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Building blocks for polymer synthesis by enzymatic catalysis
KTH, School of Biotechnology (BIO), Industrial Biotechnology.ORCID iD: 0000-0003-2644-0752
2017 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The search for alternatives to oil-based monomers has sparked interest for scientists to focus on the use of renewable resources for energy production, for the synthesis of polymeric materials and in other areas. With the use of renewable resources, scientists face new challenges to first isolate interesting molecules and then to process them.

Enzymes are nature’s own powerful catalysts and display a variety of activities. They regulate important functions in life. They can also be used for chemical synthesis due to their efficiency, selectivity and mild reaction conditions. The selectivity of the enzyme allows specific reactions enabling the design of building blocks for polymers.

In the work presented here, a lipase (Candida antarctica lipase B (CalB)) was used to produce building blocks for polymers. An efficient route was developed to selectively process epoxy-functional fatty acids into resins with a variety of functional groups (maleimide, oxetane, thiol, methacrylate). These oligoester structures, based on epoxy fatty acids from birch bark and vegetable oils, could be selectively cured to form thermosets with tailored properties.

The specificity of an esterase with acyl transfer activity from Mycobacterium smegmatis (MsAcT) was altered by rational design. The produced variants increased the substrate scope and were then used to synthesize amides in water, where the wild type showed no conversion. A synthetic procedure was developed to form mixed dicarboxylic esters by selectively reacting only one side of divinyl adipate in order to introduce additional functional groups.

Place, publisher, year, edition, pages
Stockholm: KTH Royal Institute of Technology, 2017. , p. 61
Series
TRITA-BIO-Report, ISSN 1654-2312 ; 2017:15
Keywords [en]
Enzyme, Enzyme Engineering, Biocatalysis, Lipase, CalB, MsAcT, Substrate specificity, Selectivity, Polymer Chemistry, Polymer Synthesis
National Category
Biocatalysis and Enzyme Technology
Research subject
Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-212499ISBN: 978-91-7729-494-8 (print)OAI: oai:DiVA.org:kth-212499DiVA, id: diva2:1135110
Public defence
2017-09-22, Kollegiesalen, Brinellvägen 8, Stockholm, 10:00
Opponent
Supervisors
Note

QC 20170823

Available from: 2017-08-23 Created: 2017-08-22 Last updated: 2017-08-23Bibliographically approved
List of papers
1. Enzymatic catalysis as a versatile tool for the synthesis of multifunctional, bio-based oligoester resins
Open this publication in new window or tab >>Enzymatic catalysis as a versatile tool for the synthesis of multifunctional, bio-based oligoester resins
2016 (English)In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270, Vol. 18, no 7, p. 1923-1929Article in journal (Refereed) Published
Abstract [en]

The use of enzymes as selective catalysts for processing renewable monomers into added value polymers and materials has received increased attention during the last decade. In the present work Candida antarctica lipase B (CalB) was used as catalyst in one-pot routes to synthesise multifunctional oligoester resins based on an epoxy-functional omega-hydroxy-fatty acid (EFA) extracted from birch bark. The chemoselective enzymatic process resulted in three different EFA-based telechelic oligomers with targeted molecular weights; containing maleimide, methacrylate or oxetane as end-groups, respectively. The enzyme catalysed synthesis of the maleimide and the oxetane telechelic oligomers reached full conversion of monomers (>95%) after 2 h. In the case of methacrylate functional oligomer the EFA monomer reached full conversion (>98%) after 2 h but the integration of the methacrylate moiety took more than 10 h. This was due to a rate limiting reaction path using ethylene glycol dimethacrylate as substrate. The oligomer products were characterised by NMR, MALDI-TOF-MS and SEC.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2016
Keywords
Ring-Opening Polymerization, Suberin Monomer, Lipase, Polyesters, Route, Chemistry, Polymers, Acids, Bark
National Category
Polymer Chemistry
Identifiers
urn:nbn:se:kth:diva-185665 (URN)10.1039/c5gc02597d (DOI)000372981400012 ()2-s2.0-84962377189 (Scopus ID)
Funder
EU, FP7, Seventh Framework Programme, 289253
Note

QC 20160426

Available from: 2016-04-26 Created: 2016-04-25 Last updated: 2018-04-11Bibliographically approved
2. Polymer Thermosets from Multifunctional Polyester Resins Based on Renewable Monomers
Open this publication in new window or tab >>Polymer Thermosets from Multifunctional Polyester Resins Based on Renewable Monomers
2014 (English)In: Macromolecular Chemistry and Physics, ISSN 1022-1352, E-ISSN 1521-3935, Vol. 215, no 22, p. 2198-2206Article in journal (Refereed) Published
Abstract [en]

The use of monomers based on natural materials as a future supply of raw materials has gained more interest in the last decade. Sources ranging from wood to plant oils and algae are exploited as alternatives to traditional fossil-based resources for the synthesis of polymeric materials. The use of these raw materials is not only of interest because of its abundance, but also in terms of price, durability, and/or biodegradability. In the present study, a series of resins utilizing a monomer derived from birch bark is prepared. The thermoset resins are formed by reacting an epoxy-functional omega-hydroxy fatty acid with methacrylate monomers using enzyme catalysis to form multifunctional resins via a one-pot synthesis. The derived oligomers are crosslinked through different polymerization routes to produce thermosets with different properties and/or functionalities. This approach allows natural-based resins with tuned functionalities and mechanical and thermal properties to be obtained.

