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Artificial Nanometalloenzyme for Cooperative Tandem Catalysis Hui Li, Chenggang Qiu, Xun Cao, Yuanyuan Lu, Ganlu Li, Xun He, Qiuhao Lu, Kequan Chen, Pingkai Ouyang, and Weimin Tan ACS Appl. Mater. Interfaces, Just Accepted Manuscript • DOI: 10.1021/acsami.9b03616 • Publication Date (Web): 15 Apr 2019 Downloaded from http://pubs.acs.org on April 15, 2019
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ACS Applied Materials & Interfaces
Artificial Nanometalloenzyme for Cooperative Tandem Catalysis
1 2
Hui Li,†,‡ Chenggang Qiu,†,‡ Xun Cao,†,‡ Yuanyuan Lu,†,‡ Ganlu Li,†,‡ Xun He,†,‡
3
Qiuhao Lu,†,‡ Kequan Chen,*,†,‡ Pingkai Ouyang,†,‡ and Weimin Tan∥
4 5
† College
6
Nanjing, 211816, China
7
‡
8
211816, China
9
∥National
10
of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University,
State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing,
Engineering Research Center for Coatings, CNOOC Changzhou Paint and
Coatings Industry Research Institute Co., Ltd, Changzhou 213016, P.R.China
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Abstract: Artificial metalloenzymes which combine the advantages of natural
25
enzymes and metal catalysts have been getting more research attention. As a proof of
26
concept, an artificial nanometalloenzyme (CALB-Shvo@MiMBN) was prepared by
27
co-encapsulation of metallo-organic catalyst and enzyme in a soft nanocomposite
28
consisting of 2-methylimidazole, metal ion, and biosurfactant in mild reaction
29
conditions using one-pot self-assembly method. The artificial nanometalloenzyme
30
with lipase acted as the core and metallo-organic catalyst embedded in micropore
31
exhibited a spherical structure of 30-50 nm in diameter. The artificial
32
nanometalloenzyme showed high catalytic efficiency in dynamic kinetic resolution of
33
racemic primary amines or secondary alcohols, compared to one-pot catalytic reaction
34
of
35
nanometalloenzyme holds great promise for integrated enzymatic and heterogeneous
36
catalysis.
immobilized
lipase
and
free
metallo-organic
catalyst.
This
artificial
37 38 39
Keywords: Artificial nanometalloenzyme; 2-Methylimidazole metal-biosurfactant
40
nanocomposite; Cooperative tandem catalysis; Dynamic kinetic resolution; Lipase
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1. INTRODUCTION
47
Natural metalloenzymes with high substrate specificity and high catalytic capacity
48
have attracted a great deal of research interests in medical, chemical, and biological
49
fields. Unfortunately, one major drawback of natural metalloenzymes is that they
50
often exhibit a narrow substrate range, which limits their use in synthesis.1-3 Artificial
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metalloenzymes which combine the advantages of natural enzymes and metal
52
catalysts have achieved significant progress in the last decade.4-6 Artificial
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metalloenzymes have so far been successfully applied to many types of catalytic
54
reactions. In most cases, the construction of artificial metalloenzymes involves
55
procedures of anchoring a metal catalyst to a protein or polypeptide by either a
56
covalent bond, dative, or supramolecular interaction.7-9
57
Nanomaterials as carriers for enzyme immobilization10, 11 are also promising for
58
developing artificial metalloenzymes.12-14 For example, the metallo-organic catalyst
59
immobilized on nanoporous materials exhibited high catalytic activity and
60
enantioselectivity.15 Bäckvall and coworkers16 prepared an artificial metalloenzyme
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using silica mesocellular foams (MCFs) for co-immobilization of lipase and
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Palladium (Pd) nanoparticles with applications in dynamic kinetic resolution (DKR)
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of primary amines. Metal-biosurfactant nanocomposites (MBNs), a class of hybrid
64
nanomaterials consist of metal ions and biosurfactant ligands, have showed promise in
65
enzyme immobilization, protein encapsulation, drug delivery, and biomedicine.17-19
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Compared to hard nanomaterials such as metal-organic frameworks (MOFs) and
67
nanoflowers, MBNs, as a new kind of soft hydrophobic nanomaterials, is very
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suitable for inclusion of hydrophobic catalysts and catalytic reactions in non-aqueous
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systems.19-21 Owing to the amphipathic confined environment, morphological
70
variability, and metal-ligand diversity, MBNs could be an ideal carrier for the rational
71
design of artificial nanometalloenzyme.
