Showing papers on "Immobilized enzyme published in 2018"
TL;DR: A general overview of the characteristics and properties of the materials applied for enzyme immobilization can be found in this article, where support materials are divided into two main groups, called Classic and New materials.
Abstract: In recent years, enzyme immobilization has been presented as a powerful tool for the improvement of enzyme properties such as stability and reusability. However, the type of support material used plays a crucial role in the immobilization process due to the strong effect of these materials on the properties of the produced catalytic system. A large variety of inorganic and organic as well as hybrid and composite materials may be used as stable and efficient supports for biocatalysts. This review provides a general overview of the characteristics and properties of the materials applied for enzyme immobilization. For the purposes of this literature study, support materials are divided into two main groups, called Classic and New materials. The review will be useful in selection of appropriate support materials with tailored properties for the production of highly effective biocatalytic systems for use in various processes.
580 citations
TL;DR: The overlap of technical expertise in enzyme immobilization, protein and process engineering will define the next generation of immobilized biocatalysts and the successful scale-up of their induced processes.
Abstract: Enzymes as industrial biocatalysts offer numerous advantages over traditional chemical processes with respect to sustainability and process efficiency. Enzyme catalysis has been scaled up for commercial processes in the pharmaceutical, food and beverage industries, although further enhancements in stability and biocatalyst functionality are required for optimal biocatalytic processes in the energy sector for biofuel production and in natural gas conversion. The technical barriers associated with the implementation of immobilized enzymes suggest that a multidisciplinary approach is necessary for the development of immobilized biocatalysts applicable in such industrial-scale processes. Specifically, the overlap of technical expertise in enzyme immobilization, protein and process engineering will define the next generation of immobilized biocatalysts and the successful scale-up of their induced processes. This review discusses how biocatalysis has been successfully deployed, how enzyme immobilization can improve industrial processes, as well as focuses on the analysis tools critical for the multi-scale implementation of enzyme immobilization for increased product yield at maximum market profitability and minimum logistical burden on the environment and user.
470 citations
TL;DR: This review outlines the existing methods and easy separated support materials for enzymes immobilization, and the emphasis is given on the easy separatedsupport materials of magnetic nanoparticles, membranes and capillary columns.
Abstract: Compared with free enzymes, immobilized enzymes are more robust and resistant to environmental changes. In addition, with enhanced stability, immobilized enzymes can be separated from the reaction mixture and used for repeated cycles. These advantages prompt their applications in various fields. This review outlines the existing methods and easy separated support materials for enzymes immobilization. After a brief introduction on the immobilized enzyme, the immobilization methods of adsorption, entrapment, covalent attachment and cross-linking are discussed. The emphasis is given on the easy separated support materials of magnetic nanoparticles (MNPs), membranes and capillary columns. An outlook on the immobilized enzyme is given at last.
267 citations
TL;DR: Remarkably, LDH immobilized in the large pores of the MOF is accessible to nicotinamide adenine dinucleotide coenzymes (NAD and NADH), allowing for in situ coenzyme regeneration leading to higher activity than that of the free enzyme.
244 citations
TL;DR: In this paper, a magnetically recyclable immobilized lipase was developed for biodiesel production to meet the need of green and clean production, which achieved an activity recovery of 64.9% and enzyme immobilization efficiency of 85.5%.
228 citations
TL;DR: In this article, a new class of two-dimensional transition metal carbides (or nitrides), called MXene-Ti 3 C 2, has been synthesized by exfoliating pristine Ti 3 AlC 2 phases with hydrofluoric acid.
204 citations
TL;DR: It is believed that through the integration of both enzyme engineering and enzyme immobilization strategies, novel biocatalysts can be obtained, not only as the sum of independently improved intrinsic and operational properties of enzymes, but ultimately tailored specifically for increased performance as immobilized biocAtalysts.
201 citations
TL;DR: This review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications and provides an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation.
195 citations
TL;DR: A new heterogeneous bio-catalyst was synthesized by encapsulating lipase into the microporous zeolite imidazolate framework, ZIF-67, using a bottle-around-a-ship method.
159 citations
TL;DR: In this paper, three-dimensional magnetic graphene oxide-magnetite polyvinyl alcohol (3D-GO/PVA/Fe3O4) nanocomposites were successfully prepared for porcine pancreatic lipase (PPL) enzyme immobilization.
