CHEMICAL ENGINEERING JOURNAL
·
2023
·
IF 15.1
Yaoxuan Li,Lihang Yan,Guanhua Liu,Huaxun Chen,Hao Zhao,Lihui Wang,Jing Gao,Yunting Liu,Xiaobing Zheng,Yanjun Jiang
Carbon capture, utilization and storage have become a hot topic in recent years, and enzymatic CO 2 reduction benefits from high selectivity, high efficiency and mild conditions making it promising. However, the low solubility of CO 2 , poor stability of free enzyme and high cost of coenzyme limit the application. Therefore, mesoporous silica nanoflower (SNF) was used to immobilize formate dehydrogenase (FDH) by electrostatic adsorption followed by the coating of a multifunctional zeolitic imidazolate framework (ZIF-8) layer by sequential coating of Zn 2+ and 2-methylimidazole (2-MeIm), thus obtaining a novel integrated nanocatalyst ZIF-8@FDH@SNF. Regulated by controlling the ratio of ligands, the ZIF-8 coating layer not only protected the enzyme and prevented leakage, but also increased the local CO 2 concentration using the imidazole group of ZIF-8 which improved the CO 2 adsorption by 34.5% compared with SNF. And the expensive NADH was regenerated by the coupled electrocatalysis. The optimized integrated nanocatalyst showed excellent stability and reusability. Highly efficient electroenzymatic CO 2 reduction was achieved with 1.38 mM formate yield after 3 h, 48.4% higher than that without ZIF-8 layer.
研究领域:
环境科学
·
生物化学
✓ 已验证
产品关联
DOI
高影响因子
Nanoscale
·
2024
·
IF 5.8
Xinlv Peng,Caixia Pei,Eika W. Qian,Yuguang Du,Jian-Jun Li
6′-Sialyllactose (6′-SL), the most abundant sialylated human milk oligosaccharide, has attracted attention for its potential application in supplementary infant formulas. Herein, we report a facile strategy to construct a cascade bioreactor for the enzymatic synthesis of 6′-SL by co-immobilizing an enzymatic module consisting of CMP–sialic acid synthase and α-2,6-sialyltransferase into hierarchically porous MIL-53 (HP-MIL-53). The as-prepared HP-MIL-53 showed high enzyme immobilization capacity, reaching 226 mg g−1. Furthermore, the co-immobilized enzymes exhibited higher initial catalytic efficiency, and thermal, pH and storage stability than the free ones. Finally, the 6′-SL yield remained >80% after 13 cycles of use. We expect that HP-MIL-53 would have potential industrial applications in the enzymatic modular synthesis of 6′-SL and other glycans.
研究领域:
生物化学
·
食品科学
·
材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Molecular Catalysis
·
2024
·
IF 3.9
Xiangsheng Zheng,Xiaohong Hao,Yan Wang,Siyu Gao,Dantong Wen,Jinchuan Wang
The development of novel biocatalysts is essential to promote the commercialization of biodiesel production by transesterification reaction. In this paper, Rhizopus oryzae lipase (ROL) was immobilized on an amino-functionalized zirconium-based metal organoskeleton by interfacial adsorption. The immobilization conditions were optimized and the enzymatic properties were tested, and the resulting novel biocatalysts exhibited higher stability and heat resistance. SEM, XRD and BET analyses were used to characterize the biocatalysts and carrier materials. The catalytic performance of ROL@UiO-66-NH 2 in the production of biodiesel by transesterification reaction was explored, and the production process was optimized by response surface method. The results showed that the conversion rate of FAEE reached 82.05% at molar ratio of ethanol/oil of 15.43:1, reaction temperature of 50.28°C, reaction time of 120.9 min, DES addition of 48.08 wt%, biocatalyst addition of 3 wt%, and ultrasonic power of 90 W. In addition, ROL@UiO-66-NH 2 demonstrated good recyclability, with the catalytic efficiency remaining at 71.87% after five cycles.
