Whole-Cell Photoenzymatic Cascades to Synthesize Long-Chain Aliphatic Amines and Esters from Renewable Fatty Acids

Article abstract of DOI:10.1002/anie.201915108

Long-chain aliphatic amines such as (S,Z)-heptadec-9-en-7-amine and 9-aminoheptadecane were synthesized from ricinoleic acid and oleic acid, respectively, by whole-cell cascade reactions using the combination of an alcohol dehydrogenase (ADH) from Micrococcus luteus, an engineered amine transaminase from Vibrio fluvialis (Vf-ATA), and a photoactivated decarboxylase from Chlorella variabilis NC64A (Cv-FAP) in a one-pot process. In addition, long chain aliphatic esters such as 10-(heptanoyloxy)dec-8-ene and octylnonanoate were prepared from ricinoleic acid and oleic acid, respectively, by using the combination of the ADH, a Baeyer–Villiger monooxygenase variant from Pseudomonas putida KT2440, and the Cv-FAP. The target compounds were produced at rates of up to 37 U g^?1 dry cells with conversions up to 90 %. Therefore, this study contributes to the preparation of industrially relevant long-chain aliphatic chiral amines and esters from renewable fatty acid resources.

Full text of DOI:10.1002/anie.201915108

A Journal of the Gesellschaft Deutscher Chemiker
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Accepted Article
Title: Whole-Cell Photoenzymatic Cascades to Synthesize Long Chain
Aliphatic Amines and Esters from Renewable Fatty Acids
Authors: Hee-Jeong Cha, Se-Yeun Hwang, Da-Som Lee, Ravi Kumar
Akula, Yong-Uk Kwon, Moritz Voß, Eva Schuiten, Uwe
Bornscheuer, Frank Hollmann, Deok-Kun Oh, and Jin-Byung
Park
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To be cited as: Angew. Chem. Int. Ed. 10.1002/anie.201915108
Angew. Chem. 10.1002/ange.201915108
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http://dx.doi.org/10.1002/ange.201915108

10.1002/anie.201915108
Angewandte Chemie International Edition
RESEARCH ARTICLE
Whole-Cell Photoenzymatic Cascades to Synthesize Long Chain
Aliphatic Amines and Esters from Renewable Fatty Acids
Hee-Jeong Cha,[a] Se-Yeun Hwang,[a] Da-Som Lee,[a] Ravi Kumar Akula,[a,b] Yong-Uk Kwon,[b] Moritz
Voß,[c] Eva Schuiten,[c] Uwe T. Bornscheuer,[c] Frank Hollmann,*[d] Deok-Kun Oh,*[e] and Jin-Byung
Park*[a]
Abstract: Long chain aliphatic amines such as (S,Z)-heptadec-9-en-
7-amine and 9-aminoheptadecane were synthesized from ricinoleic
acid and oleic acid, respectively, by whole-cell cascade reactions
using the combination of an alcohol dehydrogenase (ADH) from
Micrococcus luteus, an engineered amine transaminase from Vibrio
synthesis of a variety of chemicals ranging from cosmetic esters
to performance additives.[1] For instance, hydroxy fatty acids
serve as starting materials to manufacture flavors, resins, waxes,
lubricants, polymers and as additives in coatings and
paintings.[1b, 2] More recently, hydroxy fatty acids have been used
as starting materials in multi-enzyme cascades combining
alcohol dehydrogenases (ADH) and amine transaminases (ATA)
(Scheme S1).[3] The hydroxyl group can also be converted in a
sequence of ADH-catalyzed oxidation followed by a Baeyer-
Villiger monooxygenase (BVMO)-step; the resulting esters are
hydrolyzed into alkanoic acids and ω-hydroxy fatty acids by an
esterase.[4] The ω-hydroxy fatty acids can be oxidized into α,ω-
dicarboxylic acids by an alcohol/aldehyde dehydrogenase[5] or
converted into ω-amino fatty acids by an ADH and ω-
fluvialis (Vf-ATA), and
a photoactivated decarboxylase from
Chlorella variabilis NC64A (Cv-FAP) in a one-pot process. In
addition, long chain aliphatic esters such as 10-(heptanoyloxy)dec-8-
ene and octylnonanoate were prepared from ricinoleic acid and oleic
acid, respectively, by using the combination of the ADH, a Baeyer-
Villiger monooxygenase variant from Pseudomonas putida KT2440,
and the Cv-FAP. The target compounds were produced at rates of
up to 37 U/g dry cells with conversions up to 90%. Therefore, this
study contributes to the preparation of industrially relevant long chain
aliphatic chiral amines and esters from renewable fatty acid
resources.
