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

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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.

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Authors and Affiliations

  1. Department of Chemical and Biological Engineering, Korea University, Seoul, 136-701, Korea

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

  2. Divison of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Jeonju, 570-752, Korea

    Seung-Moon Park

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  1. Hah Young Yoo
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  2. Ja Hyun Lee
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  3. Young Joon Suh
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  4. Sung Bong Kim
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  5. Seung-Moon Park
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  6. Seung Wook Kim
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Correspondence to Seung Wook Kim.

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These two author’s contributed equally to this work.

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Yoo, H.Y., Lee, J.H., Suh, Y.J. et al. Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production. Biotechnol Bioproc E 19, 1042–1047 (2014). https://doi.org/10.1007/s12257-014-0298-8

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  • DOI: https://doi.org/10.1007/s12257-014-0298-8

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