Keywords
dual curing, enzymatic catalysis, renewable monomers, suberin
National Category
Polymer Technologies
Identifiers
urn:nbn:se:kth:diva-158419 (URN)10.1002/macp.201400192 (DOI)000345444200006 ()2-s2.0-84913620344 (Scopus ID)
Note

QC 20150107

Available from: 2015-01-07 Created: 2015-01-07 Last updated: 2017-12-05Bibliographically approved
3. One-pot enzyme-catalyzed synthesis of dual-functional polyester macromers towards surface active hydrophobic films
Open this publication in new window or tab >>One-pot enzyme-catalyzed synthesis of dual-functional polyester macromers towards surface active hydrophobic films
(English)Manuscript (preprint) (Other academic)
Abstract [en]

Selective enzyme catalysis is a valuable tool for the processing of monomers into value-added materials. In the present study natural resources were used to retrieve an ω-hydroxy fatty acid monomer containing an epoxide functionality. A procedure was developed for the synthesis of dual-functional oligomers by utilizing lipase catalysis in a one-pot synthesis route. The chemoselectivity of the enzyme allowed addition of thiol monomers to the retrieved epoxy monomers, without harming the epoxides, achieving a thiol-epoxy functional polyester resin. The synthesis reached full conversion (>99 %) after 8 h. It was possible to selectively crosslink the resin, through UV-initiated cationic polymerization of the epoxides into thiol-functional thermosets. The curing performance was followed in situ by Real-Time FTIR. The thiol groups on the surface of the film were accessible for post-modification.

National Category
Polymer Chemistry Biocatalysis and Enzyme Technology
Research subject
Chemistry; Biotechnology
Identifiers
urn:nbn:se:kth:diva-212428 (URN)
Note

QC 20170822

Available from: 2017-08-21 Created: 2017-08-21 Last updated: 2017-08-23Bibliographically approved
4. Engineering the esterase/acyltransferase from Mycobacterium smegmatis: extended substrate scope for amide synthesis in water
Open this publication in new window or tab >>Engineering the esterase/acyltransferase from Mycobacterium smegmatis: extended substrate scope for amide synthesis in water
(English)Manuscript (preprint) (Other academic)
Abstract [en]

Some esterases/lipases display high acyl transfer activity, favoring alcoholysis over hydrolysis, which make them valuable catalysts for synthesis reactions in aqueous media. An esterase from Mycobacterium smegmatis, MsAcT, has been characterized as an efficient catalyst for ester synthesis in water. The acyl donor specificity for MsAcT was however found to be very narrow and the enzyme displayed no activity towards esters with larger acyl group than butyrate. With rational engineering, the narrow acyl donor specificity of wild type MsAcT enzyme was altered and variants displaying extended substrate scope were generated. A double mutant, T93A/F154A, could accommodate methyl nonanoate as substrate, i.e. five carbons longer acyl group as compared to wild type, without compromising the acyl transfer capabilities. With similar selectivity towards a broad range of acyl donors (propionate to nonanoate) this is a more applicable catalyst than the wild type. Furthermore, the T93A/F154A variant was an efficient catalyst for synthesis of N-benzylhexanamide in water using methyl hexanoate as acyl donor, which is not a substrate for the wild type enzyme. The conversion reached 81% and the enzyme variant could potentially be used to produce amides in water with a wide variety of acyl donors.

National Category
Biocatalysis and Enzyme Technology
Research subject
Biotechnology
Identifiers
urn:nbn:se:kth:diva-196890 (URN)
Note

QC 20161129

Available from: 2016-11-24 Created: 2016-11-24 Last updated: 2017-08-23Bibliographically approved
5. Mixed vinyl adipate esters through selective synthesis using a designed esterase/acyltransferase
Open this publication in new window or tab >>Mixed vinyl adipate esters through selective synthesis using a designed esterase/acyltransferase
(English)Manuscript (preprint) (Other academic)
Abstract [en]

Methods for selective syntheses of mixed dicarboxylic esters from symmetrical diesters are of great interest. An esterase from Mycobacterium smegmatis, MsAcT, has shown to be an efficient catalyst for acyl transfer reactions using both alcohols and amines. It has a restricted active site resulting in a narrow acyl donor specificity. This limitation was used for the development of a selective synthesis of mixed vinyl adipate esters from divinyl adipate. The single mutant, L12A, achieved over 90% conversion of divinyl adipate with three different alcohols leading to the corresponding mixed vinyl adipate esters. This method allows the synthesis of vinyladipoyl esters at mild reaction conditions.

National Category
Biocatalysis and Enzyme Technology
Research subject
Biotechnology
Identifiers
urn:nbn:se:kth:diva-212430 (URN)
Note

QC 20170822

Available from: 2017-08-21 Created: 2017-08-21 Last updated: 2017-08-22Bibliographically approved

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