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DOI: 10.1039/D4NJ03303E (Paper) New J. Chem., 2024, 48, 15948-15955

Glucose oxidase intercalation into polydopamine and ZIF-8 as a highly efficient and stable bio-catalyst for H2O2 production†

Yalin Zhang , Xiaoyue Yang , Xinlong Liu , Zhijie Zhang and Xiaoyuan Liao *
College of Chemical Engineering and Materials Science, Tianjin University of Science and Technology, Tianjin, China. E-mail: liaoxy@tust.edu.cn

Received 24th July 2024 , Accepted 19th August 2024

First published on 2nd September 2024

Abstract

Glucose oxidase has great potential as a bio-catalyst for the determination of glucose and H2O2 concentration, but it is sensitive to environmental influences and has poor recoverability. To overcome this limitation, this study presents a promising approach, i.e., glucose oxidase interposed with dopamine and ZIF-8 to develop a highly efficient and stable bio-catalyst for H2O2 production while determining glucose concentrations. The successful synthesis of GOx@ZIF-8/PDA was verified by SEM, EDS, XRD, FTIR, XPS, and UV analyses; GOx@ZIF-8/PDA exhibited higher stability, better reproducibility, and excellent glucose assay potential compared with the free enzyme. After 7 days of storage, GOx@ZIF-8/PDA almost maintained its initial activity, and the catalytic activity remained at 92.15 ± 2.13% after five consecutive applications. This study provides a new strategy for the preparation of highly active and stable immobilized enzymes.

1. Introduction

Glucose oxidase (GOx) is a bio-catalyst specialising in the conversion of glucose to gluconic acid and hydrogen peroxide (H2O2).1 It excels in catalytic efficiency, specificity, safety, and selectivity compared to artificial catalysts.2 GOx is not only environmentally friendly and efficient but also highly specific and can effectively promote a wide range of chemical reactions under mild conditions.3 Therefore, it plays an important role in many fields, e.g., highly selective conversion of glucose into H2O2, providing non-invasive or microinvasive blood glucose monitoring technology for diabetics, and significantly improving health management.4 In addition, GOx, as an industrial catalyst, has an outstanding capability to drive H2O2 production and is widely used in the manufacture of oxidants, disinfectants, and bleach.5 The study of GOx as a representative of biological oxidase is helpful for deeply understanding the redox process in organisms and provides an important theoretical basis and experimental platform for further exploration in biochemistry and biomedicine fields,6 especially in modern science and industry.7

However, biomolecules are usually less stable in industrial environments and are particularly prone to inactivation in the presence of organic solvents, high temperatures, high-pressure environments, or inappropriate pH conditions. These factors significantly limit their efficiency in practical applications.8 In addition, free enzymes are easily disturbed by environmental factors and are difficult to recycle, leading to waste of resources and increased costs.9 These problems limit their widespread application.10

In recent years, metal–organic frameworks (MOFs) have gained wide application in the field of enzyme immobilization due to their unique functions.11 MOFs are three-dimensional mesh structures formed by combining organic ligands with inorganic metal ions or clusters.12 Their main advantages include high specific surface area, adjustable porosity, and structural diversity.13,14 These properties endow MOFs with great potential for enzyme immobilization.15 According to Li et al.,16 using a dual Zn source strategy, the mother liquor can be reused with zero emissions to ensure environmental protection while yielding high-quality ZIF-8. Zhang et al.17 used different solvents to synthesise three different morphologies of ZIF: ZIF-M, ZIF-P, and ZIF-L. In particular, the ZIF-M samples synthesised with methanol as a solvent showed high internal specific surface area and porosity. The structure of ZIF-8 is similar to that of sodium salt and zeolite, containing narrow six-membered annular pore windows and larger internal pores. The unique structure of ZIF gives it excellent chemical and heat resistance.18,19 Its high specific surface area and low cost make it ideal for use as a GOx carrier.

