Relevant bibliographies by topics / Enzymes immobilization

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Enzymes immobilization'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 April 2022

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Journal articles on the topic "Enzymes immobilization"

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Mokhtar, Nur Fathiah, Raja Noor Zaliha Raja Abd. Rahman, Noor Dina Muhd Noor, Fairolniza Mohd Shariff, and Mohd Shukuri Mohamad Ali. "The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method." Catalysts 10, no. 7 (2020): 744. http://dx.doi.org/10.3390/catal10070744.

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Four major enzymes commonly used in the market are lipases, proteases, amylases, and cellulases. For instance, in both academic and industrial levels, microbial lipases have been well studied for industrial and biotechnological applications compared to others. Immobilization is done to minimize the cost. The improvement of enzyme properties enables the reusability of enzymes and facilitates enzymes used in a continuous process. Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities. Immobilized enzymes can be used repea
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Stine, Keith J. "Enzyme Immobilization on Nanoporous Gold: A Review." Biochemistry Insights 10 (January 1, 2017): 117862641774860. http://dx.doi.org/10.1177/1178626417748607.

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Nanoporous gold (referred to as np-Au or NPG) has emerged over the past 10 years as a new support for enzyme immobilization. The material has appealing features of ease of preparation, tunability of pore size, high surface to volume ratio, and compatibility with multiple strategies for enzyme immobilization. The np-Au material is especially of interest for immobilization of redox enzymes for biosensor and biofuel cell applications given the ability to construct electrodes of high surface area and stability. Adjustment of the pore size of np-Au can yield enhancements in enzyme thermal stability
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Asnawati, Asnawati, Dwi Indarti, Tri Mulyono, and Gembong Kesuma B. "Amperometric biosensor for glucose detection based-on immobilisation of glucose oxidase in acetic cellulose membrane using ferrocene as mediator." Jurnal ILMU DASAR 14, no. 1 (2013): 45. http://dx.doi.org/10.19184/jid.v14i1.481.

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The study reported the development of glucose ampherometric biosensor based on immobilization of glucose oxidase on cellulose acetate membrane with ferrocene as a mediator. Biosensor was designed with model Fc, GOx, CP / GOx / CA where ferrocene and the enzyme glucose oxidase on carbon paste in immobilizatin on the electrode body in the form of glass tubes and in other parts of the enzyme glucose oxidase in immobilizatin on cellulose acetate membrane with adsorption techniques are placed in electrode tip by using the o-ring. The presence of enzymes immobilization was determined quantitatively
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Zhu, Chen-Yuan, Fei-Long Li, Ye-Wang Zhang, Rahul K. Gupta, Sanjay K. S. Patel, and Jung-Kul Lee. "Recent Strategies for the Immobilization of Therapeutic Enzymes." Polymers 14, no. 7 (2022): 1409. http://dx.doi.org/10.3390/polym14071409.

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Therapeutic enzymes play important roles in modern medicine due to their high affinity and specificity. However, it is very expensive to use them in clinical medicine because of their low stability and bioavailability. To improve the stability and effectiveness of therapeutic enzymes, immobilization techniques have been employed to enhance the applications of therapeutic enzymes in the past few years. Reported immobilization techniques include entrapment, adsorption, and covalent attachment. In addition, protein engineering is often used to improve enzyme properties; however, all methods prese
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Sher, Hassan, Hazrat Ali, Muhammad H. Rashid, et al. "Enzyme Immobilization on Metal-Organic Framework (MOF): Effects on Thermostability and Function." Protein & Peptide Letters 26, no. 9 (2019): 636–47. http://dx.doi.org/10.2174/0929866526666190430120046.

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MOFs are porous materials with adjustable porosity ensuing a tenable surface area and stability. MOFs consist of metal containing joint where organic ligands are linked with coordination bonding rendering a unique architecture favouring the diverse applications in attachment of enzymes, Chemical catalysis, Gases storage and separation, biomedicals. In the past few years immobilization of soluble enzymes on/in MOF has been the topic of interest for scientists working in diverse field. The activity of enzyme, reusability, storage, chemical and thermal stability, affinity with substrate can be gr
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Bié, Joaquim, Bruno Sepodes, Pedro C. B. Fernandes, and Maria H. L. Ribeiro. "Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications." Processes 10, no. 3 (2022): 494. http://dx.doi.org/10.3390/pr10030494.