72
Enantiomerically pure amines and alcohols are widely used as building blocks in
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synthetic organic chemistry, and there is a great challenge of synthesizing
74
enantiomerically pure compounds in an efficient and convenient manner.22-24 Shvo's
75
catalyst, a cyclopentadienone-ligated diruthenium complex, is an efficient catalyst for
76
the racemization of primary amines and secondary alcohols. Shvo's catalyst has
77
therefore been used in one-pot reaction with lipase for synthesizing enantiomerically
78
pure compounds in DKR processes.25-27 In DKR processes, lipase selectively
79
transforms only one enantiomer of racemic mixture into the corresponding product,
80
while the metallo-organic catalyst such as Shvo's catalyst catalyzed the racemization
81
of the rest enantiomer, resulting in 100% maximum theoretical yield of the
82
enantiomerically
83
(±)-1-phenylethanol using the Shvo's catalyst immobilized on PTA-modified
84
γ-alumina and Novozym435, obtaining a yield of 86.4% at 60℃ for 2 h. Mavrynsky et
85
al.26 performed the DKR of (±)-1-phenylethylamine on a large scale using
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Novozyme435 and free Shvo's catalyst at 105℃ and 130 mbar for 24 h in a soxhlet
87
apparatus, obtaining a yield of 65%.
pure
product.29-30
Im
et
al.25
performed
the
DKR
of
88
In this paper, MBNs, as a carrier of artificial nanometalloenzyme, was used for
89
synchronizing encapsulated lipase and Shvo's catalyst in mild reaction conditions
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using one-pot self-assembly method. In order to adapt to the alkaline catalytic
91
conditions of racemic reaction and increase the encapsulated load of hydrophobic
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catalyst, alkaline 2-methylimidazole (Mi) was added to the self-assembly conditions
93
as a metal coordination reagent. 2-Methylimidazole metal-biosurfactant nanocomposite
94
(MiMBN) increased the encapsulated load of lipase and Shvo's catalyst. Compared to
95
one-pot catalytic reaction of immobilized CALB and free Shvo's catalyst, the artificial
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nanometalloenzyme CALB-Shvo@MiMBN improved the catalytic efficiency in DKR
97
of primary amines and secondary alcohols.
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2. RESULTS AND DISCUSSION
99
2.1. Synthesis of CALB-Shvo@MiMBN. In this study, we reported an artificial
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nanometalloenzyme, which was constructed by the co-encapsulation of lipase and
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Shvo's catalyst in nanocomposites consisting of Mi, metal ion, and biosurfactant
102
(Scheme 1). In the nanocomposites, Mi can coordinate with metal ions to generate a
103
meta-organic framework,31-33 which thereby increased the loading amounts and
104
activities of lipase and Shvo's catalyst (Figure. S1 and Table S1). Nitrogen
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adsorption–desorption isotherms of metal-biosurfactant nanocomposite (MBN) and
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2-methylimidazole metal-biosurfactant nanocomposite (MiMBN) revealed differences
107
in nanostructures. The MBN and MiMBN displayed a type IV isotherm with H3
108
hysteresis, a type of porous materials with slit aperture openings (Figure. S1). The
109
introduction of Mi into MBN in one-pot self-assembly process decreased the pore
110
diameter from 26.51 to 20.74 nm, increased the pore volume from 0.2804 to 0.5639
111
cm3 g-1, and increased the specific surface area from 42.03 to 92.72 m2 g-1 (Table S1).
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Mi located in the pore diameter occupied the pore size of the slit aperture openings
113
and reduced the pore diameter. Mi located inside the pore volume enlarged the pore
114
volume at the same time. The increase in the pore volume and the specific surface
115
area favors encapsulating larger amounts of lipase and Shvo's catalyst and thereby
116
facilitates the formation of the artificial nanometalloenzyme. This artificial
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nanometalloenzyme allowed the highly efficient DKR processes of primary amines
118
and secondary alcohols in cooperative tandem catalysis.
119
We reasonably designed a novel artificial nanometalloenzyme, as shown in
120
Scheme 1. Enzyme acted as the core which induced the self-assembly of NaDC, Mi
121
and Co2+ around the protein surface.19,34,35 The metal ion was the linker to assemble
122
the nanocomposite. Mi generated metal ligand bonds with metal ions, which
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promoted encapsulation of a larger amount of the lipase. The CH3– group of Mi
124
increased the internal hydrophobicity of MBN, which promoted encapsulating a larger
125
amount of Shvo's catalyst. Mi increased the pore volume and the hydrophobicity of
126
the hydrophobic area of MBN, which also increased the amount of encapsulated
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Shvo's catalyst (Scheme 1), in one-pot self-assembly system. Due to the hydrophobic
128
interaction with NaDC, the Shvo's catalyst was encapsulated in MiMBN at the same
129
time.
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2.2. Experimental characterization. Scanning electron microscopy (SEM)
131
images and transmission electron microscopy (TEM) images (Figure. 1) suggested
132
that the MiMBN exhibited a typical coiled rod-shaped morphology with an average
133
length of >1 μm and a diameter of ~50 nm (Figure. 1a-b). The CALB@MiMBN
134
exhibited a typical spherical structure of 30-50 nm in diameter (Figure. 1cd). The
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CALB-Shvo@MiMBN showed a similar morphology as CALB@MiMBN in SEM
136
image (Figure. 1e), but there were obvious differences in TEM images (Figure. 1f). It
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is possible that the Shvo's catalyst was encapsulated in the hydrophobic pore of the
138
flexible framework structure. Energy-dispersive X-ray spectroscopy (EDS) mapping
139
under TEM (Figure. S2) also displayed the density of Ru and S elements which are
140
from Shvo's catalyst and CALB, proving the successful encapsulation.
