A Spring in Performance: Silica Nanosprings Boost Enzyme Immobilization in Microfluidic Channels

2017 ◽  
Vol 9 (40) ◽  
pp. 34641-34649 ◽  
Author(s):  
Donya Valikhani ◽  
Juan M. Bolivar ◽  
Martina Viefhues ◽  
David N. McIlroy ◽  
Elwin X. Vrouwe ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Microfluidic Channels ◽  
Silica Nanosprings

Immobilization of thermophilic enzymes in miniaturized flow reactors

2007 ◽  
Vol 35 (6) ◽  
pp. 1621-1623 ◽  
Author(s):  
A.M. Hickey ◽  
L. Marle ◽  
T. McCreedy ◽  
P. Watts ◽  
G.M. Greenway ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Flow Reactor ◽  
Capillary Flow ◽  
Enzyme Stability ◽  
Substrate Inhibition ◽  
Cost Effective ◽  
Microfluidic Channels ◽  
Flow Reactors ◽  
Thermophilic Archaeon ◽  
The Cost

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 advantages over batch enzyme assay systems. Since the assay is performed on a miniaturized scale, enzyme, substrate and cofactor quantities are significantly reduced, thus reducing the cost of laboratory-scale investigations. Since flow reactors use microfluidic systems, where the substrate and products flow out of the system, the problems of substrate inhibition and product inhibition encountered by some enzymes are avoided. Quite often, enzymes fulfil a single-use function in biotransformation processes; however, enzyme immobilization allows enzyme reuse and often helps to increase enzyme stability. We have used an aminoacylase enzyme with potential use for industrial biotransformation reactions and have successfully immobilized it in miniaturized flow reactors. This L-aminoacylase is from the thermophilic archaeon Thermococcus litoralis. Two approaches to enzyme immobilization have been examined, both involving enzyme cross-linking. The first reactor type has used monoliths, to which the enzyme was attached, and the second contained previously cross-linked enzyme trapped using frits, in the microfluidic channels. Two different microreactor designs were used in the investigation: microreactor chips for the monoliths and capillary flow reactors for the cross-linked enzyme. These systems allowed passage of the substrate and product through the system while retaining the aminoacylase enzyme performing the catalytic conversion. The enzyme has been successfully immobilized and used to produce stable biocatalytic microreactors that can be used repeatedly over a period of several months.

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  
Keyword(s):  
Enzyme Immobilization ◽  
Maleic Acid ◽  
Environmentally Friendly ◽  
Synthetic Polymer ◽  
Magnetic Composites ◽  
Interpolyelectrolyte Complex ◽  
Hydrolysis Rates ◽  
Poly Ethylene ◽  
Noncovalent Binding

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

JOULE HEATING INDUCED HEAT TRANSFER IN ELECTROKINETIC FLOW THROUGH MICROFLUIDIC CHANNELS

Equipment ◽  
2006 ◽  
Author(s):  
C. Yang ◽  
G. Y. Tang ◽  
D. G. Yan ◽  
H. Q. Gong ◽  
John C. Chai ◽  
...  
Keyword(s):  
Heat Transfer ◽  
Joule Heating ◽  
Microfluidic Channels ◽  
Electrokinetic Flow ◽  
Flow Through

Stochastic Computing via In Operando Modulation of Rectification in Molecular Tunneling Junctions

2020 ◽  
Author(s):  
Xinkai Qiu ◽  
Sylvia Rousseva ◽  
Gang Ye ◽  
Jan C. Hummelen ◽  
Ryan Chiechi
Keyword(s):  
Self Assembly ◽  
Variable Temperature ◽  
Self Assembled Monolayers ◽  
Microfluidic Channels ◽  
Proof Of Concept ◽  
Glycol Ethers ◽  
Stochastic Computing ◽  
Assembled Monolayers ◽  
In Operando ◽  
Tunneling Junctions

