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
NEW JOURNAL OF CHEMISTRY
·
2020
·Vol. 44
·期 34
·14379-14388
·
IF 3.288
Fenfen Zhu,Wei Xu,Xiao Li,Hao Meng,Yide Han,Junbiao Wu,Junli Xu,Yan Xu,Xia Zhang
Enzyme immobilization engineering is considered a valid strategy to improve the insensitivity of free enzymes to extreme conditions and thus extend their utilization in actual reactions. Although metal–organic frameworks (MOFs) are extensively applied as supports in enzyme immobilization, their separation from the liquid system after catalytic processes is problematic. In comparison, MOF-based membranes show more convenience in the subsequent solid–liquid separation. In this work, we constructed hybrid membranes by incorporating UiO-66 particles into porous polyvinylidene fluoride (PVDF) and then used them to immobilize lipase for the first time. Because of the strong affinity of UiO-66 towards lipase and the large cavity of PVDF, the hybrid membranes exhibited excellent immobilization ability towards lipase, and the resulting immobilized lipase showed an elevated operating temperature in the range of 40–70 °C with preserved activity and evidently improved thermal stability even after being stored at high temperatures for a definite time. The application of PVDF membrane makes the subsequent separation of the immobilized enzyme from the solutions easier. The immobilization kinetics, isotherm, and thermodynamics were analyzed in detail, and the immobilization mechanism was proposed. Furthermore, the immobilized lipase showed reusability and retained 48.2% of its initial activity after 7 cyclic reactions.
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
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
·
2014
·
IF 2.745
Zhongjie Wu,Wei Qi,Mengfan Wang,Rongxin Su,Zhimin He
The metal ceramic powder (MCP) was used for lipase immobilization. The MCP containing Ni 2+ (Ni-MCP) exhibited the best affinity to lipase . The effects of heating rate, lipase concentration and immobilization time on immobilized lipase (Ni-MCP-lipase) activity were measured. Under the optimal preparation conditions (heating rate: 1 °C/min, lipase concentration: 9 mg/mL, immobilization time: 8 h), Ni-MCP-lipase could obtain 1.4 U/g and 216% of activity yield. The Ni-MCP-lipase, with improved thermal stability and storage stability, had optimal pH value of 6.0 and optimal temperature of 40 °C. The characterizations clarified the effect of heating rate on Ni-MCP-lipase activity, and confirmed that lipase had been efficiently immobilized on Ni-MCP surface. Finally, cinnamyl acetate synthesis demonstrated that Ni-MCP-lipase had improved efficiency compared with free lipase. Under the optimal reaction conditions (Ni-MCP-lipase loading: 3 g; reaction temperature: 35 °C; acetic acid/cinnamyl alcohol: 2:1 in 15.0 mL reaction system), the cinnamyl acetate yield would reach 62.56%.
研究领域:
生物化学
·
酶工程
✓ 已验证
DOI
高影响因子
Journal of the Taiwan Institute of Chemical Engineers
·
2019
·
IF 3.834
Wenjing Cheng,Yun Li,Xiaoying Li,Wenjing Bai,Yunxiao Liang
A monolithic macroporous silica (MMS) was prepared by using a pillared epoxy resin macroporous polymer as template. Polydopamine (PDA) as a spacer-arm polymer was modified on the surface of MMS for immobilization of Candida rugosa lipase (CRL), aiming to improve the performance of CRL and overcome the limitations of the immobilized enzymes on mesoporous materials and fine particles. The immobilization conditions and the properties of the immobilized CRL were investigated. The as-prepared monolithic macroporous materials were characterized by SEM, TEM, MIP, BET, FT-IR and TG-DTA. The results revealed that MMS possessed two sets of well-defined and uniform continuous macroporous channels (pore size of 300–500 nm), high mechanical strength, large pore volume and specific surface area, and that the PDA/MMS macroporous composite was constructed by PDA/SiO 2 /PDA nano-film with a thickness of about 50 nm. Because of its surface chemical properties and unique macropore structure, the PDA/MMS composite provided a simple, cost-effective way to enhance the catalytic activity of directly immobilized enzyme. The activity recovery of CRL–PDA/MMS was 201%, and the stability of the immobilized lipase was remarkably improved. Moreover, this biocatalyst can be easily recovered from the reaction system without centrifugation or filtration.
