ACS Applied Materials & Interfaces
·
2015
·
IF 6.723
Yanning Qu,Renliang Huang,Wei Qi,Rongxin Su,Zhimin He
Colloidosomes are promising carriers for immobilizing enzyme for catalytic purposes in aqueous/organic media. However, they often suffer from one or more problems regarding catalytic performance, stability, and recyclability. Here, we report a novel approach for the synthesis of cross-linkable colloidosomes by the selective polymerization of dopamine at oil/water interfaces in a Pickering emulsion. An efficient enzyme immobilization method was further developed by covalently bonding enzymes to the polydopamine (PDA) layer along with the formation of such colloidosomes with lipase as a model enzyme. In this enzyme system, the PDA layer served as a cross-linking layer and enzyme support for simultaneously enhancing the colloidosomes’ stability and improving surface availability of the enzymes for catalytic reaction. It was found that the specific activity of lipases immobilized on the colloidosome shells was 8 and 1.4 times higher than that of free lipase and encapsulated lipase positioned in the aqueous cores of colloidosomes, respectively. Moreover, the immobilized lipases demonstrated excellent operational stability and recyclability, retaining 86.6% of enzyme activity after 15 cycles. It is therefore reasonable to expect that this novel approach for enzyme immobilization has great potential to serve as an important technique for the construction of biocatalytic systems.
研究领域:
材料科学
·
生物化学
·
催化工程
✓ 已验证
DOI
高影响因子
PROCESS BIOCHEMISTRY
·
2021
·
IF 3.757
Wenfeng Zhou,Xiaohong Zhou,Wei Zhuang,Rijia Lin,Ye Zhao,Lei Ge,Ming Li,Jinglan Wu,Pengpeng Yang,Hongman Zhang,Chenjie Zhu,Hanjie Ying
To effectively immobilize an enzyme while maintaining its high activity and stability, the design of supports with controlled geometric structures and heterogeneous surface properties is desirable. Towards this goal, heterogeneous titanium dioxide (TiO 2 ) surfaces with controlled pore sizes were synthesized in this study and used to efficiently immobilize lipase. The immobilized lipase activity increased by a factor of 1.31 with an increase in the TiO 2 pore size from 11.46 to 21.14 nm. The highest protein loading of 15.52 mg/g was achieved in ethenyl triethoxy silane (ETS)-modified TiO 2 (E-P25) after immobilizing the enzymes at 30 ℃, pH 7.33 for 3 h and using a protein concentration in solution of 0.176 mg/mL. Among the different surface functionalities, the highest activity yield of 428.04 % was accomplished by using TiO 2 calcinated at 650 ℃ and modified by ETS as immobilization support. The immobilized enzymes showed excellent storage stability and retained almost 95 % of their activity after being stored at 4 ℃ for 8 weeks. This research provides experimental evidence that highlights the importance of studying of enzyme immobilization on the supports with synergistically designed geometric structures and surface chemical properties.
