Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase

Biocatalysis is a powerful tool for organic synthesis, especially for the synthesis of high value products such as chiral molecules and intermediates. Chiral amines can be synthesized by kinetic resolution of racemic amines or by the asymmetric synthesis from prochiral ketones. Kinetic parameter est...

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Main Authors: S. D., Vijaya Kumar, Zainatul Bahiyah, Handani, Rohana, Abu
Format: Conference or Workshop Item
Language:English
English
Published: 2019
Subjects:
Online Access:http://umpir.ump.edu.my/id/eprint/26906/1/88.%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf
http://umpir.ump.edu.my/id/eprint/26906/2/88.1%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf
http://umpir.ump.edu.my/id/eprint/26906/
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spelling my.ump.umpir.269062020-03-18T02:29:02Z http://umpir.ump.edu.my/id/eprint/26906/ Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase S. D., Vijaya Kumar Zainatul Bahiyah, Handani Rohana, Abu TP Chemical technology Biocatalysis is a powerful tool for organic synthesis, especially for the synthesis of high value products such as chiral molecules and intermediates. Chiral amines can be synthesized by kinetic resolution of racemic amines or by the asymmetric synthesis from prochiral ketones. Kinetic parameter estimation of such biocatalytic reaction is useful to evaluate process and technology options. In this research, the Michaelis–Menten kinetic parameters from the asymmetric synthesis of (R)-1-phenylethylamine from acetophenone and alanine with immobilized ω-transaminase were estimated. The immobilized ω-transaminase was prepared by entrapment with diaion beads. The kinetic parameters such as, Michaelis-Menten constant (Km) and maximum rate of reaction (Vmax) were measured using initial rate experiments by varying the substrate acetophenone concentrations (2 mM to 10 mM) at 100 mM of amino donor. The kinetic parameters were then estimated by Lineweaver-burk analysis. The Vmax and Km was estimated at 6.33 mM/min and 0.382 mM, respectively. 2019 Conference or Workshop Item PeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/26906/1/88.%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf pdf en http://umpir.ump.edu.my/id/eprint/26906/2/88.1%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf S. D., Vijaya Kumar and Zainatul Bahiyah, Handani and Rohana, Abu (2019) Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase. In: Energy Security and Chemical Engineering Congress (ESCHE2019), 17-19 July 2019 , Parkroyal Resort Penang, Malaysia. pp. 1-4.. (Unpublished)
institution Universiti Malaysia Pahang
building UMP Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Pahang
content_source UMP Institutional Repository
url_provider http://umpir.ump.edu.my/
language English
English
topic TP Chemical technology
spellingShingle TP Chemical technology
S. D., Vijaya Kumar
Zainatul Bahiyah, Handani
Rohana, Abu
Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
description Biocatalysis is a powerful tool for organic synthesis, especially for the synthesis of high value products such as chiral molecules and intermediates. Chiral amines can be synthesized by kinetic resolution of racemic amines or by the asymmetric synthesis from prochiral ketones. Kinetic parameter estimation of such biocatalytic reaction is useful to evaluate process and technology options. In this research, the Michaelis–Menten kinetic parameters from the asymmetric synthesis of (R)-1-phenylethylamine from acetophenone and alanine with immobilized ω-transaminase were estimated. The immobilized ω-transaminase was prepared by entrapment with diaion beads. The kinetic parameters such as, Michaelis-Menten constant (Km) and maximum rate of reaction (Vmax) were measured using initial rate experiments by varying the substrate acetophenone concentrations (2 mM to 10 mM) at 100 mM of amino donor. The kinetic parameters were then estimated by Lineweaver-burk analysis. The Vmax and Km was estimated at 6.33 mM/min and 0.382 mM, respectively.
format Conference or Workshop Item
author S. D., Vijaya Kumar
Zainatul Bahiyah, Handani
Rohana, Abu
author_facet S. D., Vijaya Kumar
Zainatul Bahiyah, Handani
Rohana, Abu
author_sort S. D., Vijaya Kumar
title Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
title_short Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
title_full Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
title_fullStr Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
title_full_unstemmed Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
title_sort kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
publishDate 2019
url http://umpir.ump.edu.my/id/eprint/26906/1/88.%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf
http://umpir.ump.edu.my/id/eprint/26906/2/88.1%20Kinetic%20study%20of%20asymmetric%20synthesis%20of%20chiral.pdf
http://umpir.ump.edu.my/id/eprint/26906/
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score 13.209306