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Journal articles on the topic 'Enzymes immobilization'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 April 2022

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1

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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3

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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HARHEN, BRENDAN, and FRANK BARRY. "Immobilization of proteolytic enzymes." Biochemical Society Transactions 18, no. 2 (1990): 314–15. http://dx.doi.org/10.1042/bst0180314.

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Wackett, Lawrence P. "Immobilization of microbial enzymes." Microbial Biotechnology 3, no. 6 (2010): 729–30. http://dx.doi.org/10.1111/j.1751-7915.2010.00227.x.

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Yabutsuka, Takeshi, Masaya Yamamoto, Shigeomi Takai, and Takeshi Yao. "Enzyme Immobilization Behavior on the Surface of Hydroxyapatite Capsules under Alkaline Condition." Key Engineering Materials 782 (October 2018): 21–26. http://dx.doi.org/10.4028/www.scientific.net/kem.782.21.

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We prepared hydroxyapatite (HA) capsules encapsulating maghemite particles. In order to evaluate enzyme immobilization behavior of the HA capsules under alkaline condition, we immobilized five kinds of enzymes with different isoelectric point in carbonate/bicarbonate buffer (CBB, pH 10.0). When the enzymes in CBB were moderately charged, immobilization efficiency on the HA capsules showed the highest value. It was suggested that immobilization efficiency was affected according to both pI of enzyme and pH of the surrounding solution and that enzyme immobilized on the HA capsules by not only ele

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Mateo, C., V. Grazú, B. C. C. Pessela, et al. "Advances in the design of new epoxy supports for enzyme immobilization–stabilization." Biochemical Society Transactions 35, no. 6 (2007): 1593–601. http://dx.doi.org/10.1042/bst0351593.

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Multipoint covalent immobilization of enzymes (through very short spacer arms) on support surfaces promotes a very interesting ‘rigidification’ of protein molecules. In this case, the relative positions of each residue of the enzyme involved in the immobilization process have to be preserved unchanged during any conformational change induced on the immobilized enzyme by any distorting agent (heat, organic solvents etc.). In this way, multipoint covalent immobilization should induce a very strong stabilization of immobilized enzymes. Epoxy-activated supports are able to chemically react with al

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Zhao, Zongpei, Meng-Cheng Zhou, and Run-Lin Liu. "Recent Developments in Carriers and Non-Aqueous Solvents for Enzyme Immobilization." Catalysts 9, no. 8 (2019): 647. http://dx.doi.org/10.3390/catal9080647.

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Immobilization techniques are generally based on reusing enzymes in industrial applications to reduce costs and improve enzyme properties. These techniques have been developing for decades, and many methods for immobilizing enzymes have been designed. To find a better immobilization method, it is necessary to review the recently developed methods and have a clear overview of the advantages and limitations of each method. This review introduces the recently reported immobilization methods and discusses the improvements in enzyme properties by different methods. Among the techniques to improve e

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Sheldon, Roger. "CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy." Catalysts 9, no. 3 (2019): 261. http://dx.doi.org/10.3390/catal9030261.

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Biocatalysis has emerged in the last decade as a pre-eminent technology for enabling the envisaged transition to a more sustainable bio-based economy. For industrial viability it is essential that enzymes can be readily recovered and recycled by immobilization as solid, recyclable catalysts. One method to achieve this is via carrier-free immobilization as cross-linked enzyme aggregates (CLEAs). This methodology proved to be very effective with a broad selection of enzymes, in particular carbohydrate-converting enzymes. Methods for optimizing CLEA preparations by, for example, adding proteic fe

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Hickey, A. M., L. Marle, T. McCreedy, P. Watts, G. M. Greenway, and J. A. Littlechild. "Immobilization of thermophilic enzymes in miniaturized flow reactors." Biochemical Society Transactions 35, no. 6 (2007): 1621–23. http://dx.doi.org/10.1042/bst0351621.