155 citations
TL;DR: This review work presents state-of-the-art "Smart" chemistry of immobilization and novel potentialities of several materials-based cues with different geometries including microspheres, hydrogels and polymeric membranes, nanoparticles, nanofibers, composite and hybrid or blended support materials.
TL;DR: This article highlights the different strategies for enzyme immobilization such as physical adsorption, covalent binding, co-ordination bonding and de novo encapsulation method and about the artificial enzyme properties of magnetic-MOF coupled with enzyme to extend its application in biosensor.
TL;DR: In this paper, a nanohybrid material was developed and used for the first time to the kinetic resolution of secondary alcohols as rac-indanol, rac-1-phenylethanol (rac-1), rac-3-bromophenyl)-1-ethanol(rac-2), and rac-4.
Abstract: In this work, a nanohybrid material was developed and used for the first time to the kinetic resolution of secondary alcohols as rac-indanol, rac-1-phenylethanol (rac-1), rac-1-(3-bromophenyl)-1-ethanol (rac-2) and rac-1-(3-methylphenyl)-1-ethanol (rac-3). Chiral indanol is used as a precursor intermediate for the synthesis of enantiomeric drugs, such as (+)-Indatraline, Irindalone, Indinavir, (+)-Sertraline and Rasagiline mesylate. Chiral 1-phenylethanol is used as an ophthalmic preservative, a solvatochromic dye and an inhibitor of cholesterol absorption and as a mild floral fragrance. For this purpose, the ultrasound irradiation was used to couple APTES on the superparamagnetic nanoparticles surface. Then, the system was activated with glutaraldehyde and used as a support for immobilization of lipase from Pseudomonas fluorescens. Thermal stability analysis was performed in buffer and hexane, showing an excellent stability in buffer solution at 60 °C, holding 72% of the initial activity, even after 7 h. In hexane (40 °C), the immobilized enzyme retained 100% of activity with 693 min of half-life time at 50 °C. The high thermal stability is mainly related to the covalent bonding between enzymes and support. Immobilized lipase on magnetic support proved to be a robust biocatalyst in the kinetic resolution, leading to (S)-indanol with high selectivity (e.e. > 99%, E > 200) in 1.75 h at 50 °C, being reused five times without significant loss of the activity and selectivity. The kinetic resolution of rac-1, via acetylation reaction, catalyzed by lipase from Pseudomonas fluorescens immobilized on magnetic support, led to (R)-acetate with enantiomeric excess > 99% and to the remaining (S)-alcohol with enantiomeric excess of 94%, conversion of 49% and E > 200, after 48 h of reaction at 40 °C. Under the same reactions conditions, rac-2 and rac-3 were slightly less reactive, since the corresponding (R)-acetates were obtained with conversion values of 44%, but with high enantioselectivity (enantiomeric excesses > 99% and E values > 200). These results correspond to an important step in heterogeneous catalysis due to the ability to obtain important precursors for the synthesis of enantiomerically pure chiral drugs and other bioactive substances.
TL;DR: The utilization of site-directed spin labeling in combination with Electron Paramagnetic Resonance spectroscopy is demonstrated, which allows for the first time the characterization of the orientation of enzymes trapped on MOF surfaces.
Abstract: Enzyme immobilization in metal–organic frameworks (MOFs) offers retained enzyme integrity and activity, enhanced stability, and reduced leaching. Trapping enzymes on MOF surfaces would allow for catalysis involving large substrates. In both cases, the catalytic efficiency and selectivity depend not only on enzyme integrity/concentration but also orientation. However, it has been a challenge to determine the orientation of enzymes that are supported on solid matrices, which is even more challenging for enzymes immobilized/trapped in MOFs due to the interferences of the MOF background signals. To address such challenge, we demonstrate in this work the utilization of site-directed spin labeling in combination with Electron Paramagnetic Resonance spectroscopy, which allows for the first time the characterization of the orientation of enzymes trapped on MOF surfaces. The obtained insights are fundamentally important for MOF-based enzyme immobilization design and understanding enzyme orientation once trapped in...