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Fourier-transform infrared spectroscopy (FTIR) (Figure. 2a) confirmed the
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chemical composition of the CALB-Shvo@MiMBN, indicating the formation of
143
complexes and the presence of CALB and Shvo's catalyst in nanocomposites. We
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observed absorption bands of free CALB at 1675 cm−1 corresponding to C=O
145
stretching in the amide-I region and of free Shvo's catalyst at 1963, 2005, and 2041
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cm−1 corresponding to γ C=O stretching. Therefore, the characteristic bands of
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CALB-Shvo@MiMBN at 1675, 1963, 2005, and 2041 cm−1 demonstrated the
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presence of CALB and Shvo’s catalyst in the nanocomposite.36,37 Thermal gravity
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analysis (TGA) in a nitrogen atmosphere of MiMBN, CALB@MiMBN, and
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CALB-Shvo@MiMBN revealed the different decomposition processes (Figure. 2b).
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The CALB-Shvo@MiMBN exhibited 15% higher weight loss than the MiMBN in the
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temperature range of 350-450℃, proving the presence of CALB and Shvo's catalyst in
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the nanocomposite. Elemental analyses by inductively coupled plasma mass
154
spectrometry (ICP-MS) and protein concentration analyses by the Bradford method
155
showed that the loading amounts of CALB and Shvo's catalyst on the
156
CALB-Shvo@MiMBN were 15.21 wt% and 32.42 wt%, respectively (Table S2).
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Molar ratio of CALB and Shvo's catalyst on the CALB-Shvo@MiMBN was 1:65.7,
158
which indicated that the high ratio Shvo's catalyst could promote racemization. These
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results confirmed that the loading amounts of lipase in MiMBN was much higher than
160
that in MBN19, suggesting that MiMBN was efficient for immobilization of CALB
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and Shvo's catalyst, as 90% of the feeding enzyme and 81% of the feeding Shvo's
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catalyst were successfully encapsulated. We estimated that the volume occupied by
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lipase was larger than 675 nm3. The size of CALB is 3 nm×4 nm×5 nm and lower
164
than the volume occupied by lipase. So we believed that there are several enzymes in
165
the artificial nanometalloenzyme. The content of Co2+ and Na+ in MiMBN and
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CALB-Shvo@MiMBN was determined with ICP-MS as 174.9 mg g-1 and 1.718 mg
167
g-1, and 74.11 mg g-1 and 0.4721 mg g-1, respectively (Table S2). The results were
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consistent with the TGA analysis. X-ray diffraction (XRD) results indicated that the
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MiMBN had no obvious crystal peaks (Figure. S3), indicating an amorphous
170
structure.
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To further prove that the Shvo's catalyst was embedded in the nanocomposite
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microporous structure, nitrogen adsorption–desorption isotherms of CALB@MiMBN
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and CALB-Shvo@MiMBN were performed (Figure. 2cd). The CALB@MiMBN
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and CALB-Shvo@MiMBN displayed a type IV isotherm with H3 hysteresis, typical
175
of
176
Barrett–Joyner–Halenda (BJH) method were used to calculate the micropore and
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mesopore size distributions of CALB@MiMBN and CALB-Shvo@MiMBN,
178
respectively (Figure. 2d).37,38 As shown in Table S3, the CALB-Shvo@MiMBN had a
porous
materials.
The
Horvaih–Kawazoe
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(HK)
method
and
the
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larger BET surface area of 37.04 m2 g-1, micropore volume of 0.0121 cm3 g-1, and
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mesopore volume of 0.1439 cm3 g-1 compared to the CALB@MiMBN. However, the
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micropore diameter of CALB-Shvo@MiMBN (0.07868 nm) was smaller than that of
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CALB@MiMBN (1.131 nm). The micropore volume ratio of total pore volume of
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CALB-Shvo@MiMBN was 7.756%, smaller than that of CALB@MiMBN (10.52%).
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We observed the decrease in micropore volume ratio of CALB-Shvo@MiMBN,
185
which proved that the microporous structure was occupied by Shvo's catalyst. The
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introduction of Shvo's catalyst in CALB@MiMBN increased the mesopore diameter
187
from 3.052 to 17.52 nm (Table S3 and Figure. S5), which is favorable for the
188
transportation of substrates and products.
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X-ray photoelectron spectroscopy (XPS) was performed to investigate the
190
chemical composition of MiMBN, CALB@MiMBN, and CALB-Shvo@MiMBN. In
191
XPS analysis (Figure. 3a), the MiMBN, CALB@MiMBN and CALB-Shvo@MiMBN
192
showed a predominant narrow C 1s peak at ca. 284.8 eV, an O 1s peak at ca. 532.2 eV,
193
an N 1s peak at ca. 400.1 eV, and a Co 2p peak at ca. 781.2 eV. The Co 2p3/2 XPS
194
spectra of MiMBN, CALB@MiMBN, and CALB-Shvo@MiMBN (Figure. 3bd) can
195
be
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CALB-Shvo@MiMBN at 780.8 eV corresponded to a Co-O bond, deriving from
197
coordination of Co2+ with NaDC; the peak at 782.3 eV was attributed to the Co-N
198
bond, deriving from coordination of Co2+ with Mi; and the peak at 785.6 eV was a
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satellite peak. The Co 2p3/2 XPS spectra of the CALB@MiMBN at 780.7, 782.0, and
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785.3 eV corresponded to the Co-O bond, Co-N bond, and satellite peak, respectively.
deconvolved
into
three
subpeaks.
