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Immobilization of acetyl xylan esterase on modified graphite oxide and utilization to peracetic acid production
- Source :
- Biotechnology and Bioprocess Engineering. 19:1042-1047
- Publication Year :
- 2014
- Publisher :
- Springer Science and Business Media LLC, 2014.
-
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.
- Subjects :
- biology
Immobilized enzyme
Biomedical Engineering
Bioengineering
Graphite oxide
biology.organism_classification
Applied Microbiology and Biotechnology
Enzyme assay
Pichia pastoris
law.invention
chemistry.chemical_compound
chemistry
law
Peracetic acid
Recombinant DNA
biology.protein
Surface modification
Organic chemistry
Industrial and production engineering
Biotechnology
Nuclear chemistry
Subjects
Details
- ISSN :
- 19763816 and 12268372
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Biotechnology and Bioprocess Engineering
- Accession number :
- edsair.doi...........7b54f8124f1c53b94c3844bbe8505fa1