In addition, Wang et al.20 reported that ZIF-8-encapsulated GOx exhibited high activity. Conversely, Zhu et al.21 utilized MOFs as enzyme carriers; the GOx@ZIF-8 they developed was very stable under the harsh conditions that would decompose free GOx. ZIF-8 is stable in dry environments, but its structural stability may be reduced under wet or moist conditions, especially in high-pH environments. This situation will affect the long-term stability and reusability of the loaded enzyme.22,23

Dopamine (PDA) is valued for its excellent hydrophilicity and biocompatibility.24 The protective layer formed by PDA can cover the surface of ZIF-8 and the enzyme, effectively preventing non-specific adsorption, to maintain the activity and stability of the enzyme. This protective film not only enhances the thermal and chemical stabilities of the enzyme but also enables it to remain active over a wider range of temperatures and pH values.25

The synthesis of most MOFs must be carried out in organic solvents, so the in situ embedding method is not applicable.26 Immobilisation of GOx in the free state is also challenging. The embedding method has some drawbacks in immobilising the enzyme, such as leaching and inactivation of the enzyme.27 Therefore, we investigated GOx immobilisation by combining the structural advantages of ZIF-8 and the modification effect of PDA on the enzyme. In this experiment, we mainly used the surface adsorption method to assess the immobilisation of GOx on ZIF-8 and the influence of its encapsulation using PDA. Relatively little research has been done on this technique.

In this study, GOx@ZIF-8/PDA composites were prepared by the PDA-embedding method using zinc nitrate, dimethylimidazole, GOx, and PDA as raw materials. H2O2 was produced by a GOx-catalyzed oxygen reduction reaction. The enzymatic properties and reusability were investigated, and the synthesis mechanism of the GOx@ZIF-8/PDA biocomposite has been discussed herein.

2. Experimental

2.1 Characterization

An X-ray powder diffractometer (XRD) from Bruker, Germany, was used to analyze the phase and composition of the samples at a scanning rate of 5° min−1 using copper as the diffraction target. SEM was performed with an MIRA LMS electron microscope from TESCAN, Czech Republic. The catalyst was characterized by X-ray photoelectron spectroscopy (XPS) using a K-Alpha photoelectron spectrometer, Thermo Scientific, USA. The attenuated total reflection Fourier transform infrared (ATR-FTIR) spectra of the samples were obtained with the Nicolet 6700 (Brock, America). The measuring range of the Fourier transform infrared spectrum is 4000–500 cm−1. N2 adsorption–desorption measurements were performed at the temperature of liquid nitrogen (−196 °C) using instruments from Canta AUTOSORB IQ.

2.2 Fabrication of samples

2.2.1 Synthesis of ZIF-8. Zinc nitrate (2.975 g) and 2-methylimidazole (6.568 g) were dissolved in 50 mL of anhydrous methanol. The mixture was ultrasonicated for 15 min; 2-methylimidazole was added to zinc nitrate dropwise, stirred for 1 h, and then left for 24 h. The reaction liquid and precipitate were finally transferred to a 50-mL centrifuge tube and centrifuged at 8000 rpm for 10 min. The sediment was washed with anhydrous methanol thrice and then collected and dried in an oven at a set temperature.
2.2.2 Preparation method of ZIF-8 immobilized enzyme. A certain amount of prepared ZIF-8 and enzymes of different qualities (ZIF-8 and enzymes in a certain proportion) were weighed, and a certain volume of tris (50 mM, pH 7) was added. The mixture was stirred at a certain temperature for some time and allowed to stand for 12 h. Finally, it was vacuum freeze-dried for 48 h to obtain dry ZIF-8@GOx.
2.2.3 Preparation of GOx@ZIF-8/PDA. A gram of GOx@ZIF-8 was dispersed in 10 mL of freshly prepared Tris–HCl buffer (10 mM, pH 8.5) with 10–40 mg PDA successively. The mixture was oscillated at 180 rpm for 10 h at 25 °C in a bench temperature oscillator. The reaction liquid and precipitate were subjected to vacuum freeze-drying for 48 h to obtain dry GOx@ZIF-8/PDA (Scheme 1).
image file: d4nj03303e-s1.tif
Scheme 1 Preparation of GOx@ZIF-8/PDA.