The
Co
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2p3/2
XPS
spectra
of
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The Co 2p3/2 XPS spectra of MiMBN at 781.0, 782.2, and 785.4 eV were attributed to
202
the Co-O bond, Co-N bond, and satellite peak, respectively. The peak shifts of Co
203
2p3/2 were caused by adsorption of Co2+ with lipase.39,40 Figure. 3eh showed the
204
high-resolution
205
CALB-Shvo@MiMBN. XPS wide scan spectra of Shvo's catalyst was shown in Fig.
206
S5. The Ru 3p peak in the CALB-Shvo@MiMBN (Figure. 3f) showed weak signal
207
strength compared to the Shvo's catalyst (Figure. 3e), and the Ru 3d peak in the
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CALB-Shvo@MiMBN (Figure. 3h) had different peak signals from the Shvo's
209
catalyst (Figure. 3g), which proved that the Shvo's catalyst (Figure. 3e) was located in
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the pores of the nanocomposite.41,42 The C 1s, N 1s and O 1s peaks of MiMBN,
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CALB@MiMBN, and CALB-Shvo@MiMBN were given in Figure. S6. We can
212
observe the C=O/COO-bond in the O 1s XPS spectra (Figure. S6) of
213
CALB@MiMBN because adsorption and metal coordination of Co2+ by lipase may
214
result in C=O/COO- bonds being exposed to the surface of nanocomposite. The
215
addition of Shvo's catalyst covered C=O/COO- groups exposed to the surface of
216
nanocomposite.
217
CALB-Shvo@MiMBN, we found that adsorption and metal coordination of Co2+ by
218
encapsulated lipase and Shvo's catalyst influenced the peak shifts.43,44 XPS of
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CALB@MiMBN and CALB-Shvo@MiMBN (Figure 3a) did not detect P and S
220
characteristic element peaks, which indicated that CALB is not on the surface and is
221
on the inside of nanocomposite. Previous studies have shown that enzymes, as core,
222
are located within nanocomposite.19-21 XPS of CALB-Shvo@MiMBN (Figure 3a)
Ru
3p
From
and
the
Ru
XPS
3d
of
spectrum
MiMBN,
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of
Shvo's
catalyst
CALB@MiMBN,
and
and
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detected Ru characteristic element peaks, which proved that Shvo's catalyst is on the
224
surface of nanocomposite.
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2.3. Cooperative tandem catalysis. The artificial nanometalloenzyme
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CALB-Shvo@MiMBN was subjected to DKR of racemic primary amines or
227
secondary alcohols. In a typical experiment, we performed the DKR of
228
(±)-1-phenylethanol under argon (1 bar) in dry toluene. The results showed that the
229
artificial
230
efficiency and ee value at 70 ℃
231
CALB-Shvo@MiMBN was 10% and 12% higher than that of one-pot catalytic
232
reactions of CALB@MiMBN and free Shvo's catalyst as well as Novozym435 and
233
free Shvo's catalyst, respectively. High catalytic efficiency was maintained even
234
though the additive amount of CALB-Shvo@MiMBN and reaction temperature were
235
reduced (Table 1). The results demonstrated that the CALB-Shvo@MiMBN is a
236
highly efficient catalyst for DKR of (±)-1-phenylethanol.
nanometalloenzyme
CALB-Shvo@MiMBN
had
excellent
catalytic
as the reaction time at 2 h, and yield of
237
Racemization of racemic primary amines requires a higher temperature and
238
longer reaction time than that of racemic secondary alcohols, and produces more
239
by-products using the same catalyst.45,46 We carried out the DKR process of
240
(±)-1-phenylethylamine under argon (130 mbar) in dry toluene using the
241
CALB-Shvo@MiMBN (Table 2). The results showed that the CALB-Shvo@MiMBN
242
effectively catalyzed the DKR of racemic primary amine at 90℃ as the reaction time
243
at 6 h, the yield of CALB-Shvo@MiMBN was 4% and 6% higher than that of one-pot
244
catalytic reaction of immobilized CALB and free Shvo's catalyst. However, the
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decreased reaction temperature and the additive amount of the CALB-Shvo@MiMBN
246
were not conducive to the catalytic reaction. Racemization catalyzed by Shvo's
247
catalyst is a rate-limiting step; an increase in reaction time gave a marginally
248
improved conversion. In the initial reaction stage, increasing the amount of catalyst
249
can enhance the catalytic efficiency, but the total catalytic efficiency does not increase
250
significantly at the same catalytic long time. Figure 4 showed the reaction time curves
251
of DKR of (±)-1-phenylethylamine using three different catalysts. It is observed that
252
the CALB-Shvo@MiMBN was the best catalyst for DKR of (±)-1-phenylethylamine,
253
compared to the one-pot catalytic reactions of immobilized CALB and free Shvo's
254
catalyst. The catalytic efficiency of CALB-Shvo@MiMBN increased 17.4% and
255
7.8% compared with the one-pot catalytic reactions of CALB@MiMBN/Shvo and
256
Novozym435/Shvo at 90℃ as the reaction time at 4 h, respectively. Lipase can
257
rapidly consume one chiral enantiomer, and slowly catalyze another chiral enantiomer.