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Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their
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Lyu, Xingyi, Rebekah Gonzalez, Andalwisye Horton, and Tao Li. "Immobilization of Enzymes by Polymeric Materials." Catalysts 11, no. 10 (2021): 1211. http://dx.doi.org/10.3390/catal11101211.

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Enzymes are the highly efficient biocatalyst in modern biotechnological industries. Due to the fragile property exposed to the external stimulus, the application of enzymes is highly limited. The immobilized enzyme by polymer has become a research hotspot to empower enzymes with more extraordinary properties and broader usage. Compared with free enzyme, polymer immobilized enzymes improve thermal and operational stability in harsh environments, such as extreme pH, temperature and concentration. Furthermore, good reusability is also highly expected. The first part of this study reviews the thre
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Bhavaniramya, Sundaresan, Ramar Vanajothi, Selvaraju Vishnupriya, et al. "Enzyme Immobilization on Nanomaterials for Biosensor and Biocatalyst in Food and Biomedical Industry." Current Pharmaceutical Design 25, no. 24 (2019): 2661–76. http://dx.doi.org/10.2174/1381612825666190712181403.

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Enzymes exhibit a great catalytic activity for several physiological processes. Utilization of immobilized enzymes has a great potential in several food industries due to their excellent functional properties, simple processing and cost effectiveness during the past decades. Though they have several applications, they still exhibit some challenges. To overcome the challenges, nanoparticles with their unique physicochemical properties act as very attractive carriers for enzyme immobilization. The enzyme immobilization method is not only widely used in the food industry but is also a component m
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Singh, Kushagri, Abha Mishra, Deepankar Sharma, and Kavita Singh. "Nanotechnology in Enzyme Immobilization: An Overview on Enzyme Immobilization with Nanoparticle Matrix." Current Nanoscience 15, no. 3 (2019): 234–41. http://dx.doi.org/10.2174/1573413714666181008144144.

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Engineering of biocatalysts with the help of immobilization techniques is a worthy approach for the advancement of enzyme function and stability and is finer to the other chemical as well as biological methods. These biocatalysts encapsulation methods actually use very gentle method conditions that hardly affect biocatalysts internal specific biocatalytic activity and this leads to its internment without losing its freedom but restrict the movements related to unfolding. Additionally, enzyme encapsulation somehow imitates their mode of normal incidence within the cells and it also provides sec
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Fang, Yi, Aihua Zhang, Shaohua Li, Michael Sproviero, and Ming-Qun Xu. "Enzyme Immobilization for Solid-Phase Catalysis." Catalysts 9, no. 9 (2019): 732. http://dx.doi.org/10.3390/catal9090732.

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The covalent immobilization of an enzyme to a solid support can broaden its applicability in various workflows. Immobilized enzymes facilitate catalyst re-use, adaptability to automation or high-throughput applications and removal of the enzyme without heat inactivation or reaction purification. In this report, we demonstrate a step-by-step procedure to carry out the bio-orthogonal immobilization of DNA modifying enzymes employing the self-labelling activity of the SNAP-tag to covalently conjugate the enzyme of interest to the solid support. We also demonstrate how modifying the surface functi
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Dissertations / Theses on the topic "Enzymes immobilization"

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David, Allan E. "Immobilization of enzymes on nanoporous, silica composites." College Park, Md. : University of Maryland, 2004. http://hdl.handle.net/1903/2055.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2004.<br>Thesis research directed by: Chemical Engineering. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
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Dong, Liang-Chang. "Thermally reversible hydrogels for controlled drug delivery and enzyme immobilization /." Thesis, Connect to this title online; UW restricted, 1990. http://hdl.handle.net/1773/8009.

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Meneghello, Marta. "A modular approach for a controlled immobilization of enzymes." Thesis, University of Southampton, 2018. https://eprints.soton.ac.uk/422233/.

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Stable, site-specific immobilization of redox proteins and enzymes is of great interest for the development of biosensors and biofuel cells, where the long-term stability of enzymatic electrodes as well as the possibility of controlling the orientation of the biomolecules at the electrode surface have a great importance. For such applications, it would be desirable to immobilise redox proteins and enzymes in a specific orientation on the electrode in order to improve direct electron transfer. In this work, we describe such an approach using site directed mutagenesis to introduce cysteine resid
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Li, Dan 1971. "Immobilization, characterization and use of fish protease." Thesis, McGill University, 2006. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=102996.

