GOx@ZIF-8(NiPd) Nanoflower: An Artificial Enzyme System for Tandem Catalysis

Article abstract of DOI:10.1002/anie.201710418

We report a facile approach to prepare an artificial enzyme system for tandem catalysis. NiPd hollow nanoparticles and glucose oxidase (GOx) were simultaneously immobilized on the zeolitic imidazolate framework 8 (ZIF-8) via a co-precipitation method. The as-prepared GOx@ZIF-8(NiPd) nanoflower not only exhibited the peroxidase-like activity of NiPd hollow nanoparticles but also maintained the enzymatic activity of GOx. A colorimetric sensor for rapid detection of glucose was realized through the GOx@ZIF-8(NiPd) based multi-enzyme system. Moreover, the GOx@ZIF-8(NiPd) modified electrode showed good bioactivity of GOx and high electrocatalytic activity for the oxygen reduction reaction (ORR), which could also be used for electrochemical detection of glucose.

Full text of DOI:10.1002/anie.201710418

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Accepted Article
Title: GOx@ZIF-8(NiPd) nanoflower: an artificial enzyme system for
tandem catalysis
Authors: Qingqing Wang, Xueping Zhang, Liang Huang, Zhiquan
Zhang, and Shaojun Dong
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To be cited as: Angew. Chem. Int. Ed. 10.1002/anie.201710418
Angew. Chem. 10.1002/ange.201710418
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GOx@ZIF-8(NiPd) nanoflower: an artificial enzyme system for
tandem catalysis
Qingqing Wang,[a, b] Xueping Zhang,[b] Liang Huang,[b] Zhiquan Zhang,*[a] and Shaojun Dong*[b]
Abstract: This work reports a facile approach to fabricate an
artificial enzyme system for tandem catalysis. NiPd hollow
nanoparticles and glucose oxidase (GOx) were simultaneously
immobilized on the zeolitic imidazolate framework 8 (ZIF-8) via a co-
hollow nanoparticles, which exhibiting outstanding peroxidase-
like catalytic activity,[9] were successfully immobilized both inside
of the ZIF-8 crystal lattices and on the outer surfaces. The
obtained ZIF-8(NiPd) also possessed excellent property of
peroxidase mimic. With glucose oxidase (GOx) and NiPd hollow
nanoparticles being immobilized simultaneously on ZIF-8, an
artificial enzyme system GOx@ZIF-8(NiPd) nanoflower was
prepared for tandem catalysis. The cascade reaction for the
visual detection of glucose was successfully combined into one
step. In addition, due to the competition reactions of electro-
catalytic oxygen reduction and glucose oxidation, the GOx@ZIF-
8(NiPd) modified glassy carbon electrode (GCE) exhibits quiet
different electrochemical performance toward H2O2 and glucose.
As a result, a novel electrochemical sensor for glucose detection
could also be fabricated based on the obtained nanoflower.
More importantly, our strategy was applicable to other
nanozymes[10] and proteins such as Cyt c and horseradish
peroxidase (HRP). Various kinds of multi-enzyme system would
be fabricated, making further effort to mimic complex natural
enzyme system.
precipitation method.
The as-prepared
GOx@ZIF-8(NiPd)
nanoflower not only exhibited the peroxidase-like activity of NiPd
hollow nanoparticles but also maintained the enzymatic activity of
GOx. A colorimetric sensor for rapid detection of glucose was
fabricated through the GOx@ZIF-8(NiPd) based multi-enzyme
system and the cascade reaction for the visual detection of glucose
was successfully combined into one step. Moreover, the GOx@ZIF-
8(NiPd) modified electrode showed good bioactivity of GOx and high
electrocatalytic activity for the oxygen reduction reaction (ORR),
which could also be used for electrochemical detection of glucose.