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
Polymers
·
2018
·Vol. 10
·期 5
·523
·
IF 2.935
Limin Zang,Xuan Qiao,Lei Hu,Chao Yang,Qifan Liu,Chun Wei,Jianhui Qiu,Haodao Mo,Ge Song,Jun Yang,Chanjuan Liu
Two magnetic supports with different morphologies and particle sizes were designed and prepared for cellulase immobilization based on chitosan and industrial by-product magnetic coal fly ash (MCFA). One was prepared by coating chitosan onto spherical MCFA particles to form non-porous MCFA@chitosan gel microcomposites (Support I) with a size of several micrometers, and the other was prepared using the suspension method to form porous MCFA/chitosan gel beads (Support II) with a size of several hundred micrometers. Cellulase was covalent binding to the support by glutaraldehyde activation method. The morphology, structure and magnetic property of immobilized cellulase were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and a vibrating-sample magnetometer. The cellulase loading on Support I was 85.8 mg/g with a relatlvely high activity recovery of 76.6%, but the immobilized cellulase exhibited low thermal stability. The cellulase loading on Support II was 76.8 mg/g with a relative low activity recovery of 51.9%, but the immobilized cellulase showed high thermal stability. Cellulase immobilized on Support I had a glucose productivity of 219.8 mg glucose/g CMC and remained 69.9% of the original after 10 cycles; whereas the glucose productivity was 246.4 mg glucose/g CMC and kept 75.5% of its initial value after 10 repeated uses for Support II immobilized cellulase. The results indicate that the two supports can be used as cheap and effective supports to immobilize enzymes.Keywords:magnetic composites;chitosan;coal fly ash;enzyme immobilization
研究领域:
生物工程
·
环境科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
RSC Advances
·
2017
·Vol. 7
·期 20
·12283-12291
·
IF 3.108
Yicheng Bi,Hua Zhou,Honghua Jia,Ping Wei
In our study, a polytetrafluoroethylene (PTFE) open-tubular enzyme-immobilized microreactor has been successfully prepared using dopamine polymerization and multi-layer deposition. The polydopamine layer was utilized as a primer layer in the microchannel to provide PTFE surface reactable groups, and polyethylenimine and Candida antarctica lipase B were alternatively adsorbed on the PTFE surface by the layer-by-layer method. The lipase loading kept increasing as the number of layers increased and reached a plateau at the 8th layer. The formation of multilayers and increase of enzyme loading were described and explained by the water contact angle measurement, Fourier transform infrared spectroscopy (FI-IR), and X-ray photoelectron spectroscopy, while the morphological characteristics were observed using Atomic Force Microscopy (AFM) and field emission scanning electron microscopy (FE-SEM). Preparation of a wax ester using the microreactor had much better production efficiency (35 minutes to reach 95% yield) than that using traditional reactors (over 4 hours to complete the reaction). Very excellent stability can be achieved by the microreactor, which could be used for 144 hours with the residual activity remaining at 83% of the initial activity.
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
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
·
2020
·Vol. 21
·期 24
·9529
·
IF 4.556
Shanxia Jin,Liping Liu,Mengying Fan,Yaru Jia,Ping Zhou
Pollen grain was explored as a new carrier for enzyme immobilization. After being modified with boric acid-functionalized titania, the pollen grain was able to covalently immobilize glycosylated enzymes by boronate affinity interaction under very mild experimental conditions (e.g., pH 7.0, ambient temperature and free of organic solvent). The glucose oxidase and horse radish peroxidase-immobilized pollen grain became a bienzyme system. The pollen grain also worked as an indicator of the cascade reaction by changing its color. A rapid, simple and cost-effective approach for the visual detection of glucose was then developed. When the glucose concentration exceeded 0.5 mM, the color change was observable by the naked eye. The assay of glucose in body fluid samples exhibited its great potential for practical application.Keywords:enzyme immobilization;boronate affinity;pollen grain;glucose detection
研究领域:
生物化学
·
分析化学
·
生物技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Biotechnology for Biofuels
·
2021
·Vol. 14
·期 1
·1-12
·
IF 6.04
Zhou Zi-Wen,Cai Chun-Xian,Xing Xiu,Li Jun,Hu Zu-E.,Xie Zong-Bo,Wang Na,Yu Xiao-Qi
Background Production of biodiesel from renewable sources such as inedible vegetable oils by enzymatic catalysis has been a hotspot but remains a challenge on the efficient use of an enzyme. COFs (Covalent Organic Frameworks) with large surface area and porosity can be applied as ideal support to avoid aggregation of lipase and methanol. However, the naturally low density limits its application. In this work, we reported a facile synthesis of core–shell magnetic COF composite (Fe 3 O 4 @COF-OMe) to immobilize RML ( Rhizomucor miehei lipase), to achieve its utilization in biodiesel production. Result This strategy gives extrinsic magnetic property, and the magnetic COFs is much heavier and could disperse in water medium well, facilitating the attachment with the enzyme. The resultant biocomposite exhibited an excellent capacity of RML due to its high surface area and fast response to the external magnetic field, as well as good chemical stability. The core–shell magnetic COF-OMe structure not only achieved highly efficient immobilization and recovery processes but also maintained the activity of lipase to a great extent. RML@Fe 3 O 4 @COF-OMe performed well in practical applications, while free lipase did not. The biocomposite successfully achieved the production of biodiesel from Jatropha curcas Oil with a yield of about 70% in the optimized conditions. Conclusion Magnetic COFs (Fe 3 O 4 @COF-OMe) for RML immobilization greatly improved catalytic performance in template reaction and biodiesel preparation. The magneticity makes it easily recovered and separated from the system. This first successful attempt of COFs-based immobilized enzyme broadened the prospect of biodiesel production by COFs with some inspiration.