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Enzyme immobilization as a technique attaches free forms of enzyme molecules to stationary support materials to permit enzymes to be reused several times. Bovine trypsin as a model enzyme was immobilized onto controlled pore glass (CPG) beads to investigate the optimum conditions for immobilization, as well as the physico-chemical properties of the immobilized enzyme versus the free form of the enzyme. At pH 9, about 60% of the enzyme protein incubated with CPG was immobilized onto the CPG, and immobilized bovine trypsin activity was determined as 0.265 BAPNA U/g CPG beads. The immobilized bov
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Ampon, Kamaruzaman. "Immobilization of proteins on porous polymer beads /." The Ohio State University, 1987. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487324944212704.

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Chen, Xi. "Infrared and Uv-Vis Spectroscopic Studies of Catalytic Reaction of Enzymes and Immobilization Enzyme on Porous Polymers." University of Akron / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=akron1428327122.

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Reichstädter, Marek. "Imobilizace vybraných glykanohydroláz." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2015. http://www.nusl.cz/ntk/nusl-217152.

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The theoretical part of this thesis deals with cellulolytic enzymes, their microbial producers, the possibilities of using such enzymes in the industry and how can be enzymes - not only cellulolytic - immobilized. Experimental part examines the preparations created by immobilizing various amounts of the commercially used cellulolytic complex Cellulast 1.5L onto various synthetic carriers made of polyethylene terephthalate - commercially used Sorsilen, PET carrier and glutaraldehyde-treated PET carrier. Enzyme activity of these preparations was determined by Somogyi - Nelson method by spectroph
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Solé, Ferré Jordi. "Oxidoreductive bioprocess intensification through reaction engineering and enzyme immobilization." Doctoral thesis, Universitat Autònoma de Barcelona, 2019. http://hdl.handle.net/10803/669346.

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La investigació plasmada en aquesta tesi doctoral tracta l’aplicació dels principis d’enginyeria de reacció i immobilització enzimàtica per a la millora de reaccions d’oxidoreducció biocatalitzades. En una primera part de la tesi, es va estudiar la co-immobilització de la monooxigenasa P450 BM3 juntament amb un enzim regenerador del cofactor NADPH, la glucosa deshidrogenasa (GDH-Tac). Els millors derivats es van obtenir utilitzant dos suports d’agarosa, un funcionalitzat amb grups epoxy (83% i 20% activitats retingudes respectivament) i l’altre amb grups amino (28% i 25% activitats retin
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Myung, Suwan. "Cell-Free Biosystems Comprised of Synthetic Enzymatic Pathways: Development of Building Blocks, Immobilization of Enzymes, Stabilization of Cascade Enzymes, and Generation of Hydrogen." Diss., Virginia Tech, 2013. http://hdl.handle.net/10919/50645.

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The production of hydrogen from low-cost abundant renewable biomass would be vital to sustainable development. Cell-free (in vitro) biosystems comprised of synthetic enzymatic pathways would be a promising biomanufacturing platform due to several advantages, such as high product yield, fast reaction rate, easy control and access, and so on. However, it is essential to produce (purified) enzymes at low costs and stabilize them for long periods to decrease biocatalyst costs.<br /><br />Thermophilic recombinant enzymes as building blocks were discovered and developed: fructose 1,6-bisphosphatase
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Gao, Xiaojian. "Immobilization of lipases via sol-gel procedures and application of the immobilized lipases in oleochemicial [sic] reactions." [Lincoln, Neb. : University of Nebraska-Lincoln], 2004. http://www.unl.edu/libr/Dissertations/2004/GaoDis.pdf.

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Thesis (Ph. D.)--University of Nebraska--Lincoln, 2004.<br>PDF text: [2] leaves abstract, vii, 156 leaves dissertation : ill. (some col.). Site viewed on Jan. 25, 2005. Includes bibliographical references.
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Books on the topic "Enzymes immobilization"

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Guisan, Jose M. Immobilization of enzymes and cells. Humana Press, 2013.