研究领域:
生物化学
·
材料科学
·
酶工程
✓ 已验证
DOI
高影响因子
NEW JOURNAL OF CHEMISTRY
·
2018
·Vol. 42
·期 16
·13471-13478
·
IF 3.201
Weifan Ren,Xu Fei,Jing Tian,Yao Li,Muzi Jing,Huan Fang,Longquan Xu,Yi Wang
Enzyme–inorganic hybrid nanoflowers have drawn extensive research interest for enzyme immobilization owing to their enhanced enzymatic activity, high surface area, and excellent chemical stability. However, their low mechanical stability and challenging separation hinder their application. Herein, we report a facile and effective strategy to construct nanoflowers–PVA–chitosan composite (NPC) hydrogels that have excellent mechanical strength, high catalytic activity, and are easy to separate. Lipase–Cu3(PO4)2·3H2O nanoflowers were uniformly immobilized in hydrogel networks, and the substrate and the product can travel freely. The excellent mechanical properties of the hydrogels effectively protect the fragile nanoflowers from external stress, ensuring enzyme activity. Compared with free lipase (97.28 U g−1), NPC3 exhibited a higher enzymatic activity (146.12 U g−1) at 37 °C and pH 7.4. Furthermore, hydrogels as bulk materials can be processed into various physical forms, such as thin films and spheres. The product can easily flow out without the need for a separation process. It is expected that this immobilization method would have great potential in industrial catalysis.
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
Journal of Materials Chemistry A
·
2014
·Vol. 2
·期 43
·18339-18344
·
IF 0
Zhiming Chen,Wenhui Xu,Li Jin,Juanjuan Zha,Tingxian Tao,Ying Lin,Zhilin Wang
Amine-functionalized Fe3O4@C nanoparticles have been successfully synthesized on a large scale via a solvothermal route. The morphology, structure and properties of the Fe3O4@C nanoparticles were investigated through different analytical tools. Due to the magnetic nature and the presence of amine-functionalized groups, the as-prepared Fe3O4@C nanoparticles were employed as magnetic carriers for lipase immobilization. Our results indicate that the lipase loading amount on the magnetic Fe3O4@C nanoparticles was about 115.6 mg of protein per g. The factors related to the catalytic activity of the immobilized lipase on the magnetic carriers were systematically investigated. Hydrolytic activity tests reveal that the immobilized lipase retains about 93% of the free enzyme activity. It should be mentioned that the thermal stability of the immobilized lipase was strikingly higher than that of the free lipase. Most importantly, the immobilized lipase retained more than 68% of its initial activities after 10 times reuse. It is hoped that the amine-functionalized Fe3O4@C nanoparticles may find an application in biotechnology and catalysis.