TL;DR: An overview of the various aspects of enzymology, enzyme catalysis, enzyme immobilization and modulation of enzyme activity with special emphasis on modulation through different types of nanoparticles including their synthesis, characterization and applications is given.
TL;DR: The immobilized enzyme was found to be stabilized compared to the free enzyme, and the performance of the biocatalyst was evaluated by the degradation of phenolic compounds including phenol, p-chlorophenol and catechol.
TL;DR: In this article, the authors present a review on enzyme immobilization focusing on the three fundamental aspects to consider when dealing with the topic: catalytic properties, enzyme leakage and reusability.
Abstract: Transfer Challenges, Enzyme Leakage and Reuse of Materials DTU Orbit (04/08/2019) Enzyme Immobilization on Inorganic Surfaces for Membrane Reactor Applications: Mass Transfer Challenges, Enzyme Leakage and Reuse of Materials Enzyme immobilization is an established method for the enhancement of enzyme stability and reusability, two factors that are of great importance for industrial biocatalytic applications. Immobilization can be achieved by different methods and on a variety of carrier materials, both organic and inorganic. Inorganic materials provide the advantage of high stability and long service life which, together with the prolonged service life of the immobilized enzyme, can benefit the process economy. However, enzyme immobilization and increased stability often come at the cost of decreased enzyme activity. The main challenges involved in the design of an efficient immobilized enzyme system is to obtain both retention of high enzyme activity, enhanced stability and reusability, which is a complicated task, given the many variables involved, and the large numbers of methods and materials available. Simultaneously, new carrier materials and morphologies are constantly being developed. An investigation of enzyme immobilization systems on inorganic materials, with special emphasis on inorganic membranes, has been conducted in order to evaluate the effects of the immobilization system on the enzyme properties upon immobilization, i.e., activity, stability and reusability. The material properties of the enzyme carriers (particles and membranes) and their effects on the success of immobilization are described here. Furthermore, the reuse of inorganic membranes as enzyme carriers has been investigated and the reported examples show high ability of regeneration. To the best of our knowledge, this is the first review on enzyme immobilization focusing on the three fundamental aspects to consider when dealing with the topic: catalytic properties, enzyme leakage and reusability. Abbreviations: β‐Gal: β‐d‐galactosidase; ADH: alcohol dehydrogenase; AFM: atomic force microscopy; APTES: 3‐ aminopropyltriethoxysilane; APTMS: 3‐aminopropyltrimethoxysilane; BPA: bisphenol A; BSA: bovine serum albumin; CA: carbonic anhydrase; CALB: Candida antartica lipase B; CD: circular dichroism; CDI: carbonyldiimidazole; CLEA: cross‐ linked enzyme aggregates; CLSM: confocal laser scanning microscopy; CNT: carbon nanotube; CPG: controlled pore glass; CRL: Candida rugosa lipase; DMeDMOS: dimethyldimethoxysilane; DRIFT: diffuse reflectance Fourier transform infrared; E2: 17β‐estradiol; EDC: N‐(3‐dimethylaminopropyl)‐N′‐ethylcarbodiimide hydrochloride; EDS: electron dispersive spectroscopy; FDH: formate dehydrogenase; FESEM: field emission scanning microscopy; FT‐IR: Fourier transform infrared spectroscopy; GA: glutaraldehyde; GCSZn: coal fly ashes glass‐ceramic zinc sulfate; GOD: glucose oxidase; GPS: 3‐(glycidyloxypropyl)trimethoxysilane; HDMI: hexamethylene diisocyanate; HRP: horseradish peroxidase; IEP: isoelectric point; IPTES: (3‐isocyanatopropyl)triethoxysilane; IR: infrared spectroscopy; LbL: layer‐by‐layer: MCP: metallic ceramic powder; MeTEOS: methyltriethoxysilane; MF: microfiltration; MML: Mucor miehei lipase; MNP: magnetic nanoparticle; MPTMS: 3‐mercaptopropyltrimethoxysilane; NHS: N‐hydroxysuccinimidyl; PAH: poly(allylamine hydrochloride); PEI: polyethyleneimine; PEG: polyethylene glycol; PES: polyether sulfone; PM‐IRRAS: polarization modulation infrared reflection absorption spectroscopy; pNPA: para‐nitrophenyl acetate; pNPP: para‐nitrophenyl palmitate; PSS: polystyrene sulfonate; PTMS: phenyltrimethoxysilane; ROL: Rhizopus oryzae lipase; SCAD: Saccharomyces cerevisiae alcohol dehydrogenase; SDS: sodium dodecyl sulfate; SDS‐2: sodium dodecyl sulfonate; SEM: scanning electron microscopy; TEM: transmission electron microscopy; TEOS: tetraethoxysilane; TGA: thermogravimetric analysis; TLL: Thermomyces lanuginosa lipase; TMP: transmembrane pressure; TTIP: titanium tetraisoproxide; TVL: Trametes versicolor laccase; UF: ultrafiltration; VTMS: vinyltrimethylsilane
TL;DR: In this article, a functional biohybrid SiO2/Lig was selected to conduct the immobilization of glucose oxidase (GOx) by adsorption on its surface.