258
At long reaction time, the DKR of (±)-1-phenylethylamine catalyzed by
259
CALB-Shvo@MiMBN would show slightly lower ee value than in one-pot catalytic
260
reactions of CALB@MiMBN/Shvo and Novozym435/Shvo. The value of apparent
261
activation energy was calculated according to the Arrhenius equation. In the DKR of
262
(±)-1-phenylethanol
263
CALB-Shvo@MiMBN, the value of apparent activation energy was 10.68 and 14.37
264
kJ
265
(±)-1-phenylethylamine, the value of TOF (defined as µmol product per µmol CALB
266
protein per hour) was 1708 and 1182 h-1, respectively. Differences of apparent
mol-1,
and
respectively.
(±)-1-phenylethylamine
In
the
DKR
of
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catalyzed
by
(±)-1-phenylethanol
the
and
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267
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activation energy and TOF determine differential catalytic capacity.
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The artificial nanometalloenzyme increased the reaction rate and shortened the
269
reaction time compared to the reported one-pot reaction system using free Shvo's
270
catalyst and Novozym435 under the same conditions.23,26 According to the loading
271
amounts of CALB and Shvo's catalyst on the CALB-Shvo@MiMBN, the diameter of
272
CALB-Shvo@MiMBN, and the density of 1.06 g cm-3 of CALB-Shvo@MiMBN, We
273
estimated that the distance between CALB and Shvo's catalyst was less than 8.5 nm.
274
The artificial nanometalloenzyme CALB-Shvo@MiMBN had the better catalytic
275
efficiency than one-pot catalytic reactions in cooperative catalysis because of the
276
shorter distances between two functions. The racemic primary amines or secondary
277
alcohols entered the artificial nanometalloenzyme and exposed to CALB, leading to
278
the selective acylation of (R)-enantiomers. The rest (S)-enantiomers of primary
279
amines or secondary alcohols were then racemized by Shvo's catalyst encapsulated in
280
the artificial nanometalloenzyme, followed by the CALB-catalyzed selective
281
acylation. NaDC as a surfactant could enhance the activity of lipase in selective
282
acylation of (R)-enantiomer of the racemic secondary alcohols or primary amines, and
283
then the (S)-enantiomer of racemic secondary alcohol or primary amines rapidly
284
accumulated. Mi increased the alkaline characteristics of CALB-Shvo@MiMBN
285
microenvironment, which helps to reduce the formation of by-products of
286
racemization and increase the catalytic efficiency of racemization. A high local
287
concentration of Shvo's catalyst inside CALB-Shvo@MiMBN improved the
288
racemization efficiency. In addition the proximity of CALB and Shvo's catalyst
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increased the transportation of reaction intermediate in the tandem catalysis.47-49
290
After five consecutive reuses, the CALB-Shvo@MiMBN still maintained its
291
catalytic activity. Harsh reaction conditions which caused partial deactivation of
292
artificial nanometalloenzyme in the DKR of (±)-1-phenylethylamine, the recyclability
293
of CALB-Shvo@MiMBN in DKR of (±)-1-phenylethylamine was worse than that of
294
(±)-1-phenylethanol (Figure 5). Organic solvents and magnetic mechanical stirring
295
would cause the leaching of encapsulated lipase and Shvo's catalyst of
296
[email protected] Results of leaching showed that the Shvo's catalyst and
297
lipase have slight leaching in toluene at each reuse. However, leaching of lipase and
298
Shvo's catalyst in DKR of (±)-1-phenylethanol was lower than that of
299
(±)-1-phenylethylamine (Figure S7). Leaching led to a decrease in catalytic activity,
300
but the remaining encapsulated lipase and Shvo's catalyst in CALB-Shvo@MiMBN
301
still maintained a high catalytic activity. Catalytic conditions are the key factors
302
determining
303
nanometalloenzyme has potential for industrial application
304
3. CONCLUSIONS
the
lifetime
of
artificial
nanometalloenzyme.
The
artificial
305
We developed a novel highly efficient artificial nanometalloenzyme by
306
synchronous encapsulating a metallo-organic catalyst and an enzyme into MiMBN.
307
Mi increased the alkaline characteristics of CALB-Shvo@MiMBN microenvironment
308
and improved the encapsulated load of lipase and Shvo's catalyst, which helps to
309
reduce the formation of by-products of racemization and increase the catalytic
310
efficiency of racemization. The proximity effect of Shvo's catalyst and CALB resulted
311
in an enhanced efficiency in the DKR of racemic primary amines and secondary
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312
alcohols. The design of co-encapsulating enzymes and heterogeneous catalysts in
313
MiMBNs holds great promise for creating novel bio-chemo hybrid catalysts with
314
many potential applications in cooperative tandem catalysis.
315
4. EXPERIMENTAL SECTION
316
4.1.
Materials.