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The exploitation of enzymes for biotransformation reactions for the production of new and safer drug intermediates has been the focus of much research. While a number of enzymes are commercially available, their use in an industrial setting is often limited to reactions that are cost-effective and they are rarely investigated further. However, the development of miniaturized flow reactor technology has meant that the cost of such research, once considered cost- and time-inefficient, would be much less prohibitive. The use of miniaturized flow reactors for enzyme screening offers a number of ad

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18

Hanušová, Kristýna, Lukáš Vápenka, Jaroslav Dobiáš, and Linda Mišková. "Development of antimicrobial packaging materials with immobilized glucose oxidase and lysozyme." Open Chemistry 11, no. 7 (2013): 1066–78. http://dx.doi.org/10.2478/s11532-013-0241-4.

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AbstractPackaging based on immobilization of antimicrobial enzymes provides a promising form of active packaging systems applicable in food processing. Glucose oxidase and lysozyme were immobilized by the Ugi reaction with cyclohexyl isocyanide and glutaraldehyde on polyamide and ionomer films partially hydrolysed by hydrochloric acid. The immobilization of the enzymes on the surface of films was confirmed by FT-IR spectroscopy and the films were characterized by the specific activity of the immobilized enzymes. The enzyme migration into model solutions and the effect of pH, temperature and st

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H. Orrego, Alejandro, Maria Romero-Fernández, María Millán-Linares, María Yust, José Guisán, and Javier Rocha-Martin. "Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent." Catalysts 8, no. 8 (2018): 333. http://dx.doi.org/10.3390/catal8080333.

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Enzyme immobilization by multipoint covalent attachment on supports activated with aliphatic aldehyde groups (e.g., glyoxyl agarose) has proven to be an excellent immobilization technique for enzyme stabilization. Borohydride reduction of immobilized enzymes is necessary to convert enzyme–support linkages into stable secondary amino groups and to convert the remaining aldehyde groups on the support into hydroxy groups. However, the use of borohydride can adversely affect the structure–activity of some immobilized enzymes. For this reason, 2-picoline borane is proposed here as an alternative mi

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20

Ahmad, Raneem, Jordan Shanahan, Sydnie Rizaldo, Daniel S. Kissel, and Kari L. Stone. "Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst." Catalysts 10, no. 5 (2020): 499. http://dx.doi.org/10.3390/catal10050499.

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In many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inability to operate over larger temperature and pH ranges. Immobilization of enzymes onto solid supports has gained attention as an alternative to traditional chemical processes due to enhanced enzymatic performance and stability. This study demonstrates the co-immobilization of glucose oxidase (GOx) a

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21

Silva, Douglas Fernandes, Henrique Rosa, Ana Flavia Azevedo Carvalho, and Pedro Oliva-Neto. "Immobilization of Papain on Chitin and Chitosan and Recycling of Soluble Enzyme for Deflocculation of Saccharomyces cerevisiae from Bioethanol Distilleries." Enzyme Research 2015 (January 1, 2015): 1–10. http://dx.doi.org/10.1155/2015/573721.

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Yeast flocculation (Saccharomyces cerevisiae) is one of the most important problems in fuel ethanol production. Yeast flocculation causes operational difficulties and increase in the ethanol cost. Proteolytic enzymes can solve this problem since it does not depend on these changes. The recycling of soluble papain and the immobilization of this enzyme on chitin or chitosan were studied. Some cross-linking agents were evaluated in the action of proteolytic activity of papain. The glutaraldehyde (0.1–10% w·v−1), polyethyleneimine (0.5% v·v−1), and tripolyphosphate (1–10% w·v−1) inactivated the en

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Prlainovic, Nevena, Dejan Bezbradica, Zorica Knezevic-Jugovic, Aleksandar Marinkovic, and Dusan Mijin. "Immobilization of enzymes onto carbon nanotubes." Chemical Industry 65, no. 4 (2011): 423–30. http://dx.doi.org/10.2298/hemind110330028p.