The proposed strategy for the fabrication of artificial multi-enzyme
system builds a potential bridge of cooperation between nanozyme
and natural enzyme, combining together their properties and
functionalities, as well making efforts to multi-catalysis and tandem
reactions.
By using PVP as the nanoparticle stabilizer, NiPd hollow
nanoparticles could be located both inside and on the outer
surface of ZIF-8 crystal when PVP-stabilized nanoparticles were
added into the ZIF-8 synthesis solution at short time (less than 2
min). Via a co-precipitation procedure in aqueous solution, GOx
and NiPd hollow nanoparticles could be simultaneously
immobilized in ZIF-8. After being encapsulated into ZIF-8, GOx
reserved the enzymatic activity because the assembling process
is very gentle and environmental friendly. The strategy could not
only prevent the enzymes from leaching but also build a
potential bridge of cooperation between nanozyme and natural
enzyme, thus opening a new avenue for combining together
their properties and functionalities.
The obtained ZIF-8 based nanocomposites (Figure S1)
showed different colors with each other because different guests
were encapsulated in the ZIF-8 hosts. The morphology of the
samples was further characterized by TEM and SEM. As
displayed in Figure 1c and 1d, the hollow nanoparticles are
distributed on the ZIF-8, and the average diameter of NiPd
hollow nanoparticles is about 40 nm (Figure S2a). ZIF-8(NiPd)
maintained the morphology of ZIF-8, which has a regular smooth
fusiform structure as shown in Figure S2b. Some cruciate
flower-like structure (Figure 1c) was also observed in ZIF-
8(NiPd), which can be ascribed as the two ZIF-8 nanoparticles
assembled simultaneously during the growth of nanocrystals.
However, compared with ZIF-8, the size of GOx@ZIF-8 turned
smaller and the morphology changed obviously (Figure 1e and
1f). The novel nanoflower structure of GOx@ZIF-8 would be
facilitated by the GOx affinity towards the imidazole-containing
building block arising from intermolecular hydrogen bonding and
hydrophobic interactions.[11] The GOx-ZIF-8 interaction was
Metal-organic frameworks (MOFs),[1] which are self-
assembled from organic ligand and metal ions, have attracted
immense attention owing to their large and accessible specific
surface areas, uniform and tunable pore sizes.[2] Recently, a
series of mesoporous metalloporphyrin Fe-MOFs have been
demonstrated as an effective peroxidase mimic to catalyze the
oxidation reaction.[3] Various MOFs or modified MOFs have been
reported as enzyme mimetics with biological functions,[4]
expanding their applications in biotechnology fields such as
bioanalysis, biocatalysis, and biomedical engineering.[5] In
particular, coating enzyme with ZIF-8 could protect the
biomacromolecules from biological, thermal and chemical
degradation with maintenance of bioactivity,[6] and Cyt c/ZIF-8
composite was found exhibiting a 10-fold increase in peroxidase
activity compared to free cytochrome c (Cyt c) in solution.[7]
Inspired by the merits of ZIF-8, more and more attentions have
been paid to biomimetic mineralization of ZIF-8.[8]
In our work, ZIF-8 was chosen as a support for enzyme
immobilization to establish a mimic multi-enzyme system. NiPd
[a]
[b]
Q. Wang, Prof. Z. Zhang
College of Chemistry, Jilin University, Changchun, 130012, P. R.
China
E-mail: zzq@jlu.edu.cn.
Q. Wang, X. Zhang, L. Huang, Prof. S. Dong
State Key Laboratory of Electroanalytical Chemistry, Changchun
Institute of Applied Chemistry, Changchun, 130022, P. R. China
E-mail: dongsj@ciac.ac.cn.
Supporting information for this article is given via a link at the end of the
document.