1-Hydroxytetraphenylcyclopentadienyl-
(tetraphenyl-2,4-
317
cyclopentadien-1-one)-μ-hydrotetracarbonyldiruthenium (II) (Shvo's catalyst) was
318
purchased from Sigma–Aldrich (St. Louis, MO, USA). Sodium deoxycholate,
319
(R)-2-methoxy-N-(1-phenylethyl)
320
acetamide,
321
(±)-1-phenylethanol and isopropenyl acetate were purchased from Aladdin (Shanghai,
322
China). 2-Methylimidazole (Mi) was purchased from TCI (Tokyo, Japan).
323
Lipozyme®CALB L and Novozym435 were obtained from Novozymes (Copenhagen,
324
Denmark). Cobalt chloride hexahydrate (CoCl2·6H2O), Na2CO3 and potassium
325
tert-butoxide
326
Engineering-technological Research and Development Center (Guangzhou, China).
327
All other reagents were of analytical reagent grade, and used as received. Ultrapure
328
water (18.2 MΩ; Millpore Co., USA) was used throughout the experiment.
toluene,
isopropyl
(tBuOK)
was
acetamide, acetate,
got
(S)-2-methoxy-N-(1-phenylethyl)
pentadecane,
from
(±)-1-phenylethylamine,
Guangdong
Chemical
Reagent
329
4.2. Synthesis of MiMBN, CALB@MiMBN and CALB-Shvo@MiMBN. In a
330
typical experiment, 10 mL of CoCl2·6H2O aqueous solution (20 mM) was added into
331
10 mL of aqueous NaDC (15 mM) solution with 15 mM Mi, 12 μM Shvo's catalyst
332
(dissolved in N,N-dimethylformamide) and 2 mL CALB-L soultion. The mixture was
333
stirred at 300 rpm for 30 min at 25℃, followed by centrifugation at 7000 rpm for 10
334
min and washing twice by water to obtain nanocomposite. MiMBN does not contain
335
lipase and Shvo's catalyst, CALB@MiMBN contains lipase that does not contain
336
Shvo's catalyst and CALB-Shvo@MiMBN contains lipase and Shvo's catalyst.
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Page 16 of 35
337
4.3. Characterization. Field-emission scanning electron microscopy (FE-SEM)
338
(SEM) was performed using a Nova NanoSEM 450 (FEI, USA) using an accelerating
339
voltage of 5 kV with fit magnification. Transmission electron microscopy (TEM) was
340
carried out using a JEM-200CX analytical transmission electron microscope (Japan).
341
A Micromeritics 3Flex surface analyzer (USA) was used to analyze BET surface area,
342
pore volume and pore diameter and adsorption-desorption isotherm. Element contents
343
were analyzed by using the inductively coupled plasma mass spectrometry (ICP-MS)
344
from Aglient 7500a (USA). The chemical functional groups were analyzed by a
345
Thermo Corporation Nexus FTIR spectrophotometer (USA). TGA was performed on
346
a TGA Q500 thermogravimetric analyzer (TA, USA). The sample was heated from 25
347
°C to 450 °C at a rate of 10 °C/min under N2 atmosphere. X-ray diffraction (XRD)
348
was performed on a Rigaku Ultima IV diffractometer with Cu Kα X-rays. X-ray
349
photoelectron spectroscopy (XPS) was performed using a Kratos AXIS Ultra DLD
350
XPS system equipped with a hemispherical energy analyzer and a monochromatic Al
351
Kα source. The source was operated at 15 keV and 150 W; pass energy was fixed at
352
40 eV for the high-resolution scans. All samples were prepared as pressed powders
353
supported on a metal bar for the XPS measurements.
354
4.4.
General
procedure
for
dynamic
kinetic
resolution
of
355
(±)-1-phenylethanol. A dried 10-mL Schlenk tube was charged with the
356
CALB-Shvo@MiMBN (50 mg or 25 mg), dry Na2CO3 (25 mg) and tBuOK (25 mg).
357
Dry toluene (1 mL), (±)-1-phenylethanol (0.30 mmol), isopropenyl acetate (2.0 equiv),
358
and pentadecane (15 μL) were added subsequently. The vessel was closed, evacuated,
359
and backfilled with argon gas three times. The reaction mixture was stirred at 50, 60
360
and 70 °C for 2 and 4 h at 300 rpm. The reaction was cooled to room temperature; the
361
solids were removed by centrifugation and samples were diluted by toluene.
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362
ACS Applied Materials & Interfaces
4.5.
General
procedure
for
dynamic
kinetic
resolution
of
363
(±)-1-phenylethylamine. A dried 10-mL Schlenk tube was charged with the
364
CALB-Shvo@MiMBN (50 mg or 25 mg) and dry Na2CO3 (50 mg). Dry toluene (1
365
mL), (±)-1-phenylethylamine (0.30 mmol), isopropyl acetate (4.0 equiv), and
366
pentadecane (15 μL) were added subsequently. The vessel was closed, evacuated, and
367
backfilled with argon three times. The reaction mixture was stirred at 80 and 90 °C
368
for 6, 8, and 12 h at 300 rpm. The reaction was cooled to room temperature; the solids
369
were removed by centrifugation and samples were diluted by toluene.