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The discovery of carbon nanotubes (CNTs) has opened a new door in nanotechnology. With their high surface area, unique electronic, thermal and mechanical properties, CNTs have been widely used as carriers for protein immobilization. In fact, carbon nanotubes present ideal support system without diffusional limitations, and also have the possibility of surface covalent functionalization. It is usually the oxidation process that introduces carboxylic acid groups. Enzymes and other proteins could be adsorbed or covalently attached onto carbon nanotubes. Adsorption of enzyme is a very simple and i

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Storey, Kenneth B., and Doris Y. Schafhauser-Smith. "Immobilization of Polysaccharide-degrading Enzymes." Biotechnology and Genetic Engineering Reviews 12, no. 1 (1994): 409–66. http://dx.doi.org/10.1080/02648725.1994.10647918.

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Wood, Louis L., Carrington S. Cobbs, Leon Lantz, Lin Peng, and Gary J. Calton. "Immobilization of enzymes with polyaziridines." Journal of Biotechnology 13, no. 4 (1990): 305–14. http://dx.doi.org/10.1016/0168-1656(90)90078-p.

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Hu, Jinguang, Joshua Davies, Yiu Mok, Claudio Arato, and John Saddler. "The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers." Materials 11, no. 10 (2018): 2005. http://dx.doi.org/10.3390/ma11102005.

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Earlier work had indicated that enzyme-mediated hydrolysis of xylooligomer-rich water-soluble streams (derived from steam pre-treated wheat straw) resulted in the effective production of xylose which was subsequently used to produce bio-glycol. In the work reported here, both the thermostability and recyclability of xylanases were significantly improved by covalent immobilizing the enzymes onto alginate beads. The immobilized xylanases showed a lower hydrolytic potential (~55% xylooligomer conversion) compared to the commercial xylanase cocktail HTec3 (~90% xylooligomer conversion) when used a

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Ghosh, Shubhrima, Razi Ahmad, and Sunil Kumar Khare. "Immobilization of Cholesterol Oxidase: An Overview." Open Biotechnology Journal 12, no. 1 (2018): 176–88. http://dx.doi.org/10.2174/1874070701812010176.

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Background:Cholesterol oxidases are bacterial oxidases widely used commercially for their application in the detection of cholesterol in blood serum, clinical or food samples. Additionally, these enzymes find potential applications as an insecticide, synthesis of anti-fungal antibiotics and a biocatalyst to transform a number of sterol and non-sterol compounds. However, the soluble form of cholesterol oxidases are found to be less stable when applied at higher temperatures, broader pH range, and incur higher costs. These disadvantages can be overcome by immobilization on carrier matrices.Metho

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Califano, Valeria, and Aniello Costantini. "Immobilization of Cellulolytic Enzymes in Mesostructured Silica Materials." Catalysts 10, no. 6 (2020): 706. http://dx.doi.org/10.3390/catal10060706.

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Mesostructured silica nanoparticles offer a unique opportunity in the field of biocatalysis thanks to their outstanding properties. The tunable pore size in the range of mesopores allows for immobilizing bulky enzyme molecules. The large surface area improves the catalytic efficiency by increasing enzyme loading and finely dispersing the biocatalyst molecules. The easily tunable pore morphology allows for creating a proper environment to host an enzyme. The confining effect of mesopores can improve the enzyme stability and its resistance to extreme pH and temperatures. Benefits also arise from

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Molina, M. Asunción, Victoria Gascón-Pérez, Manuel Sánchez-Sánchez, and Rosa M. Blanco. "Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials." Catalysts 11, no. 8 (2021): 1002. http://dx.doi.org/10.3390/catal11081002.

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The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific community to develop very different strategies for the immobilization of enzymes in/on MOFs. This review focuses on one of these strategies, namely, the one-pot enzyme immobilization within sustainable MOFs, which is particularly enticing as the resultant biocomposite Enzy

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Hamsina, Hamsina, M. Tang, and Erni Indrawati Ruslan Hasani. "Activity Test, Selectivity, Stability of Chitinase on Amobil Chitosan Membranes." International Journal of Multicultural and Multireligious Understanding 8, no. 7 (2021): 453. http://dx.doi.org/10.18415/ijmmu.v8i7.2750.

