Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)

The application of biocatalyst in microfluidic systems has attracted huge attention in recent years due to their potential for creating microscale analytical tools with small volumes, high-throughput and attractive prospect for mass production. This system can be integrated with the multi-step enz...

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Main Authors:	Abdul Halim, Amanatuzzakiah, Baganz, Frank
Format:	Conference or Workshop Item
Language:	English
Published:	Kulliyah of Engineering, International Islamic University Malaysia 2016
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/52183/ http://irep.iium.edu.my/52183/ http://irep.iium.edu.my/52183/1/52183.pdf

id	iium-52183
recordtype	eprints
spelling	iium-521832016-10-13T08:35:29Z http://irep.iium.edu.my/52183/ Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR) Abdul Halim, Amanatuzzakiah Baganz, Frank TP248.13 Biotechnology The application of biocatalyst in microfluidic systems has attracted huge attention in recent years due to their potential for creating microscale analytical tools with small volumes, high-throughput and attractive prospect for mass production. This system can be integrated with the multi-step enzyme reaction to synthesize complex organic compounds such as a single diastereoisomer of 2-amino-1,3,4-butanetriol (ABT). ABT is an interesting compound, commonly used as the building block in several pharmaceutical syntheses. In this work we study a de novo designed pathway for the production of ABT using IEMRs, which is based on the reversible attachment of His6-tagged enzymes via Ni-NTA agarose beads that are packed into tubes to enable continuous flow of multi-step enzyme reactions. The synthesis of ABT was demonstrated in a three-step enzyme reaction using two enzymes; transketolase and transaminase. In the first part of the three-step reaction, His6-TAm catalysed the conversion of the substrates, serine (SER) and glycoaldehyde (GA), to form lithium-hydroxypyruvate (HPA). The product of the first reaction was then continuously fed to the second IEMR containing the immobilized His6-TK, which catalysed the reaction between HPA and GA into erythrulose (ERY). The multi-step reaction was completed with the amination of ERY by the second His6- TAm to produce the final target product, ABT. Kulliyah of Engineering, International Islamic University Malaysia 2016 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/52183/1/52183.pdf Abdul Halim, Amanatuzzakiah and Baganz, Frank (2016) Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR). In: 4th International Conference on Biotechnology Engineering 2016 (ICBioE 2016), 25th-27th July 2016, Kuala Lumpur. http://www.iium.edu.my/icbioe/2016/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Abdul Halim, Amanatuzzakiah Baganz, Frank Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
description	The application of biocatalyst in microfluidic systems has attracted huge attention in recent years due to their potential for creating microscale analytical tools with small volumes, high-throughput and attractive prospect for mass production. This system can be integrated with the multi-step enzyme reaction to synthesize complex organic compounds such as a single diastereoisomer of 2-amino-1,3,4-butanetriol (ABT). ABT is an interesting compound, commonly used as the building block in several pharmaceutical syntheses. In this work we study a de novo designed pathway for the production of ABT using IEMRs, which is based on the reversible attachment of His6-tagged enzymes via Ni-NTA agarose beads that are packed into tubes to enable continuous flow of multi-step enzyme reactions. The synthesis of ABT was demonstrated in a three-step enzyme reaction using two enzymes; transketolase and transaminase. In the first part of the three-step reaction, His6-TAm catalysed the conversion of the substrates, serine (SER) and glycoaldehyde (GA), to form lithium-hydroxypyruvate (HPA). The product of the first reaction was then continuously fed to the second IEMR containing the immobilized His6-TK, which catalysed the reaction between HPA and GA into erythrulose (ERY). The multi-step reaction was completed with the amination of ERY by the second His6- TAm to produce the final target product, ABT.
format	Conference or Workshop Item
author	Abdul Halim, Amanatuzzakiah Baganz, Frank
author_facet	Abdul Halim, Amanatuzzakiah Baganz, Frank
author_sort	Abdul Halim, Amanatuzzakiah
title	Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
title_short	Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
title_full	Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
title_fullStr	Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
title_full_unstemmed	Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)
title_sort	multi-step enzyme reaction in an immobilized enzyme microreactor (iemr)
publisher	Kulliyah of Engineering, International Islamic University Malaysia
publishDate	2016
url	http://irep.iium.edu.my/52183/ http://irep.iium.edu.my/52183/ http://irep.iium.edu.my/52183/1/52183.pdf
first_indexed	2023-09-18T21:13:58Z
last_indexed	2023-09-18T21:13:58Z
_version_	1777411438746271744

Multi-step enzyme reaction in an Immobilized Enzyme Microreactor (IEMR)

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