Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production

Hah Young Yoo; Ja Hyun Lee; Young Joon Suh; Sung Bong Kim; Seung Moon Park; Seung Wook Kim

doi:10.1007/s12257-014-0298-8

Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production

Hah Young Yoo, Ja Hyun Lee, Young Joon Suh, Sung Bong Kim, Seung Moon Park, Seung Wook Kim

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

8 Citations (Scopus)

Abstract

In the previous work, acetyl xylan esterase (AXE) of Aspergillus ficcum was successfully produced in Pichia pastoris as host. In this study, the recombinant AXE was immobilized on graphite oxide and used for the production of peracetic acid. Immobilization efficiency was enhanced by modifying graphite oxide via surface functionalization. The conditions for enzyme immobilization were also investigated and the optimal conditions were determined as 4℃ of temperature, 24 h of reaction time and pH 7. The activity of immobilized AXE was found to be 62.53 U/g-support. With the immobilized AXE, about 134 mM of peracetic acid was produced under 37℃ of temperature and 30 min of reaction time. Enzyme activity remained at > 50% of the original after 10 production cycles.

Original language	English
Pages (from-to)	1042-1047
Number of pages	6
Journal	Biotechnology and Bioprocess Engineering
Volume	19
Issue number	6
DOIs	https://doi.org/10.1007/s12257-014-0298-8
Publication status	Published - 2014 Nov

Bibliographical note

Publisher Copyright:
© 2014, The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg.

Keywords

acetyl xylan esterase
enzyme immobilization
graphite oxide
peracetic acid

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology
Biomedical Engineering

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10.1007/s12257-014-0298-8

Cite this

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title = "Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production",

abstract = "In the previous work, acetyl xylan esterase (AXE) of Aspergillus ficcum was successfully produced in Pichia pastoris as host. In this study, the recombinant AXE was immobilized on graphite oxide and used for the production of peracetic acid. Immobilization efficiency was enhanced by modifying graphite oxide via surface functionalization. The conditions for enzyme immobilization were also investigated and the optimal conditions were determined as 4℃ of temperature, 24 h of reaction time and pH 7. The activity of immobilized AXE was found to be 62.53 U/g-support. With the immobilized AXE, about 134 mM of peracetic acid was produced under 37℃ of temperature and 30 min of reaction time. Enzyme activity remained at > 50% of the original after 10 production cycles.",

keywords = "acetyl xylan esterase, enzyme immobilization, graphite oxide, peracetic acid",

author = "Yoo, {Hah Young} and Lee, {Ja Hyun} and Suh, {Young Joon} and Kim, {Sung Bong} and Park, {Seung Moon} and Kim, {Seung Wook}",

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AU - Yoo, Hah Young

AU - Lee, Ja Hyun

AU - Suh, Young Joon

AU - Kim, Sung Bong

AU - Park, Seung Moon

AU - Kim, Seung Wook

PY - 2014/11

Y1 - 2014/11

N2 - In the previous work, acetyl xylan esterase (AXE) of Aspergillus ficcum was successfully produced in Pichia pastoris as host. In this study, the recombinant AXE was immobilized on graphite oxide and used for the production of peracetic acid. Immobilization efficiency was enhanced by modifying graphite oxide via surface functionalization. The conditions for enzyme immobilization were also investigated and the optimal conditions were determined as 4℃ of temperature, 24 h of reaction time and pH 7. The activity of immobilized AXE was found to be 62.53 U/g-support. With the immobilized AXE, about 134 mM of peracetic acid was produced under 37℃ of temperature and 30 min of reaction time. Enzyme activity remained at > 50% of the original after 10 production cycles.

AB - In the previous work, acetyl xylan esterase (AXE) of Aspergillus ficcum was successfully produced in Pichia pastoris as host. In this study, the recombinant AXE was immobilized on graphite oxide and used for the production of peracetic acid. Immobilization efficiency was enhanced by modifying graphite oxide via surface functionalization. The conditions for enzyme immobilization were also investigated and the optimal conditions were determined as 4℃ of temperature, 24 h of reaction time and pH 7. The activity of immobilized AXE was found to be 62.53 U/g-support. With the immobilized AXE, about 134 mM of peracetic acid was produced under 37℃ of temperature and 30 min of reaction time. Enzyme activity remained at > 50% of the original after 10 production cycles.

KW - acetyl xylan esterase

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KW - graphite oxide

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Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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