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The use of enzymes for industrial functions needs enzymes that are stable, selective and might be used repeatedly. The aim of the study was to determine the chitinase enzyme's function, selectivity, and stability in amobil chitosan membranes. The research method consisted of stages: production of the chitinase enzyme which included the manufacture of chitin colloidal substrate, rejuvenation of thermophilic bacteria, preparation of the inoculum and determining the optimum time of production, fractionation of ammonium sulfate, chitinase enzyme immobilization technique and activity, stability and

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Lee, Sun Hyung, Ji Sook Lim, and Han Seung Kim. "Decomposition of Chlorinated Hydrocarbons Using the Biocatalyst Immobilized by Clay Minerals." Advanced Materials Research 356-360 (October 2011): 1089–92. http://dx.doi.org/10.4028/www.scientific.net/amr.356-360.1089.

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Biochemical decomposition of catechol and 4-chlorocatechol, degradation intermediate products of 4-chlorophenol, was investigated using enzymes and their immobilized forms by clay minerals. An oxygenase that can initiate oxidative ring-fission of aromatic compounds was obtained via cloning of its gene (cphA-1) encoding hydroxyquinol dioxygenase contained in Arthrobacter chlorophenolicus A6 and overexpression and purification of the enzyme. The enzyme expressed in vitro was then immobilized onto the clay mineral (montmorillonite). Michaelis-Menten kinetic analysis was conducted to compare the e

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Júnior, Aldo Araújo da Trindade, Yan Ferraz Ximenes Ladeira, Alexandre da Silva França, et al. "Multicatalytic Hybrid Materials for Biocatalytic and Chemoenzymatic Cascades—Strategies for Multicatalyst (Enzyme) Co-Immobilization." Catalysts 11, no. 8 (2021): 936. http://dx.doi.org/10.3390/catal11080936.

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During recent decades, the use of enzymes or chemoenzymatic cascades for organic chemistry has gained much importance in fundamental and industrial research. Moreover, several enzymatic and chemoenzymatic reactions have also served in green and sustainable manufacturing processes especially in fine chemicals, pharmaceutical, and flavor/fragrance industries. Unfortunately, only a few processes have been applied at industrial scale because of the low stabilities of enzymes along with the problematic processes of their recovery and reuse. Immobilization and co-immobilization offer an ideal soluti

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de Jesús Rostro-Alanis, Magdalena, Elena Ivonne Mancera-Andrade, Mayra Beatriz Gómez Patiño, et al. "Nanobiocatalysis: Nanostructured materials – a minireview." Biocatalysis 2, no. 1 (2016): 1–24. http://dx.doi.org/10.1515/boca-2016-0001.

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AbstractThe field of nanobiocatalysis has experienced a rapid growth due to recent advances in nanotechnology. However, biocatalytic processes are often limited by the lack of stability of the enzymes and their short lifetime. Therefore, immobilization is key to the successful implementation of industrial processes based on enzymes. Immobilization of enzymes on functionalized nanostructured materials could give higher stability to nanobiocatalysts while maintaining free enzyme activity and easy recyclability under various conditions. This review will discuss recent developments in nanobiocatal

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Fernández-Lafuente, Roberto, Verónica Rodrı́guez, Cesar Mateo, et al. "Stabilization of multimeric enzymes via immobilization and post-immobilization techniques." Journal of Molecular Catalysis B: Enzymatic 7, no. 1-4 (1999): 181–89. http://dx.doi.org/10.1016/s1381-1177(99)00028-4.

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Wang, Fang, Rong Li, Hui Jian, et al. "Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization." Catalysts 10, no. 4 (2020): 410. http://dx.doi.org/10.3390/catal10040410.

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In recent years, the development and application of site-specific immobilization technology for proteins have undergone significant advances, which avoids the unwanted and random covalent linkage between the support and active site of protein in the covalent immobilization. Formylglycine generating enzyme (FGE) can transform the cysteine from a conversed 6-amino-acid sequence CXPXR into formylglycine with an aldehyde group (also termed as “aldehyde tag”). Based on the frame of pET-28a, the His-tags were replaced with aldehyde tags. Afterward, a set of plasmids were constructed for site-specifi

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Oliveira-Ribeiro, Livia Maria, Lucas Meili, Georgia Nayane Silva-Belo-Gois, Renata Maria Rosas-Garcia-Almeida, and José Leandro da Silva-Duarte. "Immobilization of lipase in biochar obtained from Manihot esculenta Crantz." Revista ION 32, no. 2 (2019): 7–13. http://dx.doi.org/10.18273/revion.v32n2-2019001.

