Special Issue "Immobilized Enzymes: Strategies for Enzyme Stabilization"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: closed (15 November 2016)

Special Issue Editor

Guest Editor
Prof. Dr. Jose M. Guisan

Department of Biocatalysis, Institute of Catalysis, Spanish Research Council, ICP-CSIC, Campus UAM, 28049 Madrid, Spain
Website1 | Website2 | E-Mail
Phone: +34 91 585 48 09
Interests: enzyme engineering: purification, immobilization, stabilization, reactivation; hyperactivation; main enzymes: lipases, penicillin G acylase, endoxylanases, beta-xylosidases, etc.; enzyme processes: fine chemistry, food chemistry, analytical chemistry, green energy; enzyme reactors: stirred tanks, packed beds, etc.

Special Issue Information

Dear Colleagues,

Enzymes are able to catalyze the most complex chemical processes under the most benign experimental and environmental conditions. In this way, enzymes could be excellent catalysts for a much more sustainable chemical industry. For industrial applications, enzymes have to be immobilized, via simple and cost-effective protocols, in order to be re-used for very long periods of time. From this point of view, immobilization, simplicity and stabilization are strongly related concepts.  The preparation of optimal and cost-effective enzyme biocatalyst is the main topic of this special issue.

This Special Issue is devoted to:

  • The critical revision of simple protocols for immobilization-stabilization of enzymes
  • The improvement of functional properties of enzymes via immobilization and post-immobilization techniques.

Prof. Dr. Jose M. Guisan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • immobilization techniques
  • stabilization strategies
  • chemical modification of immobilized enzymes
  • lipases in anhydrous media
  • supports for enzyme
  • immobilization

Published Papers (13 papers)