2.3 Bio-catalytic tests

The changes of enzyme activity of GOx@ZIF-8/PDA at different temperature and pH were studied. First, a solution containing 200 mM glucose was mixed with 20 mg of GOx@ZIF-8/PDA, and the pH of the solution was adjusted to be between 5 and 8 at 25 °C for the enzymatic reaction. The enzyme activity was measured. Using the same solution, enzyme activity was measured again at a temperature range of 25 to 45 °C.
image file: d4nj03303e-t1.tif

H2O2 was prepared using a GOx-catalysed oxygen reduction method by adding 20 mg of GOx@ZIF-8/PDA to 100 mL of glucose solution (200 mM) and stirring with continuous oxygenation. One milliliter of the solution was acquired every hour and the absorbance was measured by a UV spectrophotometer. H2O2 yield was calculated based on the change in absorbance. Enzyme activity was determined by H2O2 yield. The method of calculation was adopted from the literature.19,28

3. Results and discussion

3.1 Scanning electron microscopy (SEM)

The morphologies of the prepared ZIF-8, GOx@ZIF-8, and GOx@ZIF-8/PDA were determined by scanning electron microscopy. Particle sizes were measured and compared as shown in Fig. 1, which shows that the synthesized ZIF-8 was a diamond-shaped dodecahedron with an average diameter of 559 nm.29 This morphology is similar to that of ZIF-8 synthesized in methanol as previously reported. By comparing Fig. 1(a) and (b), it is found that the morphology of GOx@ZIF-8 is similar to that of ZIF-8, but the morphology and size of GOx@ZIF-8 are more uniform while the particle surface is rougher.30 It can be observed from Fig. 1(c) that the mean diameter of GOx@ZIF-8 increases to ∼890 nm. Compared with ZIF-8, the crystal surface is rougher, and the grain size increases due to the external modification after the addition of GOx. A comparison of GOx@ZIF-8/PDA with GOx@ZIF-8 revealed that the addition of PDA did not change the basic shape of the particles, but the surface of the particles became rougher, and the average size of GOx@ZIF-8/PDA increased by ∼1354 nm compared with GOx@ZIF-8. The preliminary results show that PDA was successfully coated on the biocomposite GOx@ZIF-8. A comparison of Fig. 1(d), (e) and (f) further proves that the addition of GOx and PDA does not change the shape of the ZIF-8 rhombohedral dodecahedron.
image file: d4nj03303e-f1.tif
Fig. 1 SEM: (a) and (d) ZIF-8, (b) and (e) GOx@ZIF-8 and (c) (f) GOx@ZIF-8/PDA.

3.2 XRD and FT-IR

We confirmed that the crystallinity of ZIF-8 was not destroyed after the addition of GOx and PDA. As shown in Fig. 2(a), X-ray diffraction (XRD) shows that ZIF-8, GOx@ZIF-8, and GOx@ZIF-8/PDA have six similar sharp diffraction peaks. The diffraction peaks appear at 7.26°, 10.36°, 12.68°, 14.65°, 16.38°, and 17.98°. The XRD patterns of ZIF-8, GOx@ZIF-8, and GOx@ZIF-8/PDA show that the XRD patterns remain unchanged regardless of whether GOx or PDA is added.22
image file: d4nj03303e-f2.tif
Fig. 2 (a)The generated XRD patterns and (b) FT-IR spectra of samples.

The immobilization process of GOx was characterized by infrared spectroscopy (FTIR), and the results are shown in Fig. 2(b). The peaks at 1590–1600 cm−1, corresponding to amide I, were mainly derived from the C–O stretching mode, indicating the presence of enzymes in the composite. ZIF-8, GOx@ZIF-8, and GOx@ZIF-8/PDA presented peaks at 1560 cm−1, 742 cm−l, and 1310 cm−1. Two distinct peaks were produced at 1560 cm−1 and 742 cm−1, corresponding to the C[double bond, length as m-dash]C and C–H of 2-methylimidazole functional groups, respectively. At 1310 cm−1, the peak of the imidazole ring corresponded to the C–C stretching vibration. Compared with ZIF-8, the immobilized enzymes GOx@ZIF-8 and GOx@ZIF-8/PDA showed new characteristic peaks at 1540 cm−1 and 1650 cm−1, corresponding to the co-production of amide II by N–H bending and C–N stretching, and the coordination of Zn2+ with carboxyl groups on the enzyme, respectively.31 It was thus confirmed that the composite contained the protein GOx, indicating that GOx was adsorbed onto ZIF-8. The PDA-modified immobilized enzyme GOx@ZIF-8/PDA showed a wide infrared spectral band from 3700 cm−1 to 3150 cm−1, corresponding to the stretching of alcohol, catechol, and N–H bonds in the PDA structure. The results indicated that the immobilized enzyme GOx@ZIF-8/PDA was successfully prepared from the functional groups.25