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Figure 1. (a) SEM images of ZIF-8(NiPd). (b), (c) and (d) TEM images of ZIF-8(NiPd). (e) SEM images of GOx@ZIF-8. (f) TEM images of GOx@ZIF-8. (g) and
(h) TEM images of GOx@ZIF-8(NiPd).
probably due to the coordination between the Zn cations and the
90 °C) ranges. Because of the negligible background signal, pH
= 4.0 and 50 °C were adopted for the subsequent activity
analysis of ZIF-8(NiPd) (Figure S5). The apparent steady-state
kinetic parameters for this reaction were determined by
changing the concentration of OPD and H2O2 in the system,
respectively (Figure S7). The oxidation reaction catalyzed by
ZIF-8(NiPd) follows the typical Michaelis−Menten behavior
toward both substrates, OPD and H2O2 (Figure S7a and S7c).
The value ε= 17 000 M-1 cm-1 (at 417 nm) for DAP was used
here to obtain the corresponding concentration term from the
absorbance data. By using Lineweaver−Burk plot (Figure S7b
and S7d), Km and Vm were obtained as given in Table S1.
Compared with horseradish peroxidase (HRP) and other ZIF-8-
based catalysts shown in Table S1, the apparent Km value of
ZIF-8(NiPd) with OPD or H2O2 as the substrate is lower,
indicating the higher catalytic activity of ZIF-8(NiPd).
In the following experiments, potential enzymatic performance
of GOx@ZIF-8(NiPd) was determined in detail. As shown in
Figure 3a, the absorbance enhanced with the increase of the
reaction time, indicating the peroxidase-like activity of
GOx@ZIF-8(NiPd). And with the same content of NiPd, the
catalytic activity of GOx@ZIF-8(NiPd) was similar to that of ZIF-
8(NiPd) and NiPd hollow nanoparticles, suggesting that the
introduce of GOx and ZIF-8 had negligible effect on the catalytic
activity of NiPd hollow nanoparticles. Then, the enzymatic
activity of the GOx encapsulated in GOx@ZIF-8(NiPd) was
detected by a gluconic acid-specific colorimetric assay[13] as
GOx could catalyze the oxidation of glucose yielding gluconic
acid and H2O2. Upon the addition of hydroxamine and Fe3+, the
color of the solution turned red with a characteristic absorbance
peak at 505 nm (Figure 3b), which suggested that gluconic acid
was indeed produced in this GOx@ZIF-8(NiPd)-catalyzed
reaction. The solutions containing glucose or GOx@ZIF-8(NiPd)
alone could not introduce any color change. In particular,
GOx@ZIF-8(NiPd) exhibited much higher catalytic activity than
12]
carbonyl group of the proteins.[6b,
With the similar one-pot
strategy, NiPd hollow nanoparticles and GOx were successfully
encapsulated in ZIF-8, forming a mimic multi-enzyme system
GOx@ZIF-8(NiPd) (Figure 1g and 1h). Interestingly, the XRD
patterns of the nanocomposites (GOx@ZIF-8(NiPd), GOx@ZIF-
8 and ZIF-8(NiPd)) were almost identical to the measured
patterns of ZIF-8, indicating that the encapsulation of NiPd or
GOx had negligible effects on the phase of ZIF-8 hosts (Figure
2a). The FTIR spectra (Figure 2b) showed stretches
characteristic of GOx at ~1640-1660 cm-1, corresponding to
amide I, mainly attributed to C=O stretching mode. This result
suggested the presence of GOx in the GOx@ZIF-8(NiPd) and
GOx@ZIF-8 composites.
To investigate the mimic enzyme catalytic activity of ZIF-
8(NiPd), typical peroxidase substrate OPD was chosen as the
chromogenic substrate. As shown in Figure S4, ZIF-8(NiPd)
could catalyze the oxidation of OPD to produce a typical yellow
oxidized product 2,3-diaminophenazinc (DAP) in the presence of
H2O2 (curve 3), indicating the peroxidase-like activity of ZIF-
8(NiPd). Additionally, the absorbance changes of OPD were
investigated at different pH (pH 3.0–10.0) and temperature (20–
Figure 2. (a) XRD patterns of GOx@ZIF-8(NiPd), GOx@ZIF-8, ZIF-8(NiPd),
ZIF-8 and simulated ZIF-8. (b) FTIR spectra of GOx, ZIF-8, GOx@ZIF-8 and
GOx@ZIF-8(NiPd).