This paper describes the reconfiguration of molecular tunneling junctions during operation via the self-assembly of bilayers of glycol ethers. We use well-established functional groups to modulate the magnitude and direction of rectification in assembled tunneling junctions by exposing them to solutions containing different glycol ethers. Variable-temperature measurements establish that rectification occurs by a bias-dependent tunneling-hopping mechanism and that glycol ethers, beside being an unusually efficient tunneling medium, behave identically to alkanes. We fabricated memory bits from crossbar junctions prepared by injecting eutectic Ga-In into microfluidic channels. Two 8-bit registers were able to perform logical AND operations on bit strings encoded into chemical packets as microfluidic droplets that alter the composition of the crossbar junctions through self-assembly to effect memristor-like properties. This proof of concept work demonstrates the potential for fieldable molecular-electronic devices based on tunneling junctions of self-assembled monolayers and bilayers.

Biocatalytic Ketone Reductions Using Biobeads

2020 ◽  
Author(s):  
Jia Shen Chew ◽  
Ken Chi Lik Lee ◽  
THI THANH NHA HO
Keyword(s):  
Enzyme Immobilization ◽  
High Throughput ◽  
High Throughput Screening ◽  
Chiral Hplc ◽  
Micro Scale

<p>Lee and coworkers offers a kind of new concept to enzyme immobilization and explores its suitability in the context of miniaturisation and high-throughput screening. Here, polystyrene-immobilized ketoreductases are compared with its non-immobilized counterparts in terms of conversion and stereoselectivity (both determined by chiral HPLC), and the study indicates that the BioBeads perform similarly (sometimes slightly more selective) which may be useful whenever defined micro-scale amounts of biocatalysts were required in high-throughput experiment settings.</p>

Enzyme Immobilization on Nanomaterials for Biosensor and Biocatalyst in Food and Biomedical Industry

2019 ◽  
Vol 25 (24) ◽  
pp. 2661-2676 ◽  
Author(s):  
Sundaresan Bhavaniramya ◽  
Ramar Vanajothi ◽  
Selvaraju Vishnupriya ◽  
Kumpati Premkumar ◽  
Mohammad S. Al-Aboody ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzyme Immobilization ◽  
Food Industry ◽  
Environmental Changes ◽  
Immobilized Enzymes ◽  
Food Industries ◽  
Physiological Processes ◽  
Different Types ◽  
Simple Processing ◽  
Biomedical Industry

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 methodology in the pharmaceutical industry. Compared to the free enzymes, immobilized forms are more robust and resistant to environmental changes. In this method, the mobility of enzymes is artificially restricted to changing their structure and properties. Due to their sensitive nature, the classical immobilization methods are still limited as a result of the reduction of enzyme activity. In order to improve the enzyme activity and their properties, nanomaterials are used as a carrier for enzyme immobilization. Recently, much attention has been directed towards the research on the potentiality of the immobilized enzymes in the food industry. Hence, the present review emphasizes the different types of immobilization methods that is presently used in the food industry and other applications. Various types of nanomaterials such as nanofibers, nanoflowers and magnetic nanoparticles are significantly used as a support material in the immobilization methods. However, several numbers of immobilized enzymes are used in the food industries to improve the processing methods which not only reduce the production cost but also the effluents from the industry.

scholarly journals α-Cellulose Fibers of Paper-Waste Origin Surface-Modified with Fe3O4 and Thiolated-Chitosan for Efficacious Immobilization of Laccase

Polymers ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 581
Author(s):  
Gajanan S. Ghodake ◽  
Surendra K. Shinde ◽  
Ganesh D. Saratale ◽  
Rijuta G. Saratale ◽  
Min Kim ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Photoelectron Spectroscopy ◽  
Cellulose Fibers ◽  
Relative Activity ◽  
Significant Activity ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron ◽  
Laccase Immobilization ◽  
Surface Modified

