Nanoporous Gold for Enzyme Immobilization

2016 ◽  
pp. 37-60 ◽  
Author(s):  
Keith J. Stine ◽  
Kenise Jefferson ◽  
Olga V. Shulga
Keyword(s):  
Enzyme Immobilization ◽  
Nanoporous Gold

scholarly journals Enzyme Immobilization on Nanoporous Gold: A Review

2017 ◽  
Vol 10 ◽  
pp. 117862641774860 ◽  
Author(s):  
Keith J Stine
Keyword(s):  
Pore Size ◽  
Enzyme Immobilization ◽  
High Surface ◽  
High Surface Area ◽  
Volume Ratio ◽  
Nanoporous Gold ◽  
Biofuel Cell ◽  
Redox Enzymes ◽  
Multiple Strategies ◽  
Enzyme Thermal Stability

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. Glucose oxidase immobilization on np-Au has been a focus for development of glucose sensors. Immobilization of laccase and related enzymes has demonstrated the utility of np-Au for construction of biofuel cells. Np-Au has been used to immobilize other redox enzymes, enzyme conjugates for use in bioassays, and enzymes of interest for industrial processes.

Nanoporous Gold for Enzyme Immobilization

2010 ◽  
pp. 67-83 ◽  
Author(s):  
Keith J. Stine ◽  
Kenise Jefferson ◽  
Olga V. Shulga
Keyword(s):  
Enzyme Immobilization ◽  
Nanoporous Gold

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.

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>

Application Progress of Nanoporous Gold in Analytical Chemistry

2013 ◽  
Vol 41 (1) ◽  
pp. 137 ◽  
Author(s):  
Li-Tuo ZHENG ◽  
Yu-Lei WEI ◽  
He-Qing GONG ◽  
Lei QIAN
Keyword(s):  
Analytical Chemistry ◽  
Nanoporous Gold

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.

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