370
4.6. Recyclability and leaching test of lipase and Shvo's catalyst of
371
CALB-Shvo@MiMBN. According to the general procedure for DKR of
372
(±)-1-phenylethanol or (±)-1-phenylethylamine, recyclability and leaching of lipase
373
and Shvo's catalyst of CALB-Shvo@MiMBN were tested. For (±)-1-phenylethanol,
374
the reaction was performed at 60°C for 2 h at 300 rpm; for (±)-1-phenylethylamine,
375
the reaction was performed at 90°C for 4 h at 300 rpm. After each test, toluene was
376
used to wash the CALB-Shvo@MiMBN three times to carry out the next test.
377
ICP-MS and Bradford method was used to determine Shvo's catalyst and lipase.
378
4.7. Determination of chiral gas chromatography. The enantiomeric excess
379
was determined by analytical GC (Agilent, USA) employing a CP-Chirasil-DEX CB
380
column (25 m × 0.32 mm, Agilent, USA). Chiral GC-analysis: The carrier gas was
381
helium; the velocity was 1.6 mL/min, injector and detector 250°C, program: 100°C /5
382
min/ 155°C /3°C min-1, 5 min/ 200°C /20°C min-1, 5 min.
383 384
Supporting Information
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Page 18 of 35
385
Figure S1 (a) Nitrogen adsorption-desorption isotherms of MBN and MiMBN at 77
386
K; (b) Barrett−Joyner−Halenda (BJH) pore size distribution calculated from the
387
adsorption branch of the isotherms of MBN and MiMBN.
388
Figure S2. Energy-dispersive X-ray spectroscopy (EDS) diagram in TEM of
389
CALB-Shvo@MiMBN.
390
Figure S3. X-Ray Diffraction (XRD) diagrams of MiMBN, CALB@MiMBN, and
391
CALB-Shvo@MiMBN.
392
Figure S4. Density Functional Theory (DFT) method mesopore size distribution from
393
BET of CALB@MiMBN and CALB-Shvo@MiMBN.
394
Figure S5. XPS spectra of Shvo's catalyst.
395
Figure S6. C 1s, N 1s, and O 1s spectra of (a, d, g) MiMBN, (b, e, f)
396
CALB@MiMBN, and (c, f, i) CALB-Shvo@MiMBN from XPS.
397
Figure S7. The leaching of lipase and Shvo's catalyst of CALB-Shvo@MiMBN
398
during
399
(±)-1-phenylethylamine (b).
400
Table S1. Brunauer−Emmett−Teller (BET) surface area, pore volume, and pore
401
diameter of MBN and MiMBN.
402
Table S2. The content of CALB, Shvo's catalyst, Co2+, and Na+ in MiMBN and
403
CALB-Shvo@MiMBN.
404
Table S3. Brunauer−Emmett−Teller (BET) surface area, pore volume, and pore
405
diameter of CALB@MiMBN and CALB-Shvo@MiMBN.
dynamic
kinetic
resolution
of
(±)-1-phenylethanol
406 407
AUTHOR INFORMATION
408
Corresponding Authors
409
*E-mail:
[email protected] ACS Paragon Plus Environment
(a)
or
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410
Notes
411
The authors declare no competing financial interest.
412 413
ACKNOWLEDGMENTS
414
The authors acknowledge the financial supports of the National Natural Science
415
Foundation of China (21706126, 21606127, and 21576134), the National Key
416
Research and Development Program (2016YFA0204300), and the Jiangsu Synergetic
417
Innovation Center for Advanced Bio-Manufacture (XTE1853).
418 419
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(47) Kim, H.; Choi, Y. K.; Lee, J.; Lee, E.; Park, J.; Kim, M. J.
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Ionic-Surfactant-Coated Burkholderia cepacia Lipase as a Highly Active and
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Enantioselective Catalyst for the Dynamic Kinetic Resolution of Secondary Alcohols.
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Angew. Chem. Int. Ed. 2011, 50, 10944-10948.
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(48) Pollock, C. L.; Fox, K. J.; Lacroix, S. D.; McDonagh, J.; Marr, P. C.; Nethercott,
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A. M.; Pennycook, A.; Qian, S.; Robinson, L.; Saunders, G. C.; Marr, A. C.
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Minimizing Side Reactions in Chemoenzymatic Dynamic Kinetic Resolution:
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Organometallic and Material Strategies. Dalton Trans. 2012, 41, 13423-13428.
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(49) Zisis, T.; Freddolino, P. L.; Turunen, P.; van Teeseling, M. C. F.; Rowan, A. E.;
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Blank, K. G. Interfacial Activation of Candida antarctica Lipase B: Combined
570
Evidence from Experiment and Simulation. Biochemistry 2015, 54, 5969-5979.
571 572 573 574 575 576 577 578 579 580 581 582 583
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Figure legends
584 585
Scheme 1. Preparation and structure of the artificial nanometalloenzyme via
586
co-encapsulation
587
2-methylimidazole-metal-biosurfactant nanocomposite.
588
Figure 1. (a) Scanning electron microscopy (SEM) image and (b) transmission
589
electron microscopy (TEM) image of MiMBN. (c) SEM image and (d) TEM) image
590
of CALB@MiMBN. (e) SEM image and (f) TEM image of CALB-Shvo@MiMBN.