6]
transaminase.[5d, Further synthetic possibilities comprise the
transformation into α,ω-diols by combined reduction through
carboxylic acid reductases and ADHs[7] or into α,ω-diamines
using carboxylic acid reductases, ADHs and ω-transaminase.[6]
Another promising transformation of fatty acids includes the
decarboxylation to the corresponding, C-1 shortened alkanes
(Scheme S1). Established chemical methods, however, rely on
rather harsh reaction conditions[8] under which additional
functional groups are unlikely to remain un-altered. A very
promising solution to this challenge was reported recently by
Beisson and coworkers.[9] The photodecarboxylase from the
algae Chlorella variabilis NC64A (Cv-FAP) catalyzes the
selective, light-driven decarboxylation of (fatty) acids[10] and
thereby possibly expands the scope of products derived from
renewable oleochemicals significantly.
Introduction
There is an increasing demand for the preparation of chemical
building blocks from biomass-derived starting materials.
Renewable oils and fatty acids are particularly interesting
because they are abundant in nature and can be derived from
non-edible sources. Oils and fatty acids are already used for the
[a]
H.-J. Cha, S.-Y. Hwang, D.-S. Lee, Dr. A. R. Kumar, Prof. Dr. J.-B.
Park
In this study, a novel fatty acid biotransformation pathway was
investigated to produce long chain aliphatic amines and esters
from renewable fatty acids, which can be used as active
ingredients in cosmetic formulations and performance additives
in oleochemicals.[1b, 1c, 2b] For instance, the biotransformation of
ricinoleic acid (1) into (S,Z)-heptadec-9-en-7-amine (5) and 10-
Department of Food Science & Engineering
Ewha Womans University
Seoul 03760 (Republic of Korea)
E-mail: jbpark06@ewha.ac.kr
Dr. A. R. Kumar, Prof. Dr. Y.-U Kwon
Department of Chemistry and Nanoscience
Ewha Womans University
Seoul 03760 (Republic of Korea)
M. Voß, E. Schuiten, Prof. Dr. U. T. Bornscheuer
Institute of Biochemistry
[b]
[c]
[d]
(heptanoyloxy)dec-8-ene
(7)
(Scheme
1)
and
the
biotransformation of oleic acid ((Z)-octadec-9-enoic acid (10))
into 9-aminoheptadecane (14) and octylnonanoate (16)
(Scheme 2) were investigated by using Cv-FAP as a key
enzyme.
Department of Biotechnology & Enzyme Catalysis
Greifswald University, 17487 Greifswald (Germany)
Prof. Dr. F. Hollmann
Department of Biotechnology
Delft University of Technology
Van der Maasweg 9, 2629HZ Delft (The Netherlands)
E-mail: f.hollmann@tudelft.nl
Prof. Dr. D.-K. Oh
Results and Discussion
[e]
Department of Bioscience and Biotechnology
Konkuk University
Seoul 05029 (Republic of Korea)
E-mail: deokkun@konkuk.ac.kr
In a first set of experiments we created an Escherichia coli-
based whole cell catalyst expressing Cv-FAP and tested it for
the transformation of ricinoleic acid (1) into (Z)-heptadec-9-en-7-
ol (2) (Scheme 1).