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We also investigated the electrocatalytic activity of GOx@ZIF-
8(NiPd) in detail. As shown in Figure 4a, the cathodic peak
current at about -0.45 V increased when the H2O2 concentration
rose from 0 to 10 mM, indicating the electrocatalytic activity of
GOx@ZIF-8(NiPd) towards the reduction of H2O2. To be
surprised, the cathodic peak current decreased significantly with
the increase of glucose concentration (Figure 4b). The
mechanism of the process was quite different from the reported
glucose electrochemical sensor based on GOx and peroxidase
mimics. The reduction peaks of GOx@ZIF-8(NiPd)/GCE in
Figure 4b would be generated mainly from ORR. With the
addition of glucose, GOx@ZIF-8(NiPd)/GCE could catalyze the
oxidation of glucose and decrease the concentration of
dissolved oxygen in the solution, resulting in an obvious drop of
the cathodic peak current of ORR. Therefore, the signal of
glucose could be distinguished easily with that of H2O2 by the
opposite response current as shown in Figure 4c. For
comparison, the electrochemical performance of ZIF-
8(NiPd)/GCE towards H2O2 and glucose was also investigated
respectively. As displayed in Figure S10a and S10b, ZIF-
8(NiPd)/GCE could also electro-catalyze the reduction of H2O2,
but no obvious changes were found at the cathodic peak current
in the presence of glucose because glucose oxidation could not
happen without GOx. Figure S10c and S10d further
Figure 3. (a) Time-dependent absorbance changes at 417 nm of OPD using
different catalysts. (b) UV-Vis absorbance spectra and visual color changes for
different samples obtained by a gluconic acid-specific assay.
GOx@ZIF-8 although both of them can catalyze the oxidation of
glucose. The higher catalytic activity can be ascribed to the
hollow nanoparticle structure of NiPd in GOx@ZIF-8(NiPd),
which could help capturing more GOx molecules into ZIF-8,
improving the catalytic activity of the composite. As a result, the
as-prepared GOx@ZIF-8(NiPd) nanoflower not only exhibited
the peroxidase-like activity of NiPd hollow nanoparticles but also
reserved the enzymatic activity of GOx.
A
multi-enzyme system could be fabricated based on
GOx@ZIF-8(NiPd) nanoflower, and the feasibility of cascade
reaction was verified. That is, GOx@ZIF-8(NiPd) first catalyzed
the glucose oxidation to yield gluconic acid and H2O2 by means
of molecular oxygen, and then catalyzed the oxidation of OPD
by produced H2O2 resulting in the formation of a colored product
of DAP [eq.1]:
demonstrated
that
GOx@ZIF-8(NiPd)/GCE
and
ZIF-
8(NiPd)/GCE both possessed high electrocatalytic activity
towards ORR, which originated from the encapsulation of NiPd.
A direct 4-electron reduction pathway for ORR possibly occurred
at the modified electrode. The mechanism of the process could
be expressed as following [eqs 2 and 3]:
(
)
GOx@ZIF−8 NiPd
→
glucose + OPD + O2
gluconic acid+ DAP + H2O (1)
As shown in Figure S8, the cascade reaction for the visual
detection of glucose could be combined into one step, and the
optimized conditions of pH 4.0 and 50 °C were adopted for
subsequent one-pot detection of glucose. With the increase of
the glucose concentration, the absorbance of the solution
increased gradually and its corresponding solution color
changed from very light yellow to deep yellow (Figure S9a).
