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Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads

Aminoacylase I (EC 3.5.1.14) encapsulated in calcium alginate beads stabilized with poly-L-lysine was used for the production of L-phenylalanine by the hydrolysis of a racemic mixture of N-acetyl-DL-phenylalanine. The immobilized aminoacylase was studied with respect to operational stability, therma...

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Main Authors: Lee, Kong H., Lee, Pat M., Siaw, Yew S.
Format: Article
Published: Wiley 1993
Online Access:http://psasir.upm.edu.my/id/eprint/111896/
https://onlinelibrary.wiley.com/doi/10.1002/jctb.280570106
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spelling my.upm.eprints.1118962025-03-03T02:42:15Z http://psasir.upm.edu.my/id/eprint/111896/ Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads Lee, Kong H. Lee, Pat M. Siaw, Yew S. Aminoacylase I (EC 3.5.1.14) encapsulated in calcium alginate beads stabilized with poly-L-lysine was used for the production of L-phenylalanine by the hydrolysis of a racemic mixture of N-acetyl-DL-phenylalanine. The immobilized aminoacylase was studied with respect to operational stability, thermal stability, effects of pH and temperature and kinetic constants. The leakage of enzyme from the stabilized beads was eliminated. The immobilized enzyme retained high biological activity. The Km and Vmax values for the stabilized beads were 11.11 mmol dm−3 and 0.076 μmol min−1 respectively. The optimum pH and temperature for the hydrolysis were 6.5 and 55°C respectively. Scanning electron micrographs revealed crosslinked structures on the surface of the beads. The operational performances of the beads in a batch reaction and a packed-bed bioreactor for continuous reaction were investigated. With batch reaction, only about 5% of enzyme activity was lost within ten reaction cycles and there was no significant loss of activity over 600 h of continuous operation after equilibrium was reached, and a conversion yield of about 80% was obtained. Wiley 1993 Article PeerReviewed Lee, Kong H. and Lee, Pat M. and Siaw, Yew S. (1993) Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads. Journal of Chemical Technology & Biotechnology, 57 (1). pp. 27-32. ISSN 0268-2575; eISSN: 1097-4660 https://onlinelibrary.wiley.com/doi/10.1002/jctb.280570106 10.1002/jctb.280570106
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description Aminoacylase I (EC 3.5.1.14) encapsulated in calcium alginate beads stabilized with poly-L-lysine was used for the production of L-phenylalanine by the hydrolysis of a racemic mixture of N-acetyl-DL-phenylalanine. The immobilized aminoacylase was studied with respect to operational stability, thermal stability, effects of pH and temperature and kinetic constants. The leakage of enzyme from the stabilized beads was eliminated. The immobilized enzyme retained high biological activity. The Km and Vmax values for the stabilized beads were 11.11 mmol dm−3 and 0.076 μmol min−1 respectively. The optimum pH and temperature for the hydrolysis were 6.5 and 55°C respectively. Scanning electron micrographs revealed crosslinked structures on the surface of the beads. The operational performances of the beads in a batch reaction and a packed-bed bioreactor for continuous reaction were investigated. With batch reaction, only about 5% of enzyme activity was lost within ten reaction cycles and there was no significant loss of activity over 600 h of continuous operation after equilibrium was reached, and a conversion yield of about 80% was obtained.
format Article
author Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
spellingShingle Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
author_facet Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
author_sort Lee, Kong H.
title Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
title_short Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
title_full Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
title_fullStr Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
title_full_unstemmed Immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
title_sort immobilization of aminoacylase by encapsulation in poly-l-lysine-stabilized calcium alginate beads
publisher Wiley
publishDate 1993
url http://psasir.upm.edu.my/id/eprint/111896/
https://onlinelibrary.wiley.com/doi/10.1002/jctb.280570106
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score 13.244413

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