Supporting information for this article is given via a link at the end of
the document.
This article is protected by copyright. All rights reserved.

10.1002/anie.201915108
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RESEARCH ARTICLE
Next, we aimed at the conversion of ricinoleic acid (1) into
(S,Z)-heptadec-9-en-7-amine (5) (Cascade 1, Figure 2). For this,
we used a previously reported recombinant E. coli system (Cat-
3)[3] comprising a secondary alcohol dehydrogenase (sADH)
with a transaminase (Vf-ATA_H3-RA) and the long chain fatty acid
transporter (FadL) with the aforementioned Cat-1. Though the
transformation proceeded smoothly to full conversion (Figure
S4a), the enantiomeric purity of the desired (S,Z)-heptadec-9-
en-7-amine (5) was disappointingly low (27% ee, Scheme S3
and Figure S5). Therefore, Vf-ATA_H3-RA was subjected to
structure-based
rational
engineering
to
improve
its
enantioselectivity. Substrate docking revealed that Lysine 163
may play a crucial role (Figure S6). Indeed, substitution of this
amino acid by aspartic acid (Vf-ATA_H3-RA_K163D) resulted in a
more active and more enantioselective (71% ee) catalyst (Cat-4)
(Table S2 and Figure S4b). Overall, using the combination of
Cat-1 and Cat-4 yielded in 78% conversion of ricinoleic acid (1)
into (S,Z)-heptadec-9-en-7-amine (5) (71% ee, Table 2).
Scheme 1. Cascades for the transformation of ricinoleic acid (1) into
secondary fatty alcohols (2) or amines (5), fatty acid esters (7) or the
5b, 11]
corresponding acids (8) and alcohol (9).[3,
Details about the catalysts
used can be found in Table 2.
(4)
(1)
(3)
(5)
5
4
3
2
1
0
0
1
2
3
time [h]
Figure 1. Biotransformation of ricinoleic acid (1, , ) into (Z)-heptadec-9-en-
7-ol (2, , ) using Cat-1 (closed symbols) or Cat-2 (open symbols).
Conditions: c(1) = 10 mM, c(Cat-1) or c(Cat-2) = 3.6 gCDW L-1, illumination with
blue light (=450 nm).
Figure 2. Cascade-1: Biotransformation of ricinoleic acid (1, ) into (S,Z)-
heptadec-9-en-7-amine (5, ) via (Z)-12-oxooctadec-9-enoic acid (3, ) and
(S,Z)-12-aminooctadec-9-enoic acid (4, ). Conditions: c(1) = 5 mM, c(Cat-1)
= 3.6 gCDW L-1, c(Cat-4) = 7.2 gCDW L-1, c(methyl benzyl amine) = 10 mM,
illumination with blue light (=450 nm) was initiated at t = 2h.
Since the expression level of a long chain fatty acid
transporter (FadL) in E. coli had previously been shown
accelerate whole-cell biotransformation rates of long chain fatty
acids,[1f, 12] two types of E. coli-based biocatalysts (Cat-1 and
Cat-2 (Table 2)) were constructed. Cat-1 is the recombinant E.
coli expressing the Cv-FAP in the cytoplasm while Cat-2 is the
recombinant E. coli expressing Cv-FAP in the cytoplasm and
FadL in the outer membrane.
It is worth noting, that at the time the illumination was
initiated not all starting material had been converted into (S,Z)-
12-aminooctadec-9-enoic acid (4), therefore, also trace amounts
of the decarboxylation products of the non-reacted starting
material and intermediate were observed (Figure 2, symbols
).