Abstract: In this paper, a novel procedure for receiving enzyme biosensor based on the cheap and functional silica/lignin (SiO2/Lig) hybrid material is presented. In this study, a functional biohybrid SiO2/Lig was selected to conduct the immobilization of glucose oxidase (GOx) by adsorption on its surface. The immobilized amount of GOx at SiO2/Lig was 25.28 mg g−1, twice as much compared to its amount at non-functionalized SiO2. The system of GOx-SiO2/Lig was combined with single-walled carbon nanotubes/platinum nanoparticles support to prepare a I generation glucose biosensor. Moreover, the GOx-SiO2/Lig based carbon paste electrode with ferrocene redox mediator was evaluated as an active material in II generation glucose biosensor. The GOx-SiO2/Lig/CPE was subjected to an examination in glucose solution by electrochemical techniques such as cyclic voltammetry (CV) and chronoamperometry. The obtained results suggest that GOx-SiO2/Lig can be a material of choice for preparation of an efficient and low-cost biosensor working in various electrode configurations. The newly obtained glucose biosensor presents promising electrochemical parameters for glucose determination. The glucose-sensing sensitivity amounted 0.78 μA mM−1. The biosensor showed a linear response range of 0.5–9 mM with a detection limit (LOD) of 145 μM.
TL;DR: It is demonstrated, for the first time, that the MOF matrix could act in synergy with the enzyme (Microperoxidase-8) and enhance selectivity the oxidation reaction of dyes and enhance resistance to acidic conditions.
Abstract: Microperoxidase-8, a small, peroxidase-type enzyme was immobilized into nanoparticles of the mesoporous and ultra-stable metal-organic framework (MOF) MIL-101(Cr). The immobilized enzyme fully retained its catalytic activity and exhibited enhanced resistance to acidic conditions. The biocatalyst was reusable and showed a long-term stability. By exploiting the properties of the MOF's framework, we demonstrated, for the first time, that the MOF matrix could act in synergy with the enzyme (Microperoxidase-8) and enhance selectivity the oxidation reaction of dyes. The oxidation rate of the harmful negatively charged dye (methyl orange) was significantly increased after enzyme immobilization, probably as a result of the pre-concentration of the methyl orange reactant owing to a charge matching between this dye and the MOF.
TL;DR: A self-powered biosensor was constructed by combining the PEC, and supercapacitor behavior of Co3O4 for the first time, and the utilization of the present PEC material can be extended to the other analytes detection through photoelectrochemistry.
TL;DR: In this paper, a new nano-system was designed as a solid support for cellulase immobilization which enhanced its thermal stability and facilitated its long term storage, while enzyme separation can be simply carried out by an external magnet.
TL;DR: The potential for the use of BCNF as carrier for lysozyme immobilization is demonstrated and the XRD analyses showed a decrease in diffraction intensities and crystallinity index of BC NF after immobilization of lyso enzyme.
TL;DR: This study illustrates the feasibility and the potential of a series of MOF-derived materials for biosensors with improved electrochemical performance and found that La-MOF-NH2 with wool-ball-like structure not only provided more active sites of multicontents to increase AChE immobilization amount but also facilitated the accessibility of electron transfer and shorten their diffusion length on the surface of electrode.