研究领域:
生物化学
·
材料科学
·
可再生能源
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2025
·Vol. 105
·期 7
·3931-3941
·
IF 3.5
Jiawei Zheng,Qiangyue Zhang,Nanjing Zhong
BACKGROUND Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, Candida antarctica lipase B (CALB) was immobilized onto the macroporous resin ADS-17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single-factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS-17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS-17 was investigated. RESULTS Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS-17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was ln V 0 = 6.3316 − 4.3321/ T , and the activation energy ( E a ) was 36.02 kJ mol −1 . CALB@ADS-17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of v max , k cat , K m , K i , and k ca t /K m were 0.01265 μmol L −1 s −1 , 9310.72 s −1 , 0.4907 mmol L −1 , 3.997 mmol L −1 , and 1.90 × 10 4 L mmol −1 s −1 , respectively. CONCLUSION CALB@ADS-17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS-17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry.
研究领域:
生物化学
·
酶工程
✓ 已验证
产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Zichen Wang,Tongyue Zhu,Hu Sun,Geling Kuang,Yuxiao Feng,Jiandong Cui
The encapsulation of enzymes in ZIF-8 (enzyme@ZIF-8 composites) via co-precipitation has attracted considerable attention. However, enzyme@ZIF-8 composites often exhibit low activity due to the three-dimensional (3D) structural characteristics of ZIF-8 and the protonation of the precursor, 2-methylimidazole (2-MeIm). In this study, a novel 2D catalase@ZIFs(SO4) composite was synthesized as an alternative to the conventional 3D catalase@ZIF-8 composites. The 2D catalase@ZIFs(SO4) composites demonstrated a nine-fold increase in activity and three-fold higher enzyme loading compared to their 3D counterparts. The enhanced catalytic performance is attributed to the 2D structure of the composites and the partial replacement of 2-MeIm with sulfate during enzyme immobilization, which reduces the protonation of 2-MeIm, enhances the hydrophilic microenvironment, and facilitates substrate transfer. Furthermore, compared to free enzymes, the 2D catalase@ZIFs(SO4) composites exhibited an expanded pH tolerance range, superior thermal stability, enhanced resistance to denaturants, and improved storage stability. To validate the concept, glucose oxidase, glutamate oxidase, and phenylalanine ammonia lyase were immobilized using the same approach. All immobilized enzymes demonstrated increased activity relative to the traditional CAT@ZIF-8 composites. This study offers a versatile platform for enzyme encapsulation within ZIF-8 through co-precipitation.
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
CHEMICAL ENGINEERING SCIENCE
·
2024
·
IF 4.1
Shaobin Zhang,Junjun Liu,Xuan Wang,Dezhi Liu,Qikai Tian,Haixia Shen,Jing Zhang,Dongpo Song,Weiliang Dong,Ziyi Yu
While enzymatic degradation has proven to be an effective way of remediating nanoplastic-related pollution, the practical deployment of this technique is hampered by concerns over enzyme stability, costs, and the low concentration of nanoplastics in natural settings. In this study, we unveil a facile microreactor-enhanced method that improves the effective remediation capacity of cutinase for nanoplastic-polluted water systems. Our approach leverages the self-assembly capabilities of block copolymers within microfluidic droplets to fabricate Janus microspheres with distinct dual-porosity features, which have an enzyme loading capacity of up to 103.8 mg cutinase/g microsphere. The cutinase-anchored microspheres can act as microreactors to capture and degrade nanoplastics. Despite its lower enzymatic activity, the immobilized cutinase exhibits degradation performance comparable to that of its free enzyme counterpart. Moreover, it displays good operational stability over six degradation cycles. Therefore, our findings shed some light on achieving more efficient and cost-effective enzymatic nanoplastic remediation.