In another example we evaluated the conversion of ricinoleic
acid (1) to (Z)-10-(heptanoyloxy)dec-8-ene (7) (Cascade 2,
Figure 3). For this Cat-1 and Cat-5 were combined. The latter
comprised recombinant E. coli expressing the FadL[4, 12-13], sADH
Cat-1 completely converted ricinoleic acid (1) into (Z)-
heptadec-9-en-7-ol (2) within only 15 min (Figure 1 and Figure
S1). The transformation took significantly longer (30 min) using
Cat-2 under otherwise identical conditions (Figure 1 오류! 참조
원본을 찾을 수 없습니다.). Similar observations were also made
for the transformations of oleic acid and linoleic acid (Figure S2).
The lower rates might be due to a negative impact of the
expression of FadL on the Cv-FAP expression (Figure S3).
Therefore, we used Cat-1 as chassis for all further catalyst
designs.
and
Pseudomonas
a
Baeyer-Villiger
putida
monooxygenase
KT2440 (E6BVMO_C302L).
variant
from
The
biotransformation was initiated by adding ricinoleic acid (1, 15
mM) to the culture broth of Cat-5 (Figure 3). After 8 h the
transformation of ricinoleic acid into 11-(heptanoyloxy)undec-9-
enoic acid (6) was nearly complete and Cat-1 was added and
illumination was initiated for another 4 h. 9.7 mM of the desired
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10.1002/anie.201915108
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RESEARCH ARTICLE
product (Z)-10-(heptanoyloxy)dec-8-ene (7) was obtained
(Figure 3 and Figure S8a). The overall isolated yield from
ricinoleic acid was 52% with a purity of 92% (Figure S8b). Upon
addition of the esterase from Pseudomonas fluorescens SIK WI
(Pf-Esterase) the ester product (7) could also be hydrolyzed into
n-heptanoic acid (8) and 2-decen-1-ol (9) from the ester
compound (7) (Scheme 1 and Figure S8c).
Combining Cat-6 with Cat-1 enabled us to transform oleic
acid (10, 5.2 mM) into 9-aminoheptadecane (14) (Cascade 3,
Figure 4a). In contrast to Cascade 1, the amine donor for the
reductive amination step could not be added from the beginning
of the reaction as it severely inhibited OhyA.[3] Nevertheless, the
target product 9-aminoheptadecane (14) was obtained in an
overall 58% conversion (at 3 mM).
Finally, we performed the transformation of oleic acid (10,
10.5 mM) into octylnonanoate (16) (Cascade 4, Figure 4b).
Using a combination of Cat-7 and Cat-1, octylnonanoate (16)
was obtained at an overall conversion of 69 % (7.2 mM) from
oleic acid (Table 2). The ester (16) was isolated in an overall
yield of 48% with a purity of 90% (Figure S10c). Addition of Pf-
esterase into the reaction medium resulted in complete
hydrolysis of 16 into n-nonanoic acid (17) and n-octanol (18).
a)
(10)
(11)
(12)
(13)
(14)
5
4
3
2
1
0
Figure 3. Cascade-2: Biotransformation of ricinoleic acid (1, ) into 10-
(heptanoyloxy)dec-8-ene (7, ) via (Z)-12-oxooctadec-9-enoic acid (3, ) and
11-heptanoyloxyundec-9-enoic acid (6, ). Conditions: c(1) = 15 mM, c(Cat-1)
= 3.6 gCDW L-1, c(Cat-5) = 3.6 gCDW L-1, illumination with blue light (=450 nm)
was initiated at t = 8h. Minor amounts of the decarboxylation products of 1 ()
and 3 () were observed as well.
0
2
4
6
8
10
time [h]
A key element of the transformations shown above is the
hydroxyl functionality present in ricinoleic acid. To broaden the
substrate scope, we decided to enlarge the cascades by a C=C-
double bond hydration step (Scheme 2). To achieve this, Cat-3
and Cat-5 were supplemented with a fatty acid double bond
hydratase (OhyA) from Stenotrophomonas maltophilia
generating Cat-6 and Cat-7 (Table 2).