Abstract: An efficient and facile metal–organic framework (MOF)-template strategy for preparing carbon nanocomposites has been developed. First of all, a series of metal ions, including Fe3+, Zr4+, and La3+, were respectively connected with 2-aminoterephthalate (H2ATA) to form three metal-organic frameworks (MOFs) and then three novel MOF-derived materials were obtained by annealing them at 550 °C under N2 atmosphere. The morphologies and microstructure results showed that they still retained the original structure of MOFs and formed carbon-supported metal oxide hybrid nanomaterials. Interestingly, it was found that La-MOF-NH2 and its derived materials were first reported, which had wool-ball-like structure formed by many streaky-shaped particles intertwining each other. Furthermore, these MOF-derived materials were all successfully used as effective immobilization matrixes of acetylcholinesterase (AChE) to construct biosensors for the detection of methyl parathion. Especially, [La-MOF-NH2]N2 with wool-ball-like st...
TL;DR: Improvements in enzyme catalytic properties via immobilization made this nanobiocatalyst as a good candidate in bio-industrial applications and the synthesized nanocomposite would have the potential for practical applications in other and binary enzyme immobilization.
TL;DR: A novel biocompatible magnetic chitin nanofiber composite (MCNC) was developed as a support for enzyme immobilization, and the enzyme-immobilizing ability was elucidated using chymotrypsin (CT) as a model enzyme.
Abstract: In this study, a novel biocompatible magnetic chitin nanofiber composite (MCNC) was developed as a support for enzyme immobilization, and the enzyme-immobilizing ability was elucidated using chymotrypsin (CT) as a model enzyme. Chitin nanofibers (CNFs) were prepared via 2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO)-mediated oxidation of chitin and then further modified with magnetic nanoparticles. Glutaraldehyde was used to cross-link the additional CT molecules and aggregate them onto the MCNCs. The CNFs were characterized by transmission electron microscopy, and Fourier transform infrared spectroscopy. The results showed that the CNFs were properly formed and that the CT molecules immobilized on the MCNCs presented excellent properties. After heating the composites at 60 °C for 3 h, the non-cross-linked and cross-linked immobilized CTs retained 51.6% and 70.7% of the initial activity, respectively, whereas the free CTs retained only 29.6% of the initial activity. In addition, non-cross-linked and cross-l...
TL;DR: In this paper, a one-step encapsulation method for synthesizing X-shaped zeolitic imidazolate frameworks (ZIF-8) and immobilizing Rhizomucor miehei lipase (RML) was presented.
Abstract: This study presents a one-step encapsulation method for synthesizing X-shaped zeolitic imidazolate frameworks (ZIF-8) and immobilizing Rhizomucor miehei lipase (RML). We proved that the morphological structure of ZIF-8 had changed after immobilization with enhanced characterization using a field-emission scanning electron microscope, an energy-dispersive spectrometer, a transmission electron microscope, a Fourier transform infrared spectrometer, and powder X-ray diffraction. The surface area and pore size of the carrier were investigated before and after immobilization using Brunauer–Emmett–Teller and Barrett–Joyner–Halenda methods, respectively. RML@ZIF-8 exhibited high recovery activity of up to 2632%, representing a 26-fold increase in its free lipase. Encapsulated RML was used for biodiesel production from soybean oil in an isooctane system with a conversion yield of 95.6% under optimum conditions. The resulting reusability of the immobilized enzyme indicated no substantial decline in the conversion yield, which remained at 84.7% of the initial activity after 10 cycles. The stability and high performance of the immobilized enzyme are attributed to the harmony between RML and ZIF-8 based on the easy synthesis of ZIF-8 and the short time required to immobilize RML.
TL;DR: The immobilized enzyme retained >90% of its initial capability to degrade BPA after 15cycles of reuse and could be an economical alternative for large scale degradation of BPA in aqueous systems.
TL;DR: The new biocatalysts are significantly more stable and avoid enzyme subunit desorption, being the immobilization pH a key point in their design.
TL;DR: In this paper, supports based on chitosan and nanoclays were produced by solvent casting technique, and investigated for use as a covalently linked bromelain carrier in wine-like medium.
TL;DR: A novel method of enzyme immobilization involving covalent immobilization of β-galactosidase on 3-aminopropyl triethoxysilane(3-APTES)-modified glass beads was developed by the cross-linking method and increased pH and thermal stabilities were observed for the immobilized enzyme versus the free enzyme.