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Improved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method

Authors
Ryu, Young HaYeo, Ki BaekKi, Mi-RanKim, Yong JunPack, Seung Pil
Issue Date
15-Jan-2016
Publisher
ELSEVIER SCIENCE BV
Keywords
Cellulase; Immobilised enzymes; Immobilization; Polypeptides; Biosilicification; Silica forming peptide
Citation
BIOCHEMICAL ENGINEERING JOURNAL, v.105, pp.144 - 149
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL ENGINEERING JOURNAL
Volume
105
Start Page
144
End Page
149
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/89786
DOI
10.1016/j.bej.2015.09.006
ISSN
1369-703X
Abstract
The functional improvement of endoglucanase (EG), a key cellulose-hydrolyzing biocatalyst, is imperative for the practical use of cellulosic materials such as lignocellulose, stove and straws. Here, we employed a bio-inspired silica-encapsulation method to improve the stability and reusability of EG. We introduced a new silica-forming peptide (SFP) from Ectocarpus siliculosus at the C-terminus of EG to generate a recombinant fusion protein, EG-SFP, with auto-silicifying ability. We obtained an EG-SFP-encapsulated silica matrix (EG-SFP@Silica) via the EG-SFP-mediated auto-silicification process under ambient conditions. The immobilization efficiency was 90%. The introduction of SFP did not significantly affect the functionality of EG, and moreover, EG-SFP@Silica demonstrated higher thermostability by 5 degrees C than free EG-SFP or EG. In addition, EG-SFP@Silica retained 90% of its initial residual activity with up to 18 uses. These results provide a platform for the development of a practical enzymatic hydrolysis process for cellulosic materials. (C) 2015 Elsevier B.V. All rights reserved.
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