研究领域:
生物化学
·
催化材料
·
可再生能源
✓ 已验证
产品关联
DOI
高影响因子
MICROPOROUS AND MESOPOROUS MATERIALS
·
2024
·
IF 4.8
Yang Zhou,Zhenzhu xia,Frank Peprah Addai,Jinping Chen,Chengxiang Feng,Zongjian Zhen,Juan Han,Feng Lin,Zhirong Wang,Yun Wang
Most pristine metal organic frameworks (MOFs) are inherently microporous. To introduce desired porosity for easy enzyme infiltration and immobilization, polystyrene spheres was used as sacrificial template to design hierarchical ordered micro-mesoporous truncated single-crystalline ZIF-8 (SOM-ZIF-8). The surface area and pore diameter of the SOM-ZIF-8 were 821 m 2 /g and 7.09 nm which changed to 669 m 2 /g and 4.98 nm respectively, after lipase immobilization, suggesting the pores and surface of the SOM-ZIF-8 served as binding sites for the enzyme, and could reach a loading capacity of 134 mg/g after 24 h. The optimal conditions for achieving maximum lipase activity for free LipaseELP, ZIF-8@LipaseELP and SOM-ZIF-8@LipaseELP were pH 7.8 at 45 °C, and maintained 33.67 %, 45.6 % and 57.78 % residual activity after incubation at 80 °C for 2 h. The specific activity towards tributyrin and p-nitrophenyl acetate were observed to be SOM-ZIF-8@LipaseELP (0.25 and 45.85 U/mg) compared to ZIF-8@LipaseELP (0.211 and 43.62 U/mg) and LipaseELP (0.179 and 41.09 U/mg) respectively. The SOM-ZIF-8@LipaseELP could further be recovered and reused for 9 rounds while maintaining 73.8 % of its original activity. This study demonstrates that introducing mesoporous structures into ZIF-8 could improve its binding enzyme property for enhanced hydrolytic function.
研究领域:
材料科学
·
生物技术
✓ 已验证
DOI
高影响因子
BIOCHEMICAL ENGINEERING JOURNAL
·
2017
·
IF 2.892
Yinzhou Guo,Jiangtao Liu,Kehu Zhang,Honghong Zhang,Yan Li,Zhongli Lei
In this study, a novel type of stimuli-responsive support materials was synthesized successfully by atom transfer radical polymerization (ATRP) and ring opening polymerization (ROP) of N-isopropylacrylamide (NIPAAm), tert -butyl methacrylate (tBMA) and ε-caprolactone (CL). β-Cyclodextrin (β-CD) and azobenzene (Azo) were employed as the starting groups to form PCL-hv-PNIPAAm by host–guest inclusion complexation, while PCL-PMAA was converted by simple hydrolysis of PCL-PtBMA with trifluoroacetic acid. Both PCL-PMAA and PCL-hv-PNIPAAm formed the microspheres by self-assembly. Their characteristics were confirmed by NMR, TEM, GPC, DLS, etc. Then, the microspheres were used for the immobilization of pectinase by electrostatic interaction. The optimal immobilization reaction parameters were 10 U/mL for pectinase at 25 °C for 4 h at pH = 6. Compared with free pectinase, the immobilized enzymes were found to exhibit better tolerance of variations in pH and temperature, as well as improved storage stability. Furthermore, the relative activity of the immobilized pectinase was controlled at approximately 13% when the temperature was higher than the LCST of PNIPAAm. With different light irradiation, there is approximately a 15% influence on the relative activity of the immobilized pectinase. This new enzyme support material has good environmental adaptability and can make the activity of immobilized enzymes be tailored predictably and enable the enzyme to be used as a biocatalyst for various applications in the food industry.
研究领域:
生物化学
·
材料科学
·
食品科学
✓ 已验证
DOI
高影响因子
CHINESE JOURNAL OF CHEMICAL ENGINEERING
·
2021
·
IF 3.171
Junyang Xu,Yanjun Jiang,Liya Zhou,Li Ma,Zhihong Huang,Jiafu Shi,Jing Gao,Ying He
Immobilization is an effective method to promote the application of enzyme industry for improving the stability and realizing recovery of enzyme. To some extent, the performance of immobilized enzyme depends on the choice of carrier material. Therefore, the development of new carrier materials has been one of the key issues concerned by enzyme immobilization researchers. In this work, a novel organic–inorganic hybrid material, nickel-carnosine complex (NiCar), was synthesized for the first time by solvothermal method. The obtained NiCar exhibits spherical morphology, hierarchical porosity and abundant unsaturated coordination nickel ions , which provide excellent anchoring sites for the immobilization of proteins. His-tagged organophosphate-degrading enzyme (OpdA) and ω-transaminase (ω-TA) were used as model enzymes to evaluate the performance of NiCar as a carrier. By a simple adsorption process , the enzyme molecules can be fixed on the particles of NiCar, and the stability and reusability are significantly improved. The analysis of protein adsorption on NiCar verified that the affinity adsorption between the imidazole functional group on the protein and the unsaturated coordination nickel ions on NiCar was the main force in the immobilization process, which provided an idea way for the development of new enzyme immobilization carriers.
