lignocellulosic Biomass. J Thermodyn Catal 6:149. doi:10.4172/2157-7544.1000149
Copyright: © 2015 Ikeda Y, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Enzyme immobilization is a promising approach to reduce enzyme cost in lignocellulose-based biorefining. This paper describes the reusability of immobilized cellulases and examines hydrolysis of various components of lignocellulose and industrial lignocellulosic biomass when using immobilized cellulases. Two different commercial cellulases, previously denoted as Cellulases 1 (C1) and Cellulases 2 (C2), were separately immobilized on nonporous (S1) and porous (S2) silica. Enzyme immobilization was achieved using a simple, cheap, and safe absorption method that maintains high hydrolysis yields by creating a cellulosome-like environment. Here, we show that all immobilized cellulases could be reused for at least 4 cycles while maintaining ≥ 50% of their activity. In fact, systems containing immobilized C1 displayed >40% activity in the 6th cycle, regardless of the silica used. We obtained relatively high-retained enzyme activities when our immobilized cellulases were employed to hydrolyze cellophane paper (60%–78%), phosphoric acid swollen cellulose (72%–79%), a common component of hemicellulose (xylan; 62%– 84%), steam-exploded poplar (41%–62%), and waste office automation paper (34%–48%). Thus, the immobilized cellulase systems used in this study may be industrially feasible as they can be reused while maintaining relatively high levels of enzyme activities. Importantly, we also show that our immobilized cellulase systems can be applied to not only model substrates, but also to industrially produced lignocellulosic biomass.

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