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

Young Ha Ryu; Ki Baek Yeo; Mi Ran Ki; Yong Jun Kim; Seung Pil Pack

doi:10.1016/j.bej.2015.09.006

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

Young Ha Ryu
, Ki Baek Yeo
, Mi Ran Ki
, Yong Jun Kim
, Seung Pil Pack^*

^*Corresponding author for this work

Korea University (SEJONG)

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

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. °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.

Original language	English
Pages (from-to)	144-149
Number of pages	6
Journal	Biochemical Engineering Journal
Volume	105
DOIs	https://doi.org/10.1016/j.bej.2015.09.006
Publication status	Published - 2016 Jan 15

Bibliographical note

Publisher Copyright:
© 2015 Elsevier B.V.

Keywords

Biosilicification
Cellulase
Immobilised enzymes
Immobilization
Polypeptides
Silica forming peptide

ASJC Scopus subject areas

Biotechnology
Environmental Engineering
Bioengineering
Biomedical Engineering

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10.1016/j.bej.2015.09.006

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

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. °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.",

keywords = "Biosilicification, Cellulase, Immobilised enzymes, Immobilization, Polypeptides, Silica forming peptide",

author = "Ryu, \{Young Ha\} and Yeo, \{Ki Baek\} and Ki, \{Mi Ran\} and Kim, \{Yong Jun\} and Pack, \{Seung Pil\}",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier B.V.",

year = "2016",

month = jan,

day = "15",

doi = "10.1016/j.bej.2015.09.006",

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T1 - Improved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method

AU - Ryu, Young Ha

AU - Yeo, Ki Baek

AU - Ki, Mi Ran

AU - Kim, Yong Jun

AU - Pack, Seung Pil

PY - 2016/1/15

Y1 - 2016/1/15

N2 - 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. °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.

AB - 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. °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.

KW - Biosilicification

KW - Cellulase

KW - Immobilised enzymes

KW - Immobilization

KW - Polypeptides

KW - Silica forming peptide

UR - https://www.scopus.com/pages/publications/84942531836

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DO - 10.1016/j.bej.2015.09.006

M3 - Article

AN - SCOPUS:84942531836

SN - 1369-703X

VL - 105

SP - 144

EP - 149

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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