12
10
8
b)
(12)
(10)
(11)
(15)
(16)
6
4
2
0
0
2
4
6
8
10
time [h]
Figure 4. a) Cascade-3: Biotransformation of oleic acid (10, ) into 9-
aminoheptadecane (14, ) via (R)-10-hydroxyoctadecanoic acid (11, ), 10-
oxooctadecanoic acid (12, ) and 10-aminooctadecanoic acid (13, ).
Conditions: c(10) = 5.2 mM, c(Cat-1) = 3.6 gCDW L-1, c(Cat-6) = 7.2 gCDW L-1,
illumination with blue light (=450 nm) was initiated at
t
=
6h.
b) Cascade-4: Biotransformation of oleic acid (10, ) into octylnonanoate (16,
) via (R)-10-hydroxyoctadecanoic acid (11, ), 10-oxooctadecanoic acid (12,
) and 9-(nonanoyloxy)nonanoic acid (15, ). Conditions: c(10) = 10.5 mM,
c(Cat-1) = 3.6 gCDW L-1, c(Cat-7) = 3.6 gCDW L-1, illumination with blue light
(=450 nm) was initiated at t = 7h.
Scheme 2. Cascades for the transformation of oleic acid (10) into fatty amines
(14), fatty acid esters (16) or the corresponding acids (17) and alcohol (18).[1f, 3,
5b] Details about the catalysts used can be found in Table 2.
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10.1002/anie.201915108
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RESEARCH ARTICLE
Table 1. Summary of the products obtained through the presented
photoenzymatic cascades.
Cv-FAP: photodecarboxylase from Chlorella variabilis NC64A, FadL: long
chain fatty acid transporter, sADH: secondary alcohol dehydrogenase from
Micrococcus luteus, Vf-ATA_H3-RA: amine transaminase variant from Vibrio
Cascade
Products
Final
product
[mM]
Conversion
[%]
fluvialis, Vf-ATA_H3-RA_K163D
:
the engineered Vf-ATA_H3-RA to improve
enantioselectivity, E6BVMO_C302L: engineered variant of the Baeyer-Villiger
monooxygenase from Pseudomonas putida KT2440, OhyA: fatty acid double
bond hydratase from Stenotrophomonas maltophilia. See the Table S1 for
details of the plasmids.
-
(R,Z)-heptadec-9-en-7-ol (2)
(S,Z)-heptadec-9-en-7-amine (5)
10-(heptanoyloxy)dec-8-ene (7)
9-aminoheptadecane (14)
octylnonanoate (16)
9.1
3.9
9.7
3
91
78
65
58
69
1
2
3
4
Acknowledgements
This work was supported by C1 Gas Refinery Research Center
(NRF Grant Number: 2018M3D3A1A01055735-3) of the
National Research Foundation (NRF) of Korea funded by
Ministry of Science and ICT and by the Marine Biomaterials
Research Center grant from the Marine Biotechnology Program
[No. D11013214H480000100] funded by the Ministry of Oceans
and Fisheries, Korea. F. H. gratefully acknowledges support by
The Netherlands Organisation for Scientific Research through a
VICI grant (No. 724.014.003) and the European Research
Commission (ERC consolidator grant No. 648026). U.T.B.
gratefully acknowledges support by the European Union’s
Horizon 2020 Programme (Marie-Curie Actions, grant No.
722610) and the German Research Foundation, DFG (grant
No.: BO 1862/16-1).
7.2
Experimental
A full description of the experimental procedures, analytical
details and additional experimental data can be found in the
Supporting Information.
Table 2. List of the recombinant biocatalysts used in this study.
Name
Description
Remark
Cat-1
Cat-2
E. coli BL21 (DE3)
pET28a-Cv-FAP
Photodecarboxylase (Cv-FAP)
Keywords: Enzyme catalysis • photodecarboxylase • long chain
aliphatic amines and esters • fatty acids • Escherichia coli
E. coli BL21 (DE3)
pACYC-FadL
Photodecarboxylase (Cv-FAP)
+Fatty acid transporter (FadL)
/pET28a-Cv-FAP
[1]
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Metzger, H. J. Schäfer, Angew. Chem. 2011, 123, 3938-3956, Angew.