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Guisan, Jose M., ed. Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9.

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Guisan, Jose M., ed. Immobilization of Enzymes and Cells. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-550-7.

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Guisan, Jose M., Juan M. Bolivar, Fernando López-Gallego, and Javier Rocha-Martín, eds. Immobilization of Enzymes and Cells. Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0215-7.

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Bickerstaff, Gordon. Immobilization of Enzymes and Cells. Humana Press, 1996. http://dx.doi.org/10.1385/0896033864.

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Enzyme stabilization and immobilization: Methods and protocols. Humana Press, 2011.

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Co, Business Communications, ed. Bio-immobilization: Technology, products, and markets. Business Communications Co., 1994.

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Sheng wu gu ding hua ji shu ji ying yong: Biological technology and applications of immobilization. Hua xue gong ye chu ban she, 2009.

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Goosen, Mattheus F. A. Fundamentals of animal cell encapsulation and immobilization. CRC Press, 1993.

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Dwevedi, Alka. Enzyme Immobilization. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-41418-8.

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Book chapters on the topic "Enzymes immobilization"

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Brena, Beatriz M., and Francisco Batista-Viera. "Immobilization of Enzymes." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_2.

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Roy, Ipsita, and Munishwar N. Gupta. "Bioaffinity Immobilization." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_10.

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Torchilin, Vladimir P. "Immobilization of Therapeutic Enzymes." In Progress in Clinical Biochemistry and Medicine. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75821-8_3.

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Sillu, Devendra, Yeshaswi Kaushik, and Shekhar Agnihotri. "Immobilization of Enzymes onto Silica-Based Nanomaterials for Bioprocess Applications." In Immobilization Strategies. Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-7998-1_11.

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Mallick, Nirupama. "Immobilization of Microalgae." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_33.

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Besic, Sabina, and Shelley D. Minteer. "Micellar Polymer Encapsulation of Enzymes." In Enzyme Stabilization and Immobilization. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6499-4_8.

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Besic, Sabina, and Shelley D. Minteer. "Micellar Polymer Encapsulation of Enzymes." In Enzyme Stabilization and Immobilization. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-895-9_10.

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Silva Nunes, Gilvanda, and Jean-Louis Marty. "Immobilization of Enzymes on Electrodes." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_21.

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Andreescu, Silvana, Bogdan Bucur, and Jean-Louis Marty. "Affinity Immobilization of Tagged Enzymes." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_9.

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Kundu, Debasree, M. S. Thakur, and Sanjukta Patra. "Textile Fabric Processing and Their Sustainable Effluent Treatment Using Enzymes—Insights and Challenges." In Immobilization Strategies. Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-7998-1_19.

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Conference papers on the topic "Enzymes immobilization"

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Thomas, N., I. Lahdesmaki, and B. Parviz. "Direct immobilization of enzymes on common photoresists." In 2011 IEEE 24th International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2011. http://dx.doi.org/10.1109/memsys.2011.5734404.

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Tasic, Ljubica, and Paula Moretti. "Immobilization of Hydrolytic Enzymes on Functionalized and Hybrid Ferromagnetic and Silica Nanoparticles." In XXIII Congresso de Iniciação Científica da Unicamp. Galoá, 2015. http://dx.doi.org/10.19146/pibic-2015-38168.

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Sulman, Aleksandrina, Valentina Matveeva, Olga Grebennikova, Boris Tikhonov, and Natalya Lakina. "MAGNETIC MESOPOROUS MATERIALS AS AN EFFECTIVE SUPPORT FOR THE IMMOBILIZATION OF ENZYMES." In 21st SGEM International Multidisciplinary Scientific GeoConference Proceedings 2021. STEF92 Technology, 2021. http://dx.doi.org/10.5593/sgem2021/6.1/s25.24.

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Akers, Nick L., and Shelley D. Minteer. "A Novel Approach to Designing Highly Efficient and Commercially Viable Biofuel Cells." In ASME 2004 2nd International Conference on Fuel Cell Science, Engineering and Technology. ASMEDC, 2004. http://dx.doi.org/10.1115/fuelcell2004-2512.