研究领域:
生物化学
·
材料科学
·
酶工程
✓ 已验证
产品关联
DOI
高影响因子
ACS Applied Nano Materials
·
2021
·
IF 5.097
Jiawei Lu,Youran Li,Huilin Zhu,Guiyang Shi
Nanoscale particle-based enzyme immobilization carries a risk of dissolving or breaking the material when applied. One effective strategy to improve the stability and functionality of this type of nanomaterial is compounding with polymers. In this study, Fe3O4 nanoparticles were synthesized and coated with SiO2, after which magnetic hollow composite beads with nanoscale porous structures, named, lipase/Fe3O4/PAN (L/FP), were fabricated by compounding polyacrylonitrile and SiO2-coated Fe3O4 nanoparticles to immobilize Candida antarctica lipase B (CALB) in one step. Fourier transform infrared spectroscopy, scanning electron microscopy, the Brunauer–Emmett–Teller method, vibrating sample magnetometer measurements, and thermogravimetry analysis were used to analyze the structure of hollow beads. It was found that composite beads retained nanoscale channels and had a larger specific surface area (27.2 m2/g), a higher pore volume (0.09 cm3/g), and better saturation magnetization values (9.8 emu/g) than PAN hollow beads (6.2 m2/g, 0.03 cm3/g, and 0 emu/g, respectively). After optimizing fabrication and immobilization conditions, L/FP showed a high lipase capacity (50 mg protein/g support) at 2 mg/mL lipase, and the immobilized yield was up to 98.4% when the mass ratio of the starting lipase and support was 1.3 (mg lipase/g support). The immobilized lipase in L/FP showed greater thermal stability and resistance to alkali than free CALB. L/FP also had good stability in most organic solvents. In all tested cycles, it also had better reusability (78.4, 47.2, and 23.8% retained activity after 10, 20, and 30 cycles, respectively) in ester hydrolysis than CALB-immobilized Fe3O4 nanoparticles or PAN beads and had higher activity than the commercial immobilized lipase (Novo 435).
研究领域:
生物化学
·
材料科学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF COLLOID AND INTERFACE SCIENCE
·
2021
·
IF 8.128
Yuxiao Feng,Hongtong Hu,Zichen Wang,Yingjie Du,Le Zhong,Chenxi Zhang,Yanjun Jiang,Shiru Jia,Jiandong Cui
Metal-organic frameworks (MOFs) have been emerged as a promising support for immobilizing enzymes owing to the tunable porosity, high surface area, and structural diversity. However, most of these possess nanometer size and small pores, which are difficult to recover them from the reaction medium and present low immobilization efficiency and protein loading capacity, and high substrate diffusion limitations. Herein, a novel magnetic amino-functionalized zeolitic imidazolate framework-8 (ZIF-8) with 3D highly ordered macroporous structure was synthesized using the assembled polystyrene (PS) nanosphere monoliths as a template. Subsequently, catalase (CAT) molecules were immobilized on the surface of macroporous magnetic ZIF-8 and inside the macropores by precipitation, covalent binding and cross-linking. The resultant immobilized CAT showed high immobilization efficiency (58%) and protein loading capacity (29%), leading to 500% higher activity than the immobilized CAT on ZIF-8 (CAT/ZIF-8). Meanwhile, the immobilized CAT could be easily recovered with a magnet without obvious activity loss. The traditional CAT/ZIF-8 lost its activity after 6 cycles, whereas, the immobilized CAT retained 90% activity of its initial activity after reusing for 8 cycles, indicating excellent reusability. In conclusion, this study provides a facile and efficient approach to immobilize enzymes on/in MOFs with enhanced activity and excellent recyclability.
研究领域:
生物化学
·
材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Nanoscale
·
2016
·Vol. 8
·期 11
·6071-6078
·
IF 7.76
Hao Liang,Shuhui Jiang,Qipeng Yuan,Guofeng Li,Feng Wang,Zijie Zhang,Juewen Liu
Preserving enzyme activity and promoting synergistic activity via co-localization of multiple enzymes are key topics in bionanotechnology, materials science, and analytical chemistry. This study reports a facile method for co-immobilizing multiple enzymes in metal coordinated hydrogel nanofibers. Specifically, four types of protein enzymes, including glucose oxidase, Candida rugosa lipase, α-amylase, and horseradish peroxidase, were respectively encapsulated in a gel nanofiber made of Zn2+ and adenosine monophosphate (AMP) with a simple mixing step. Most enzymes achieved quantitative loading and retained full activity. At the same time, the entrapped enzymes were more stable against temperature variation (by 7.5 °C), protease attack, extreme pH (by 2-fold), and organic solvents. After storing for 15 days, the entrapped enzyme still retained 70% activity while the free enzyme nearly completely lost its activity. Compared to nanoparticles formed with AMP and lanthanide ions, the nanofiber gels allowed much higher enzyme activity. Finally, a highly sensitive and selective biosensor for glucose was prepared using the gel nanofiber to co-immobilize glucose oxidase and horseradish peroxidase for an enzyme cascade system. A detection limit of 0.3 μM glucose with excellent selectivity was achieved. This work indicates that metal coordinated materials using nucleotides are highly useful for interfacing with biomolecules.
