| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 69380 | Journal of Molecular Catalysis B: Enzymatic | 2015 | 5 Pages |
•Aminoacylase was immobilized on polyvinyl alcohol-based nanofibrous membranes.•The immobilized aminoacylase showed the optimal catalytic conditions at pH 8 and 52 °C.•Thermostability and storage stability of the immobilized aminoacylase were significantly improved.•The nanofibrous-immobilized aminoacylase could be used to produce pure l-theanine.
The enzyme aminoacylase was used to produce l-theanine from its derivative N-acetyl-dl-theanine. For stabilization purposes the aminoacylase was immobilized on polyvinyl alcohol-based nanofibrous membranes generated by electrospinning. The immobilized aminoacylase exhibited better resistance to changes in temperature and pH than the free enzyme with optimal conditions being pH 8 and 52 °C. Under these conditions, Km values were two to three times higher than those of the free enzyme (3.6 mM). Thermostability was also significantly improved; the activity of the immobilized enzyme was retained at approximately 70% after 6 days at 52 °C. These results indicate potential applications of nanofibrous-immobilized aminoacylase for industrial production of pure l-theanine.
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