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 journalArticle

5 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 languageEnglish
Pages (from-to)1042-1047
Number of pages6
JournalBiotechnology and Bioprocess Engineering
Volume19
Issue number6
DOIs
Publication statusPublished - 2015 Jan 1

Fingerprint

acetylxylan esterase
Peracetic Acid
Graphite
Immobilization
Oxides
Acids
Enzyme immobilization
Temperature
Pichia
Aspergillus
Enzyme activity
Enzymes
Esterases
Xylans

Keywords

  • acetyl xylan esterase
  • enzyme immobilization
  • graphite oxide
  • peracetic acid

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering
  • Bioengineering

Cite this

Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production. / Yoo, Hah Young; Lee, Ja Hyun; Suh, Young Joon; Kim, Sung Bong; Park, Seung Moon; Kim, Seung Wook.

In: Biotechnology and Bioprocess Engineering, Vol. 19, No. 6, 01.01.2015, p. 1042-1047.

Research output: Contribution to journalArticle

Yoo, Hah Young ; Lee, Ja Hyun ; Suh, Young Joon ; Kim, Sung Bong ; Park, Seung Moon ; Kim, Seung Wook. / Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production. In: Biotechnology and Bioprocess Engineering. 2015 ; Vol. 19, No. 6. pp. 1042-1047.
@article{6213112064384d4db5427ca00009acfd,
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}",
year = "2015",
month = "1",
day = "1",
doi = "10.1007/s12257-014-0298-8",
language = "English",
volume = "19",
pages = "1042--1047",
journal = "Biotechnology and Bioprocess Engineering",
issn = "1226-8372",
publisher = "Korean Society for Biotechnology and Bioengineering",
number = "6",

}

TY - JOUR

T1 - Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production

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 - 2015/1/1

Y1 - 2015/1/1

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

KW - enzyme immobilization

KW - graphite oxide

KW - peracetic acid

UR - http://www.scopus.com/inward/record.url?scp=84921038537&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84921038537&partnerID=8YFLogxK

U2 - 10.1007/s12257-014-0298-8

DO - 10.1007/s12257-014-0298-8

M3 - Article

AN - SCOPUS:84921038537

VL - 19

SP - 1042

EP - 1047

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

SN - 1226-8372

IS - 6

ER -