研究领域:
生物技术
·
催化科学
✓ 已验证
产品关联
DOI
RSC Advances
·
2015
·Vol. 5
·期 29
·23039-23045
·
IF 3.84
Weiwei Zhu,Yijing Li,Fang Zeng,Hang Yin,Liyuan Wang,Hao Zhu
Superparamagnetic Fe3O4 nanoparticles with diameter about 18 nm were prepared by a solvothermal method. A simple and green method was used to prepare amino-rich magnetic nanoparticles. The magnetic nanoparticles were modified by polyethylenimine (PEI) which is a polycationic polymer when pH < 10. The resulted magnetic nanoparticles were activated by glutaraldehyde to obtain nanoscale support for Candida rugosa Lipase (CRL) immobilization. The CRL was immobilized on the magnetic nanoparticles covalently, as well as via ionic exchange. The structure and magnetic behavior of the magnetic nanoparticles were confirmed by transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FT-IR), and vibrating sample magnetometer (VSM). Then the properties of the immobilized CRL were investigated, and the results showed that the obtained immobilized lipase displayed good reusability and applicability. The immobilized Candida rugosa Lipase (ICRL) presented wider pH tolerance (residual activity > 80% in a pH range from 5.5 to 8.0) than free Candida rugosa Lipase (residual activity decreased rapidly when the pH values were away from 7.0). ICRL showed excellent thermal stability (the relative of ICRL > 90%) after keeping in the water bath at 50 °C for 150 min while free Candida rugosa Lipase (FCRL) was absolutely deactivated. After being reused 10 times, ICRL maintained 60% relative activity.
研究领域:
生物化学
·
纳米生物技术
·
酶工程
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF FOOD BIOCHEMISTRY
·
2017
·Vol. 41
·期 5
·e12395
·
IF 1
Shuai Cui,Qin-Wei Zhou,Xiao-Ling Wang,Si-Qi Yang,Kai Chen,Zhi-Yuan Dai,Yao-Wen Huang,Tao Zhou
Bovine pancreatic lipase was immobilized onto N -succinyl-chitosan beads by using N -(3-dimethylaminopropyl)- N ′-ethylcarbodiimide (EDC)/ N -hydroxysuccinimide (NHS) as the activating agent. The immobilized lipase was characterized by Fourier transform infrared spectra and scanning electron microscopy. The activity of the immobilized lipase obtained under the optimized immobilization conditions was found to reach 1,480 U/g, with enzyme activity recovery of 74.5%. Compared to the free lipase, thermal stability of the immobilized lipase was greatly improved. The reusability study indicated that the immobilized lipase retained 76.6% of its initial activity after being recycled five times. A preliminary study indicated that the prepared immobilized lipase can effectively enrich the polyunsaturated fatty acid in fish oil (increasing from 45.1 to 67.7%), of which the combined docosahexaenoic acid and eicosapentaenoic acid contents increased from 16.3 to 27.1%. Practical applications To overcome the drawbacks of using free lipase, an effective method was developed by immobilization of lipase onto N -succinyl-chitosan beads using EDC/NHS as the activating agent. The immobilized lipase prepared by this method may find application in the enrichment of polyunsaturated fatty acids of fish oil.
研究领域:
生物化学
·
食品科学
✓ 已验证
产品关联
DOI
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2021
·
IF 5.268
Hongbo Suo,Moju Li,Renmin Liu,Lili Xu
In this study, imidazolium-based ionic liquid with [tf 2 N] − as the anion was successfully grafted to magnetic polydopamine nanoparticles (MPDA). The prepared materials were well characterized and used as supports for lipase immobilization. The immobilized lipase (PPL-ILs-MPDA) exhibited excellent activity and stability. The specific activity of PPL-ILs-MPDA was 2.15 and 1.49 folds higher than that of free PPL and PPL-MPDA. In addition, after 10 rounds of reuse, the residual activity of PPL-ILs-MPDA was 86.2 % higher than that of PPL-MPDA (75.4 %). Furthermore, the kinetic assay indicated that the affinity between PPL-ILs-MPDA and substrate had increased. Analysis of the secondary structure using circular dichroism was used to explain the mechanism underlying the improvement in the performance of PPL-ILs-MPDA. In addition, the immobilized lipase can be easily separated from the reaction system with a magnet. The observations regarding the development of new supports for lipase immobilization may provide new ideas regarding further studies in this field.