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A biofuel cell is an electrochemical device in which the energy stored in a fuel, such as ethanol, is converted to electrical energy by the means of the catalytic activity of enzymes. Biofuel cells have traditionally suffered from low power densities and short lifetimes due to the fragility of the enzyme catalyst. Utilizing a novel quaternary ammonium salt treated Nafion membrane for enzyme immobilization in a biofuel cell results in increases in power densities and enzyme lifetimes to commercially viable levels. Additionally, this method provides sufficient protection to develop a membrane el
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GULOTTA, Florencia A., Ladislao DIAZ VERGARA, Mariana MONTENEGRO, Nancy F. FERREYRA, and Verónica I. PAZ ZANINI. "SELF-ASSEMBLED MULTILAYERS OF WATER-SOLUBLE MODIFIED-CHITOSAN AND GLUCOSE OXIDASE FOR DETECTION OF GLUCOSE IN MILK SAMPLES." In SOUTHERN BRAZILIAN JOURNAL OF CHEMISTRY 2021 INTERNATIONAL VIRTUAL CONFERENCE. DR. D. SCIENTIFIC CONSULTING, 2022. http://dx.doi.org/10.48141/sbjchem.21scon.07_abstract_ferreyra.pdf.

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Multilayer films made of glucose-functionalized chitosan (G-Chit) and glucose oxidase (GOx) were built by layer-by-layer self-assembly technique onto carbon paste electrodes (CPE). The obtained bioelectrodes were characterized by cyclic voltammetry and chronoamperometry. Results indicated that catalytic response increases with the number of bilayers G-Chit/GOx and the enzyme concentration obtaining the best responses for 3 bilayers and 2 mg ml-1, respectively. The effect of pH on the bioelectrode response was also investigated, it was found that the optimal working value is 7.0. Under optimize
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Preethichandra, D. M. G., and E. M. I. Mala Ekanayake. "Performance dependency of enzyme based nano-biosensors on fabrication and enzyme immobilization techniques." In 2017 Eleventh International Conference on Sensing Technology (ICST). IEEE, 2017. http://dx.doi.org/10.1109/icsenst.2017.8304520.

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Nakagawa, Kyuya, Yuki Goto, and Akihiro Tamura. "A New Approach for Enzyme Immobilization in a Microreactor." In 14th Asia Pacific Confederation of Chemical Engineering Congress. Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-1445-1_369.

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Kumar, V. T. Fidal, Anshika Agarwal, Pitam Subha, Anant Raheja, T. S. Natarajan, and T. S. Chandra. "Electrospinning as a simple enzyme immobilization technique for application in enzyme based biofuel cells." In 2011 International Conference on Nanoscience, Technology and Societal Implications. IEEE, 2011. http://dx.doi.org/10.1109/nstsi.2011.6111982.

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Wang, Y. T., J. Wang, H. Peng, and J. Z. Zhu. "Improved enzyme immobilization for enhanced bioelectrocatalytic activity of choline sensor." In 2013 Transducers & Eurosensors XXVII: The 17th International Conference on Solid-State Sensors, Actuators and Microsystems (TRANSDUCERS & EUROSENSORS XXVII). IEEE, 2013. http://dx.doi.org/10.1109/transducers.2013.6626775.

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Voicu, Stefan Ioan, Aurelia Cristina Nechifor, Ovidiu Gales, and Gheorghe Nechifor. "Covalent enzyme immobilization onto carbon nanotubes using a membrane reactor." In SPIE Microtechnologies, edited by Ángel B. Rodríguez-Vázquez, Rainer Adelung, Ricardo A. Carmona-Galán, Gustavo Liñán-Cembrano, and Carsten Ronning. SPIE, 2011. http://dx.doi.org/10.1117/12.888780.

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Reports on the topic "Enzymes immobilization"

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Flounders, A. W., S. C. Carichner, A. K. Singh, J. V. Volponi, J. S. Schoeniger, and K. Wally. Immobilization, stabilization and patterning techniques for enzyme based sensor systems. Office of Scientific and Technical Information (OSTI), 1997. http://dx.doi.org/10.2172/642677.

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Rajan, K. S. Enzymatic Detoxification of Chemical Warfare Agents: Immobilization of the Enzyme for Material Surfaces. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada231056.

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Lupoi, Jason. Developments in enzyme immobilization and near-infrared Raman spectroscopy with downstream renewable energy applications. Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1082965.

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