3.3 BET

The pore structures of catalysts were studied by N2 adsorption. The adsorption–desorption isotherms showed typical I-shaped curves, confirming the presence of micropores in the samples (Fig. 3 and Fig. S1, ESI†). According to the data in Table 1, GOx@ZIF-8/PDA has the smallest specific surface area of 146.3 m2 g−1. The specific surface areas of GOx@ZIF-8 and ZIF-8 are 370.5 m2 g−1 and 1775.2 m2 g−1, respectively. The average pore sizes were 1.85 nm, 1.76 nm, and 1.59 nm and the total pore volumes were 0.07 mL g−1, 0.16 mL g−1, and 0.71 mL g−1, respectively.32
image file: d4nj03303e-f3.tif
Fig. 3 (a) N2 adsorption/desorption isotherms of the samples and (b) aperture distribution.
Table 1 Textural properties of catalysts
Sample Specific surface area (m2 g−1) Mean aperture (nm) Micropore volume (mL g−1)
ZIF-8 1775.2 1.59 0.71
GOx@ZIF-8 370.5 1.76 0.16
GOx@ZIF-8/PDA 146.3 1.85 0.07

The BET-specific surface area and total pore volume of GOx@ZIF-8 were lower than those of ZIF-8, but the average pore size was larger than that of ZIF-8, indicating that the added GOx filled the original pores of ZIF-8 and successfully adsorbed onto it.33 In addition, the specific surface area and pore volume of GOx@ZIF-8/PDA were smaller than those of GOx@ZIF-8, while the average pore diameter was larger than that of GOx@ZIF-8. This indicated that PDA was encapsulated on the surface and in some of the pores of GOx@ZIF-8; this observation agrees with the findings from SEM observations.

3.4 XPS

XPS characterization provided chemical information on the surface of ZIF-8, GOx@ZIF-8, and GOx@ZIF-8/PDA.29,30 Wide-scan XPS spectra show the presence of C, O, N, S, and Zn in GOx@ZIF-8 and additional inclusions in GOx@ZIF-8/PDA (Fig. S2, ESI†). It is confirmed that PDA was successfully loaded into GOx@ZIF-8, and peaks corresponding to Zn 2p (Fig. 4a) and N 1s (Fig. 4b) can be observed in the XPS spectra of GOx@ZIF-8 and GOx@ZIF-8/PDA.34
image file: d4nj03303e-f4.tif
Fig. 4 XPS spectra of the samples. (a) N 1s and (b) Zn 2p spectra of catalysts.

In addition, the XPS Zn 2p spectra (Fig. 4a) show that the two characteristic peaks are located at the binding energy of 1021.35 eV and 1044.55 eV, which belong to the two dimorphs Zn 2p3/2 and Zn 2p1/2. The XPS spectrum of N 1s (Fig. 4b) shows that GOx@ZIF-8/PDA contains three nitrogen elements with binding energies of 398.15, 398.60, and 400.65 eV, respectively. Furthermore, in Fig. 4b, the peak at 400.65 eV represents a terminal –NH2 group. By analyzing ZIF-8 and GOx@ZIF-8, we find that the –NH2 binding energy of GOx@ZIF-8 shifts to a higher value and the peak intensity is also higher. This suggests a stronger interaction between them. This change implies more binding of ZIF-8 to the –NH2 group after the addition of GOx, which further indicates that the enzyme is successfully loaded on ZIF-8.35 The peak value at 398.15 eV indicates that sp2-bonded nitrogen in PDA shifts towards higher binding energy than the nitrogen in GOx@ZIF-8/PDA. This implies that more sp2-bonded nitrogen is retained after PDA encapsulation, indicating a stronger interaction between them. This enhanced interaction prompts and helps immobilize the enzyme more efficiently.

3.5 Bio-catalytic tests

According to Fig. 5(a) and 6(a), the enzyme activity reaches its highest value when the dosage of the enzyme is 10%, and the yield of H2O2 is 555.6 μmol h−1 g−1. However, with further increases in the enzyme dosage, the enzyme activity shows a downward trend. This phenomenon may be due to the overcrowding of the immobilized enzyme space, which hinders the mass transfer of the substrate.36 Therefore, the amount of enzyme added was selected as 10%.
image file: d4nj03303e-f5.tif
Fig. 5 H2O2 production as a function of (a) GOx dosage over ZIF-8, (b) PDA loading over GOx@ZIF-8/PDA, (c) temperature, and (d) pH value.

image file: d4nj03303e-f6.tif
Fig. 6 H2O2 production as a function of (a) different GOx dosage, (b) PDA loading, (c) temperature, and (d) pH value.