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
Scientific Reports
·
2017
·Vol. 7
·期 1
·1-9
·
IF 4.259
Yi Shixiong,Dai Fangyin,Zhao Cunyi,Si Yang
Enzyme-immobilized nanoparticles that are both catalysis effective and recyclable would have wide applications ranging from bioengineering and food industry to environmental fields; however, creating such materials has proven extremely challenging. Herein, we present a scalable methodology to create Candida rugosa lipase-immobilized magnetic nanoparticles (L-MNPs) by the combination of nonionic reverse micelle method and Fe 3 O 4 nanoparticles. Our approach causes the naturally abundant and sustainable Candida rugose lipase to ordered-assemble into nanoparticles with high catalytic activity and durability. The resultant L-MNPs exhibit the integrated properties of high porosity, large surface area, fractal dimension, robust enzymatic activity, good durability, and high magnetic saturation (59 emu g −1 ), which can effectively catalyze pentyl valerate esterification and be easily separated by an external magnet in 60 second. The fabrication of such fascinating L-MNPs may provide new insights for developing functional enzyme-immobilized materials towards various applications.
研究领域:
生物工程
·
食品工业
·
环境科学
✓ 已验证
DOI
PubMed
高影响因子
JOURNAL OF POROUS MATERIALS
·
2019
·Vol. 27
·期 2
·549-554
·
IF 1.947
Chen Meng,Wu Haoming,Li Zhentao,Wu Keke,Jiao Yanpeng,Zhou Changren
Chitin/graphene oxide (Ch/GO) composite aerogel beads were fabricated by a simple and environmentally friendly method for lipase immobilization. The morphology and specific surface area of these beads were investigated by scanning electron microscopy (SEM) and Brunauer–Emmett–Teller (BET), respectively. The results revealed that the prepared beads showed three-dimensional porous structure, and GO was successfully bound to chitin with enhanced surface area and mechanical strength. Candida rugose lipase (CRL) was immobilized on Ch/GO aerogel beads under optimum conditions by adsorption and subsequent cross-linking with glutaraldehyde which is added in the presence of the unbound proteins by conjugation. The maximum immobilization capacity of Ch, Ch/GO-5, Ch/GO-10 were 129.9, 141.1, 151.9 mg/g support . The immobilized lipases exhibited good temperature and thermal stability in comparison to free CRL. After recycling 5 times, the immobilized lipases remained more than 90% of their initial activity and the activity of Ch/GO-10 could remain 84.2% of free CRL. With these desired characteristics, the design of Ch/GO composite aerogel beads for lipase immobilization may have potential applications in various lipase-based industrial processes.
研究领域:
生物化学
·
材料科学
✓ 已验证
DOI
高影响因子
JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
·
2017
·Vol. 17
·期 1
·370-376
·
IF 1.483
Xia Guo-Hua,Liu Wei,Jiang Xiao-Ping,Wang Xiang-Yu,Zhang Ye-Wang,Guo Jianyong
Magnetic Fe3O4 nanoparticles were prepared through hydrothermal method and coated with silica on the surface to obtain Fe3O4@SiO2 core–shell nanoparticles. After modification with different functional groups including aldehyde,
amine and diimide, the nanoparticles were used as carrier for covalent immobilization of lipase. The nanoparticles with aldehyde groups showed highest immobilization yield (52.8%) and efficiency (86.5%). And the immobilization conditions including pH, temperature and the concentration of enzyme
were optimized. After immobilization, the K
m of lipase was altered from 2.3 to 3.2 mM. The thermal stability and pH stability were enhanced by immobilization at the investigated conditions: pH 5.0–8.0 and temperature 30–70 °C. After 10 batches conversion of
4-Nitrophenyl palmitate into p-Nitrophenol, the immobilized lipase retained over 75% of the original activity. Compared with the commercial lipase Novozym435, the immobilized lipase showed better stability and higher catalytic efficiency. These results demonstrate that the immobilized lipase
on the modified Fe3O4@SiO2 magnetic nanoparticles has enhanced stability and reusability, which make lipase of potential interest in a number of industrial applications.
研究领域:
生物化学
·
纳米材料科学
·
酶工程
✓ 已验证
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）