研究领域:
生物纳米技术
·
材料科学
·
分析化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
LANGMUIR
·
2017
·
IF 3.833
Jinghui Wang,Renliang Huang,Wei Qi,Rongxin Su,Zhimin He
Enzyme-loaded water-in-oil Pickering emulsion is a promising system for biphasic catalytic reactions. In this paper, we report on oriented enzyme immobilization at the oil/water interface in a Pickering emulsion, in which CHO-Janus silica nanoparticles (CHO-JNPs) are utilized as a stabilizer of the emulsion and support for the enzyme to enhance both catalytic activity and recyclability. The catalytic performance of this immobilized enzyme (lipase from Candida sp.) was evaluated by esterification of hexanoic acid and 1-hexanol in a water/heptane biphasic medium. The results show that the specific catalytic activity of the immobilized enzyme (33.2 U mL–1) was 6.5 and 1.4 times higher than that of free enzyme (5.1 U mL–1) and encapsulated enzyme in the liquid core (23.3 U mL–1), respectively. Moreover, the immobilized enzyme demonstrated good stability and recyclability, retaining 75% of its activity after 9 cycles. We expect that oriented enzyme immobilization at the oil/water interface will be an important strategy for enhancing catalytic performance in Pickering emulsions.
研究领域:
生物化学
·
材料科学
·
催化工程
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Materials Today Chemistry
·
2022
·
IF 7.613
X. Shen,Y. Du,Z. Du,X. Tang,P. Li,J. Cheng,R. Yan,J. Cui
Zeolitic imidazolate framework (ZIF) has recently emerged as a promising material for the encapsulation of enzymes because of their high surface area and facile construction conditions. However, the enzymes are partial even completely inactive after encapsulation owing to the confinement effect and competing coordination, and otherwise, the alkaline environment caused by the protonation effect of 2-methylimidazole also damages enzyme molecules. Herein, a novel glutathione (GSH)-boosted one pot embedding strategy that enabled to rapidly encapsulate enzyme within GSH hybrid MOF (named enzyme@GMOF) with a high embedding efficiency was constructed. Hybrid of GSH and imidazole as synchronous ligands for GMOF to immobilize enzyme can offer sufficient well microenvironment for enzyme exhibiting high activity. The obtained catalysts (CAT@GZIF-67) displayed 9.0-fold higher catalytic activity than traditional ZIF-67 immobilized CAT (CAT@ZIF-67) and superior reusability and storage stability compared with CAT@ZIF-67 and free CAT. As one kind of biomacromolecules, bio-affinity of GSH can create an affinitive microenvironment for enzymes and reduce the influence of other factors during the use of biomacromolecules on their conformation and activity.
研究领域:
生物化学
·
材料科学
✓ 已验证
产品关联
DOI
高影响因子
CELLULOSE
·
2022
·Vol. 29
·期 16
·8769-8780
·
IF 6.123
Bao Chunyang,Chen Jing,Wang Yan,Yang Tao,Xu Xiaoling,Zhang Qiang
Cellulose-based matrices are expected to be ideal enzyme carriers due to their sustainability and biocompatibility. However, the linkages between immobilized enzymes and celluloses often suffer from low-density and non-biodegradability, leading to inefficient loading of enzymes as well as persistent generation of solid wastes after reuse. In the present study, cellulose-based functional materials with degradable polycarbonates brushes have been successfully synthesized as enzyme carriers via ring-opening polymerization of 5-methyl-5-allyloxycarbonyl-1,3-dioxan-2-one (MAC) following with ally epoxidation of MAC units. After covalent bonding with laccase, the resulting HPC-PMAC-Laccase could assemble in aqueous solution to form spherical nanoparticles with an enzyme immobilization efficiency of 88%. The immobilized laccase showed more tolerance towards pH and high temperature compared with free laccase. Moreover, the immobilized laccase demonstrated effective removal efficiency of bisphenol A and reached 83% in 3 h. After repeated usage for 8 times, the HPC-PMAC-Laccase still maintained relatively high enzyme activity. Especially, the polycarbonates brushes in the enzyme carriers could be totally hydrolyzed in 12 h to achieve its degradable property. Graphical abstract Cellulose-based functional polycarbonates as degradable enzyme carriers.
研究领域:
生物化学
·
材料科学
·
环境科学
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）