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The immobilized enzymes are catalysts of great industrial interest, as it unites the advantages of heterogeneous catalysis with the high selectivity and mild operation conditions of the enzymes. Biochar is a porous carbonaceous material, which have characteristic that it makes a strong candidate to incorporate enzymes in its structure. Another relevant fact is the possibility of changes and adaptations by synthesis condition in the biochar structure due to the application needs. In this context, the objective of this work was the study of immobilization of lipase (type II, code l3126, Sigma Al

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Wu, Zhuofu, Linjuan Shi, Xiaoxiao Yu, Sitong Zhang, and Guang Chen. "Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran." Molecules 24, no. 20 (2019): 3648. http://dx.doi.org/10.3390/molecules24203648.

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Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address th

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Kazenwadel, F., H. Wagner, B. E. Rapp, and M. Franzreb. "Optimization of enzyme immobilization on magnetic microparticles using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) as a crosslinking agent." Analytical Methods 7, no. 24 (2015): 10291–98. http://dx.doi.org/10.1039/c5ay02670a.

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Zhao, Man, Xiangmin Zhang, and Chunhui Deng. "Rational synthesis of novel recyclable Fe3O4@MOF nanocomposites for enzymatic digestion." Chemical Communications 51, no. 38 (2015): 8116–19. http://dx.doi.org/10.1039/c5cc01908g.

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Bonine, Bárbara M., Patricia Peres Polizelli, and Gustavo O. Bonilla-Rodriguez. "Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads." Enzyme Research 2014 (April 10, 2014): 1–7. http://dx.doi.org/10.1155/2014/738739.

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This study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized en

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Federsel, Hans-Jürgen, Thomas S. Moody, and Steve J. C. Taylor. "Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox." Molecules 26, no. 9 (2021): 2822. http://dx.doi.org/10.3390/molecules26092822.

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Enzymes have been exploited by humans for thousands of years in brewing and baking, but it is only recently that biocatalysis has become a mainstream technology for synthesis. Today, enzymes are used extensively in the manufacturing of pharmaceuticals, food, fine chemicals, flavors, fragrances and other products. Enzyme immobilization technology has also developed in parallel as a means of increasing enzyme performance and reducing process costs. The aim of this review is to present and discuss some of the more recent promising technical developments in enzyme immobilization, including the sup

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Lv, Shanshan. "Silk Fibroin-Based Materials for Catalyst Immobilization." Molecules 25, no. 21 (2020): 4929. http://dx.doi.org/10.3390/molecules25214929.

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Silk fibroin is a widely and commercially available natural protein derived from silkworm cocoons. Thanks to its unique amino acid composition and structure, which lead to localized nanoscale pockets with limited but sufficient hydration for protein interaction and stabilization, silk fibroin has been studied in the field of enzyme immobilization. Results of these studies have demonstrated that silk fibroin offers an important platform for covalent and noncovalent immobilization of enzymes through serving as a stabilization matrix/support with high retention of the biological activity of the e

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Alkan, S., H. Ceylan, and O. Arslan. "Bentonite-supported catalase." Journal of the Serbian Chemical Society 70, no. 5 (2005): 721–26. http://dx.doi.org/10.2298/jsc0505721a.

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The properties of the clay bentonite as a support for enzyme immobilization were studied using the enzyme catalase. Such an immobilization does not result in enzyme inactivation and constitutes a valuable method for immobilizing catalase at high ionic strength. The bentonite-supported catalase was characterized in terms of pH and ionic strength dependencies, thermal and storage stability and kinetic parameters. These studies indicate that bentonite is a valuable support for the simple adsorption of enzymes. .

