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Integrated Heterogeneous Metal/Enzymatic Multiple Relay Catalysis for Eco-Friendly and Asymmetric Synthesis
Mid Sweden University.
KTH, School of Biotechnology (BIO), Industrial Biotechnology.
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2016 (English)In: ACS Catalysis, ISSN 2155-5435, E-ISSN 2155-5435, Vol. 6, 3932-3940 p.Article in journal (Refereed) Published
Resource type
Text
Abstract [en]

Organic synthesis is in general performed using stepwise transformations where isolation and purification of key intermediates is often required prior to further reactions. Herein we disclose the concept of integrated heterogeneous metal/enzymatic multiple relay catalysis for eco-friendly and asymmetric synthesis of valuable molecules (e.g., amines and amides) in one-pot using a combination of heterogeneous metal and enzyme catalysts. Here reagents, catalysts, and different conditions can be introduced throughout the one-pot procedure involving multistep catalytic tandem operations. Several novel cocatalytic relay sequences (reductive amination/amidation, aerobic oxidation/reductive amination/amidation, reductive amination/kinetic resolution and reductive amination/dynamic kinetic resolution) were developed. They were next applied to the direct synthesis of various biologically and optically active amines or amides in one-pot from simple aldehydes, ketones, or alcohols, respectively.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2016. Vol. 6, 3932-3940 p.
Keyword [en]
heterogeneous metal, enzyme, reductive amination, relay catalysis, heterogeneous catalysis, tandem reactions, kinetic resolution, dynamic kinetic resolution
National Category
Organic Chemistry
Research subject
Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-187377DOI: 10.1021/acscatal.6b01031ISI: 000377326700066Scopus ID: 2-s2.0-84973911460OAI: oai:DiVA.org:kth-187377DiVA: diva2:930082
Note

QC 20160623

Available from: 2016-05-22 Created: 2016-05-22 Last updated: 2017-01-12Bibliographically approved
In thesis
1. Amine Transaminases in Multi-Step One-Pot Reactions
Open this publication in new window or tab >>Amine Transaminases in Multi-Step One-Pot Reactions
2017 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Amine transaminases are enzymes that catalyze the mild and selective formation of primary amines, which are useful building blocks for biologically active compounds and natural products. In order to make the production of these kinds of compounds more efficient from both a practical and an environmental point of view, amine transaminases were incorporated into multi-step one-pot reactions. With this kind of methodology there is no need for isolation of intermediates, and thus unnecessary work-up steps can be omitted and formation of waste is prevented. Amine transaminases were successfully combined with other enzymes for multi-step synthesis of valuable products: With ketoreductases all four diastereomers of a 1,3-amino alcohol could be obtained, and the use of a lipase allowed for the synthesis of natural products in the form of capsaicinoids. Amine transaminases were also successfully combined with metal catalysts based on palladium or copper. This methodology allowed for the amination of alcohols and the synthesis of chiral amines such as the pharmaceutical compound Rivastigmine. These examples show that the use of amine transaminases in multi-step one-pot reactions is possible, and hopefully this concept can be further developed and applied to make industrial processes more sustainable and efficient in the future.

Place, publisher, year, edition, pages
Stockholm: KTH Royal Institute of Technology, 2017. 58 p.
Series
TRITA-BIO-Report, ISSN 1654-2312 ; 2017:3
Keyword
Biocatalysis, enzyme, amine transaminase, ω-transaminase, amination, primary amine, chiral amine, chemoenzymatic, green chemistry, synthesis, cascade
National Category
Biochemistry and Molecular Biology
Research subject
Biotechnology
Identifiers
urn:nbn:se:kth:diva-199646 (URN)978-91-7729-254-8 (ISBN)
Public defence
2017-02-17, Kollegiesalen, Brinellvägen 8, KTH, 10:00 (English)
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Supervisors
Note

QC 20170113

Available from: 2017-01-13 Created: 2017-01-12 Last updated: 2017-01-13Bibliographically approved

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Publisher's full textScopushttp://dx.doi.org/10.1021/acscatal.6b01031

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