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Cat-3
Cat-4
Cat-5
Cat-6
E. coli BL21 (DE3)
pACYC-ADH-FadL
/pET24b-Vf-ATA_H3-RA
Secondary alcohol
dehydrogenase (sADH)+Fatty
acid transporter (FadL)+
Amine transaminase (Vf-ATA_H3-
)
RA
E. coli BL21 (DE3)
pACYC-ADH-FadL
/pET24b-Vf-ATA_H3-
RA_K163D
Secondary alcohol
dehydrogenase (sADH)+Fatty
acid transporter (FadL)+
Amine transaminase (Vf-ATA_H3-
)
RA_K163D
E. coli BL21 (DE3)
pAPTm-E6BVMO_C302L
ADH /pCon-FadL
Secondary alcohol
-
dehydrogenase (sADH)+Fatty
acid transporter (FadL)+
Baeyer-Villiger monooxygenase
(E6BVMO_C302L
)
[2]
[3]
a) C. T. Hou, Handbook of industrial biocatalysis, CRC press, 2005; b)
U. Schörken, P. Kempers, Eur. J. Lipid Sci. Technol. 2009, 111, 627-
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E. coli BL21 (DE3)
pACYC-ADH-FadL-
OhyA
Secondary alcohol
dehydrogenase (sADH)+Fatty
acid transporter (FadL)+
Fatty acid hydratase
a) D. S. Lee, J. W. Song, M. Voß, E. Schuiten, R. K. Akula, Y. U. Kwon,
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(OhyA)+Amine transaminase (Vf-
ATA_H3-RA
)
Cat-7
E. coli BL21 (DE3) ΔinfA
harboring pACYC-ADH-
FadL-OhyA and
pSTAPL_E6BVMO_C302L
_M340L_Lv3
Secondary alcohol
[4]
[5]
E.-J. Seo, H.-J. Kim, M.-J. Kim, J.-S. Kim, J.-B. Park, Chem. Commun.
2019, 55, 14462-14465.
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Fatty acid hydratase
(OhyA)+Baeyer-Villiger
monooxygenase
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Adv. Synth. Catal. 2018, 360, 696-703; b) J. W. Song, E. Y. Jeon, D. H.
Song, H. Y. Jang, U. T. Bornscheuer, D. K. Oh, J. B. Park, Angew.
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J. M. Park, S.-M. Lim, C.-G. Lee, J.-B. Park, Biores. Technol. 2018, 251,
(E6BVMO_C302L_M340L
)
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Angewandte Chemie International Edition
RESEARCH ARTICLE
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10.1002/anie.201915108
Angewandte Chemie International Edition
RESEARCH ARTICLE
Entry for the Table of Contents
RESEARCH ARTICLE
Long chain aliphatic amines such as
(S,Z)-heptadec-9-en-7-amine and 9-
aminoheptadecane as well as long
chain aliphatic esters such as 10-
(heptanoyloxy)dec-8-ene and
Hee-Jeong Cha, Se-Yeun Hwang, Da-
Som Lee, Ravi Kumar Akula, Yong-Uk
Kwon, Moritz Voß, Eva Schuiten, Uwe
T. Bornscheuer, Frank Hollmann,*
Deok-Kun Oh,* & Jin-Byung Park*
octylnonanoate were prepared at high
yields from ricinoleic acid and oleic
acid by the whole-cell enzyme
cascades using a photoactivated
decarboxylase from Chlorella
Page No. – Page No.
Whole-Cell Photoenzymatic Cascade
Transformation of Renewable Fatty
Acids into Long Chain Aliphatic
Amines and Esters
variabilis NC64A (Cv-FAP) as a key
enzyme in a one-pot process.
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