There is a good linear relationship between the absorbance of
DAP and glucose concentrations in the range of 0.01-0.3 mM
with a limit of detection (LOD) of 9.2 μM, which was comparative
to other colorimetric methods as shown in Table S2. Moreover,
the specificity of the colorimetric sensor was tested using other
saccharides such as fructose, maltose, lactose, and sucrose.
The color difference can be distinguished by the naked eye as
shown in Figure S9b, suggesting a good selectivity of the
developed glucose biosensor.
(
)
(
)
glucose + GOx FAD →GOx FADH2 + gluconolactone
(2)
NiPd
(
)
(
)
GOx FADH2 + O2 → GOx FAD + H2O
(3)
Total reaction:
(
)
GOx@ZIF−8 NiPd
→
glucose + O2
gluconolactone + H2O
(4)
Based on the competitive reactions of oxygen reduction and
glucose oxidation, electrochemical glucose biosensors could be
fabricated.[14] As shown in Figure 4c, GOx@ZIF-8(NiPd)/GCE
could be used for glucose sensing. The response current
increased to reach a steady-state with addition of H2O2 and
reduced steeply with addition of glucose under constant
potential of −0.45 V. The relative standard deviation (RSD) for
16 successive determinations was 0.8% for glucose detection,
suggesting good stability and reproducibility of the glucose
biosensor.
A
well-defined linear relationship between
Figure 4. (a) CVs at GOx@ZIF-8(NiPd)/GCE in 10 mM pH 7.0 PBS containing 0, 1, 2, 3, 5, 10 mM H2O2. Scan rate is 50 mV s-1. (b) CVs at GOx@ZIF-
8(NiPd)/GCE in 10 mM pH 7.0 PBS containing 0, 1, 2, 3, 4 mM glucose. (c) Amperometric time curves at GOx@ZIF-8(NiPd)/GCE in 10 mM pH 7.0 PBS upon
successive injection of 1 mM H2O2 or 0.1 mM glucose for each step at -0.45 V.
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the current and glucose concentration can be observed from 0.1
to 1.7 mM (Figure S11). The new electrochemical glucose
biosensor exhibits much wider range of glucose detection than
that of mentioned colorimetric sensor, expanding the
applications of bioanalysis.
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In summary, we have fabricated
a
colorimetric and
electrochemical glucose sensor based on the multi-enzyme
system GOx@ZIF-8(NiPd). GOx@ZIF-8(NiPd) not only exhibited
the peroxidase-like activity but also could catalyze the oxidation
of glucose. Besides, GOx@ZIF-8(NiPd)/GCE possessed high
electrocatalytic activity for ORR and showed good
electrochemical performance toward glucose. We also believe
that the obtained ZIF-8(NiPd) has the ability of the molecule-
size-selective catalysis in the hydrogenation. In a word, we
reported a simple, facile and green method for the direct
synthesis of enzyme-embeded MOFs with multi-catalysis
properties, and the obtained nanocomposites exhibited special
nanoflower structure. Given the variety of nanozyme and
proteins, this new method opens an avenue for combining
together their properties and functionalities, displaying important
features enabling applications in biosensors, biofuel cells,
analytical devices and industrial catalysis.
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Keywords: GOx@ZIF-8(NiPd) nanoflower • artificial enzyme
system • tandem catalysis • oxygen reduction reaction • glucose
detection
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Entry for the Table of Contents
COMMUNICATION
Tandem catalysis: NiPd hollow
nanoparticles and glucose oxidase
(GOx) were simultaneously
immobilized on ZIF-8 via a co-
precipitation method. The proposed
strategy for the fabrication of artificial
multi-enzyme system builds a
potential bridge of cooperation
between nanozyme and natural
enzyme.
Q. Wang, X. Zhang, L. Huang, Prof. Z.
Zhang*, Prof. S. Dong*
Page No. – Page No.
GOx@ZIF-8(NiPd) nanoflower: an
artificial enzyme system for tandem
catalysis
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