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Giannakopoulou, Archontoula, Michaela Patila, Konstantinos Spyrou, et al. "Development of a Four-Enzyme Magnetic Nanobiocatalyst for Multi-Step Cascade Reactions." Catalysts 9, no. 12 (2019): 995. http://dx.doi.org/10.3390/catal9120995.

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We report the preparation, characterization and application of a novel magnetic four-enzyme nanobiocatalyst prepared by the simultaneous covalent co-immobilization of cellulase (CelDZ1), β-glucosidase (bgl), glucose oxidase (GOx) and horseradish peroxidase (HRP) onto the surface of amino-functionalized magnetic nanoparticles (MNPs). This nanobiocatalyst was characterized by various spectroscopic techniques. The co-immobilization process yielded maximum recovered enzymatic activity (CelDZ1: 42%, bgl: 66%, GOx: 94% and HRP: 78%) at a 10% v/v cross-linker concentration, after 2 h incubation time

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Parvulescu, Viorica, Adriana Popa, Gabriela Paun, Ramona Ene, Corneliu-Mircea Davidescu, and Gheorghe Ilia. "Effect of polymer support functionalization on enzyme immobilization and catalytic activity." Pure and Applied Chemistry 86, no. 11 (2014): 1793–803. http://dx.doi.org/10.1515/pac-2014-0715.

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Abstract Two enzymes, laccase and peroxidase, were immobilized on chloromethylated styrene-divinylbenzene copolymers supports functionalized with phosphonates ((RO)2PO) or mixed ammonium and phosphonium groups (N+R3Cl–, P+Ph3Cl–). Phosphonates groups and quaternary ammonium salts were grafted on the “gel-type” copolymer by Michaelis–Becker polymer analogue reaction. Mixed polymer-supported ammonium and phosphonium salts were obtained by transquaternization of the ammonium groups to phosphonium group. The degrees of functionalization for obtained polymers were relatively high ensuring a suffici

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Taha, Abdul Sattar Jabbar. "Different methods and carriers for immobilization cellulase from Trichoderma viride and its remaining activity." Pharmaceutical and Biological Evaluations 4, no. 1 (2017): 9. http://dx.doi.org/10.26510/2394-0859.pbe.2017.02.

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Objective: Many methods for enzymes immobilization and large number of carriers for immobilized enzymes, there are many benefits and diffeculties for immobilization, so the objective of this paper is to determine the suitable method and carrier for cellulase immobilization.Methods: Three methods used for immobilization which they adsorption, Glutaraldehyde and modified glutaraldehyde using two different carriers the first anion exchanger AM-21-A, and the second cation exchange fiber VION KN -1.Results: The result shows that the degree of saving catalytic activity for immobilized and free cellu

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Colon, Hugh D., and David R. Walt. "Immobilization of enzymes in polymer supports." Journal of Chemical Education 63, no. 4 (1986): 368. http://dx.doi.org/10.1021/ed063p368.

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Palomo, Jose. "Modulation of Enzymes Selectivity Via Immobilization." Current Organic Synthesis 6, no. 1 (2009): 1–14. http://dx.doi.org/10.2174/157017909787314885.

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Keusgen, Michael, Janina Glodek, Peter Milka, and Ingo Krest. "Immobilization of enzymes on PTFE surfaces." Biotechnology and Bioengineering 72, no. 5 (2001): 530–40. http://dx.doi.org/10.1002/1097-0290(20010305)72:5<530::aid-bit1017>3.0.co;2-j.

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Kalska-Szostko, B., M. Rogowska, A. Dubis, and K. Szymański. "Enzymes immobilization on Fe3O4–gold nanoparticles." Applied Surface Science 258, no. 7 (2012): 2783–87. http://dx.doi.org/10.1016/j.apsusc.2011.10.132.

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Daunert, Sylvia, Leonidas G. Bachas, Vesna Schauer-Vukasinovic, Kalvin J. Gregory, G. Schrift, and Sapna Deo. "Calmodulin-mediated reversible immobilization of enzymes." Colloids and Surfaces B: Biointerfaces 58, no. 1 (2007): 20–27. http://dx.doi.org/10.1016/j.colsurfb.2006.10.020.

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