591
Figure 2. (a) Thermal gravity analysis (TGA) curves of MiMBN, CALB@MiMBN,
592
and CALB-Shvo@MiMBN in a nitrogen atmosphere. (b) Fourier-transform infrared
593
spectroscopy (FTIR) of free CALB, free Shvo's catalyst, MiMBN, CALB@MiMBN,
594
and CALB-Shvo@MiMBN. (c) Nitrogen adsorption–desorption isotherms from
595
microporous
596
CALB-Shvo@MiMBN at 77 K; (d) Horvaih−Kawazoe (HK) micropore and
597
Barrett−Joyner−Halenda (BJH) mesopore size distributions calculated from the
598
adsorption branch of the isotherms of CALB@MiMBN and CALB-Shvo@MiMBN.
599
Figure 3. (a) XPS analysis of MiMBN, CALB@MiMBN and CALB-Shvo@MiMBN.
600
(b-d) Co 2p spectra of MiMBN, CALB@MiMBN and CALB-Shvo@MiMBN. (e-f)
601
Ru 3p spectra of Shvo's catalyst and CALB-Shvo@MiMBN. (g-h) Ru 3d spectra of
602
Shvo's catalyst and CALB-Shvo@MiMBN.
603
Figure
604
(±)-1-phenylethylamine by CALB-Shvo@MiMBN, CALB@MiMBN/Shvo, and
605
Novozym435/Shvo.
606
Figure 5. Recyclability study for dynamic kinetic resolution of (±)-1-phenylethanol
607
or (±)-1-phenylethylamine by CALB-Shvo@MiMBN.
4.
of
a
metallo-organic
Brunner−Emmet−Teller
Comparative
study
catalyst
(BET)
for
of
dynamic
608
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and
an
enzyme
CALb@MiMBN
kinetic
resolution
into
and
of
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ACS Applied Materials & Interfaces
Figures
609 610
611 612
Scheme 1.
613 614 615 616 617 618 619 620 621 622
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a
b
c
d
e
f
623
624
625 626
Figure 1.
627 628 629 630 631
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a
b b
632
c
d
633 634
Figure 2.
635 636 637 638 639 640 641 642
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a
b
643
c
d
e
f
g
h
644
645
646 647
Figure 3.
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ACS Applied Materials & Interfaces
648 649
Figure 4.
650 651 652 653 654 655 656 657 658 659 660 661
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662 663
Figure 5.
664 665 666 667 668 669 670 671 672 673 674 675 676 677
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ACS Applied Materials & Interfaces
Table
678 679
Table 1. Summary of results from the DKR of (±)-1-phenylethanol catalyzed by the
680
CALB-Shvo@MiMBN, the one-pot reaction of CALB@MiMBN and free Shvo's
681
catalyst and the one-pot reaction of Novozym435 and free Shvo's catalyst.[a]
682
Entry
Catalyst
T [℃]
t [h]
Yield [%][b]
ee [%][b]
1
CALB-Shvo@MiMBN
70
2
92
99
2
CALB-Shvo@MiMBN
70
4
98
99
3
CALB-Shvo@MiMBN
60
2
89
99
4
CALB-shvo@MiMBN
60
4
95
99
5
CALB-Shvo@MiMBN
50
2
83
99
6
CALB-Shvo@MiMBN
50
4
92
99
7
CALB-Shvo@MiMBN[c]
70
4
95
99
8
CALB@MiMBN/Shvo
70
2
82
99
9
Novozym435/Shvo
70
2
80
99
683
[a] Reaction conditions: All of the reactions were carried out in dry toluene (1 mL)
684
under 1 bar argon gas environment, catalyst (50 mg), (±)-1-phenylethanol (0.30
685
mmol), isopropenyl acetate (2.0 equiv), dry Na2CO3 (25 mg), tBuOK (25 mg),
686
pentadecane (15 μL) as internal standard, and 300 rpm. [b] Determined by GC
687
analysis. [c] Catalyst was 25 mg.
688
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689
Table 2. Summary of results from the DKR of (±)-1-phenylethylamine catalyzed by
690
the CALB-Shvo@MiMBN, the one-pot reaction of CALB@MiMBN and free Shvo's
691
catalyst and the one-pot reaction of Novozym435 and free Shvo's catalyst.[a] Entry
Catalyst
T[℃]
t [h]
Yield [%][b]
ee[%][b]
1
CALB-Shvo@MiMBN
90
6
76
98
2
CALB-Shvo@MiMBN
90
8
78
96
3
CALB-Shvo@MiMBN
90
12
79
92
4
CALB-Shvo@MiMBN
80
12
67
96
5
CALB-Shvo@MiMBN[c]
90
8
69
95
6
CALB@MiMBN/Shvo
90
8
72
94
7
Novozym435/Shvo
90
8
68
98
692
[a] Reaction conditions: All of the reactions were carried out in dry toluene (1 mL)
693
under 130 mbar argon gas environment, catalyst (50 mg), ( ± )-1-phenylethylamine
694
(0.30 mmol), isopropyl acetate (4.0 equiv), dry Na2CO3 (50 mg), pentadecane (15 μL)
695
as internal standard, and 300 rpm. [b] Determined by GC analysis. [c] Catalyst was 25
696
mg.
697 698 699 700 701 702
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