The effect of PDA content on fixation is shown in Fig. 5(b) and 6(b). The enzyme activity of the immobilized enzymes first increased and then decreased with the increase in PDA content, and the maximum H2O2 yield was 2520.3 μmol h−1 g−1 when the PDA content reached 3%. This is because the catechol group in PDA can induce complexation with zinc ions on the surface of ZIF-8, forming a hydrophilic PDA coating with a controllable thickness on the surface of the immobilized enzyme. These changes help prevent the collapse and dissolution of the immobilized enzyme. With the increase in PDA content, the hydrophilic coating gradually thickens, the hydrophilicity of the immobilized enzyme increases, and the enzyme activity gradually increases. However, when the PDA content exceeds 3%, the PDA layer becomes too thick, preventing the substrate from approaching the catalytic center of the enzyme, and the enzyme activity of the immobilized enzyme gradually decreases. Therefore, 3% PDA is the best immobilization load.

According to previous reports, free GOx performs best at 40 °C.37 As can be seen in Fig. 5(c) and 6(c), GOx@ZIF-8/PDA performs best at 25 °C. After immobilization, the optimal reaction temperature decreases slightly. During the substrate reaction, GOx fixed on the ZIF-8/PDA carrier may exhibit higher activity than GOx in its free state. The literature also indicates that free GOx achieves optimal activity at pH 5, while the optimal pH of GOx fixed on the ZIF-8/PDA carrier is 8. After immobilization, the optimal pH value increased slightly. During the substrate reaction, GOx fixed on the ZIF-8/PDA carrier may exhibit higher activity than GOx in the free state.

3.6 Stability and reusability

Storage stability and reproducibility of enzymes are key to the development of good bio-catalysts. The storage stability curves of free GOx and GOx@ZIF-8/PDA at 4 °C are shown in Fig. 6a. After being stored at 4 °C for 7 d, the relative activity of free GOx was only 60.12 ± 3.26%, while that of GOx@ZIF-8/PDA was close to 96.31 ± 2.87%. Results showed that the storage stability of immobilized GOx was significantly higher than that of free GOx, which could be related to the protective effect of ZIF-8/PDA on the enzyme. In addition, recyclability tests showed that the enzyme activity of GOx@ZIF-8/PDA remained at ∼92.15 ± 2.13% after five reuses (Fig. 7b). According to SEM, there was no significant change in the morphology of the reused samples (Fig. S3, ESI†).
image file: d4nj03303e-f7.tif
Fig. 7 (a) Effect of storage time (4 °C) and (b) reusability.

4. Conclusion

In this work, we successfully synthesized GOx@ZIF-8 biocomposites and coated them with PDA for H2O2 production. The optimal operating conditions for GOx@ZIF-8/PDA were pH 8.0 and 25 °C, when the highest H2O2 yield (2520.3 μmol h−1 g−1) was achieved. In addition, after five repeated recycles, the activity of GOx@ZIF-8/PDA could be maintained at approximately 92.15%. This is because ZIF-8 has a large specific surface area, which helps effectively disperse GOx, enhancing its activity. Our observations indicate that the introduction of PDA helps improve the activity of GOx@ZIF-8 biocomposites. In addition, GOx@ZIF-8/PDA has better reusability and storage stability compared to free GOx. The proposed method is expected to provide technical support for the construction of efficient, stable, and reusable bio-catalysts to realize efficient and low-cost practical improvements in enzyme catalysis and bioanalysis.

Author contributions

Y. Zhang: formal analysis, investigation, writing – review & editing. X. Yang: investigation. X. Liu: data curation, validation. Z. Zhang: investigation, validation. X. Liao: project administration, writing – review & editing.

Data availability

The authors declare that all data supporting the findings of this study are available within the article and its supplementary information files and from the corresponding author on reasonable request.

Conflicts of interest

There are no conflicts to declare.

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Footnote

† Electronic supplementary information (ESI) available. See DOI: https://doi.org/10.1039/d4nj03303e
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