The utilization of waste-paper-biomass for extraction of important α-cellulose biopolymer, and modification of extracted α-cellulose for application in enzyme immobilization can be extremely vital for green circular bio-economy. Thus, in this study, α-cellulose fibers were super-magnetized (Fe3O4), grafted with chitosan (CTNs), and thiol (-SH) modified for laccase immobilization. The developed material was characterized by high-resolution transmission electron microscopy (HR-TEM), HR-TEM energy dispersive X-ray spectroscopy (HR-TEM-EDS), X-ray diffraction (XRD), vibrating sample magnetometer (VSM), X-ray photoelectron spectroscopy (XPS), and Fourier transform infrared spectroscopy (FT-IR) analyses. Laccase immobilized on α-Cellulose-Fe3O4-CTNs (α-Cellulose-Fe3O4-CTNs-Laccase) gave significant activity recovery (99.16%) and laccase loading potential (169.36 mg/g). The α-Cellulose-Fe3O4-CTNs-Laccase displayed excellent stabilities for temperature, pH, and storage time. The α-Cellulose-Fe3O4-CTNs-Laccase applied in repeated cycles shown remarkable consistency of activity retention for 10 cycles. After the 10th cycle, α-Cellulose-Fe3O4-CTNs possessed 80.65% relative activity. Furthermore, α-Cellulose-Fe3O4-CTNs-Laccase shown excellent degradation of pharmaceutical contaminant sulfamethoxazole (SMX). The SMX degradation by α-Cellulose-Fe3O4-CTNs-Laccase was found optimum at incubation time (20 h), pH (3), temperatures (30 °C), and shaking conditions (200 rpm). Finally, α-Cellulose-Fe3O4-CTNs-Laccase gave repeated degradation of SMX. Thus, this study presents a novel, waste-derived, highly capable, and super-magnetic nanocomposite for enzyme immobilization applications.

scholarly journals Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

2021 ◽  
Author(s):  
Agnieszka Kołodziejczak-Radzimska ◽  
Long D. Nghiem ◽  
Teofil Jesionowski
Keyword(s):  
Wastewater Treatment ◽  
Enzyme Immobilization ◽  
Organic Dyes ◽  
Scientific Progress ◽  
Immobilized Enzymes ◽  
Chemical Oxidation ◽  
Biologically Active ◽  
Water Pollutants ◽  
Untreated Wastewater ◽  
Functionalized Materials

Abstract Purpose of Review Untreated wastewater discharge can significantly and negatively impact the state of the environment. Rapid industrialization and economic development have directly contributed to land and water pollution resulting from the application of many chemicals such as organic dyes, pharmaceuticals, and industrial reagents. The removal of these chemicals before effluent discharge is crucial for environmental protection. This review aims to explore the importance of functionalized materials in the preparation of biocatalytic systems and consider their application in eliminating water pollutants. Recent Findings Wastewater treatment methods can be classified into three groups: (i) chemical (e.g., chemical oxidation and ozonation), (ii) physical (e.g., membrane separation and ion exchange), and (iii) biological processes. Biological treatment is the most widely used method due to its cost-effectiveness and eco-friendliness. In particular, the use of immobilized enzymes has recently become more attractive as a result of scientific progress in advanced material synthesis. The selection of an appropriate support plays an important role in the preparation of such biologically active systems. Recent studies have demonstrated the use of various materials for enzyme immobilization in the purification of water. Summary This review identifies and discusses different biocatalytic systems used in the enzymatic degradation of various water pollutants. Materials functionalized by specific groups can serve as good support matrices for enzyme immobilization, providing chemical and thermal stability to support catalytic reactions. Enzymatic biocatalysis converts the pollutants into simpler products, which are usually less toxic than their parents. Due to immobilization, the enzyme can be used over multiple cycles to reduce the cost of wastewater treatment. Future studies in this field should focus on developing new platforms for enzyme immobilization in order to improve degradation efficiency.

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