研究领域:
环境科学
·
生物技术
·
材料科学
✓ 已验证
产品关联
DOI
高影响因子
ACS Applied Materials & Interfaces
·
2023
·
IF 9.5
Feifei Jia,Yunting Liu,Xuewu Deng,Xue Cao,Xiaobing Zheng,Liya Zhou,Jing Gao,Yanjun Jiang
A three-in-one heterogeneous catalyst (UPO@dTiO2-CD) was fabricated by grafting cyclodextrins (CDs) on the dehiscent TiO2 (dTiO2) surface and subsequently immobilizing unspecific peroxygenase (rAaeUPO), which exhibited double enhanced electron/mass transfer in photo-enzymatic enantioselective hydroxylation of the C–H bond. The tunable anatase/rutile phase ratio and dehiscent mesoporous architectures of dTiO2 and the electron donor feature and hydrophobic inner cavity of the CDs are independently responsible for accelerating both electron and mass transfer. The coordination of the photocatalytic and enzymatic steps was achieved by structural and compositional regulation. The optimized UPO@dTiO2-CD not only displayed high catalytic efficiency (turnover number and turnover frequency of rAaeUPO up to >65,000 and 91 min–1, respectively) but also exhibited high stability and reusability.
研究领域:
生物化学
·
材料科学
·
环境科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2018
·
IF 3.909
Yue Li,Nanjing Zhong,Ling-Zhi Cheong,Jianrong Huang,Hongxiao Chen,Shaoyan Lin
In this study, SBA-15 was modified by a series of silane coupling reagents and later used to immobilize Candida antartica lipase B (CALB). The enzymatic properties of the immobilized CALB samples were studied. In addition, the catalytic performance in glycerolysis of soybean oil for diacylglycerols (DAG) production was also investigated. The highest enzymatic activity up to 6100.00 ± 246.41 U/g was observed from the propyl methacrylate group modified SBA-15 supported CALB. No loss of activity was observed from the propyl methacrylate group modified SBA-15 supported CALB, but a higher-than-initial activity was notably found from 3-aminopropyl group and n -octyl group modified SBA-15 supported CALB after a 4-h incubation in air at 70 °C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90 ± 2.38 wt% and a DAG/MAG ratio at 3.11 ± 0.08 was obtained after a 24-h reaction at 60 °C in a solvent-free system.
研究领域:
生物化学
·
酶工程
·
食品科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
·
2022
·
IF 4.326
Lili Xu,Renmin Liu,Zhaofang Li,Moju Li,Min Zhao,Yingjie Li,Guiyue Hou,Aifeng Li,Hongbo Suo
In this study, imidazolium-based ionic liquids (ILs) were used to modify carboxymethyl cellulose-coated Fe3O4 nanoparticles with graphene oxide deposition (ILs-MCMC/GO). The prepared composites were characterized and used to immobilize lipase. The prepared biocatalyst (PPL-ILs-MCMC/GO) exhibited higher activity, which was 3.55-fold that of free lipase and 1.41-fold that of immobilized lipase without IL (PPL-MCMC/GO). After reusing 10 times, the residual activity of PPL-ILs-MCMC/GO was 91.3%, which was higher than those of PPL-MCMC/GO (83.6%) and PPL-MCMC (73.6%). In addition, using kinetic analysis, we showed that the affinity between PPL-ILs-MCMC/GO and the substrate was improved. The secondary structures of free and immobilized lipase were analyzed to explain the mechanism by which the performance of PPL-ILs-MCMC/GO was improved. The introduction of imidazole-based IL was useful in improving the microenvironment of immobilized lipase. Furthermore, magnetic supports loaded with lipase could be recovered easily.
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
危险品化学品经营许可证（带存储）