View options order results:
result details:
Displaying articles 1-13
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle Stabilization of a Lipolytic Enzyme for Commercial Application
Catalysts 2017, 7(3), 91; doi:10.3390/catal7030091
Received: 26 January 2017 / Revised: 6 March 2017 / Accepted: 10 March 2017 / Published: 21 March 2017
PDF Full-text (2811 KB) | HTML Full-text | XML Full-text
Abstract
Thermomyces lanouginosa lipase has been used to develop improved methods for carrier-free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator
[...] Read more.
Thermomyces lanouginosa lipase has been used to develop improved methods for carrier-free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator molecule, in order to obtain a higher number of the individual lipase molecules in the ”open lid” conformation prior to the cross-linking step. A terminator step has been introduced to quench the cross-linking reaction at an optimal time by treatment with an amine buffer in order to obtain smaller and more homogenous cross-linked particles. This improved immobilization method has been compared to a commercially available enzyme and has been shown to be made up of smaller and more homogenous particles with an average diameter of 1.85 ± 0.28 µm which are 129.7% more active than the free enzyme. The CLEAs produced show improved features for commercial applications such as an improved wash performance comparable with the free enzyme, improved stability to proteolysis and a higher activity after long-term storage. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessArticle Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles
Catalysts 2017, 7(2), 49; doi:10.3390/catal7020049
Received: 9 December 2016 / Revised: 18 January 2017 / Accepted: 25 January 2017 / Published: 6 February 2017
PDF Full-text (4327 KB) | HTML Full-text | XML Full-text
Abstract
Here, core-shell structured polydopamine-coated Fe3O4 nanoparticles were constructed to immobilize thermostable lipase QLM from Alcaligenes sp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 ± 1.47 mg/g immobilized
[...] Read more.
Here, core-shell structured polydopamine-coated Fe3O4 nanoparticles were constructed to immobilize thermostable lipase QLM from Alcaligenes sp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 ± 1.47 mg/g immobilized enzyme. Then, the immobilized enzyme was demonstrated to possess favorable catalytic activity and stability in the ester hydrolysis, using p-nitrophenyl caprylate as the substrate. Further, it was successfully employed in the kinetic resolution of (R, S)-2-octanol, and satisfactory enantioselectivity and recyclability could be obtained with an enantiomeric ratio (E) of 8–15 over 10 cycle reactions. Thus, core-shell structured polydopamine-coated Fe3O4 nanoparticles can be potentially used as a carrier for enzyme immobilization to improve their activity, stability, and reusability, which is beneficial for constructing efficient catalysts for industrial biocatalysis. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessArticle Sucrose Hydrolysis in a Bespoke Capillary Wall-Coated Microreactor
Catalysts 2017, 7(2), 42; doi:10.3390/catal7020042
Received: 14 November 2016 / Accepted: 24 January 2017 / Published: 27 January 2017
Cited by 2 | PDF Full-text (2440 KB) | HTML Full-text | XML Full-text
Abstract
Microscale technology has been increasingly used in chemical synthesis up to production scale, but in biocatalysis the implementation has been proceeding at a slower pace. In this work, the design of a low cost and versatile continuous flow enzyme microreactor is described that
[...] Read more.
Microscale technology has been increasingly used in chemical synthesis up to production scale, but in biocatalysis the implementation has been proceeding at a slower pace. In this work, the design of a low cost and versatile continuous flow enzyme microreactor is described that illustrates the potential of microfluidic reactors for both the development and characterization of biocatalytic processes. The core structure of the developed reactor consists of an array of capillaries with 450 μm of inner diameter with their inner surface functionalized with (3-aminopropyl)triethoxysilane (APTES) and glutaraldehyde where Saccharomyces cerevisiae invertase was covalently bound. The production of invert sugar syrup through enzymatic sucrose hydrolysis was used as model system. Once the microreactor assembly reproducibility and the immobilized enzyme behavior were established, the evaluation of the immobilized enzyme kinetic parameters was carried out at flow rates ranging from 20.8 to 219.0 μL·min−1 and substrate concentrations within 2.0%–10.0% (w/v). Despite the impact of immobilization on the kinetic parameters, viz. Km(app) was increased two fold and Kcat showed a 14-fold decrease when compared to solution phase invertase, the immobilization proved highly robust. For a mean residence time of 48.8 min, full conversion of 5.0% (w/v) sucrose was observed over 20 days. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessArticle Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid
Catalysts 2017, 7(1), 26; doi:10.3390/catal7010026
Received: 27 October 2016 / Revised: 6 January 2017 / Accepted: 10 January 2017 / Published: 14 January 2017
Cited by 2 | PDF Full-text (4218 KB) | HTML Full-text | XML Full-text
Abstract
This article presents a novel route for crosslinking a polysaccharide and polysaccharide/protein shell coated on magnetic nanoparticles (MNPs) surface via condensation reaction with squaric acid (SqA). The syntheses of four new types of collagen-, chitosan-, and chitosan–collagen coated magnetic nanoparticles as supports for
[...] Read more.
This article presents a novel route for crosslinking a polysaccharide and polysaccharide/protein shell coated on magnetic nanoparticles (MNPs) surface via condensation reaction with squaric acid (SqA). The syntheses of four new types of collagen-, chitosan-, and chitosan–collagen coated magnetic nanoparticles as supports for enzyme immobilization have been done. Structure and morphology of prepared new materials were characterized by attenuated total reflectance Fourier-transform infrared (ATR-FTIR), XRD, and TEM analysis. Next, the immobilization of lipase from Candida rugosa was performed on the nanoparticles surface via N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride (EDC)/N-hydroxy-succinimide (NHS) mechanism. The best results of lipase activity recovery and specific activities were observed for nanoparticles with polymer shell crosslinked via a novel procedure with squaric acid. The specific activity for lipase immobilized on materials crosslinked with SqA (52 U/mg lipase) was about 2-fold higher than for enzyme immobilized on MNPs with glutaraldehyde addition (26 U/mg lipase). Moreover, a little hyperactivation of lipase immobilized on nanoparticles with SqA was observed (104% and 112%). Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Open AccessArticle Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System
Catalysts 2017, 7(1), 14; doi:10.3390/catal7010014
Received: 24 November 2016 / Revised: 27 December 2016 / Accepted: 29 December 2016 / Published: 31 December 2016
Cited by 2 | PDF Full-text (3464 KB) | HTML Full-text | XML Full-text
Abstract
A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force
[...] Read more.
A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 °C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7–9 and temperature from 30 °C to 60 °C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 °C. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Open AccessArticle Synthesis and Characterization of Highly Stabilized Polymer–Trypsin Conjugates with Autolysis Resistance
Catalysts 2017, 7(1), 4; doi:10.3390/catal7010004
Received: 30 November 2016 / Revised: 20 December 2016 / Accepted: 22 December 2016 / Published: 26 December 2016
Cited by 1 | PDF Full-text (1806 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Protein digestion by trypsin has been widely used in many industrial and research applications. However, extensive use of trypsin is limited because of the rapid decrease in enzymatic activity caused by autolysis at optimal pH and temperature. To improve the enzymatic performance of
[...] Read more.
Protein digestion by trypsin has been widely used in many industrial and research applications. However, extensive use of trypsin is limited because of the rapid decrease in enzymatic activity caused by autolysis at optimal pH and temperature. To improve the enzymatic performance of trypsin, we synthesized highly stabilized polymer–trypsin conjugates using vinylmethylether-maleic acid copolymer (VEMAC) via multi-point attachment. The VEMAC modification significantly enhanced the thermal stability of trypsin, and the resulting conjugates showed a strong resistance to autolysis. VEMAC-modified trypsin (VEMAC-Tryp) showed maximum activity at 55 °C and at 1.4-fold higher levels than that of unmodified trypsin. Bovine serum albumin was effectively digested by VEMAC-Tryp, indicating that the modified trypsin can be used for digestion of high molecular weight substrates. VEMAC modification is a simple and cost-effective strategy to obtain fully active modified enzymes, and may be used to develop bioreactors. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Open AccessArticle Investigation of the Effect of Plasma Polymerized Siloxane Coating for Enzyme Immobilization and Microfluidic Device Conception
Catalysts 2016, 6(12), 209; doi:10.3390/catal6120209
Received: 14 October 2016 / Revised: 25 November 2016 / Accepted: 9 December 2016 / Published: 16 December 2016
Cited by 1 | PDF Full-text (2935 KB) | HTML Full-text | XML Full-text
Abstract
This paper describes the impact of a physical immobilization methodology, using plasma polymerized 1,1,3,3, tetramethyldisiloxane, on the catalytic performance of β-galactosidase from Aspergillus oryzae in a microfluidic device. The β-galactosidase was immobilized by a polymer coating grown by Plasma Enhanced Chemical Vapor Deposition
[...] Read more.
This paper describes the impact of a physical immobilization methodology, using plasma polymerized 1,1,3,3, tetramethyldisiloxane, on the catalytic performance of β-galactosidase from Aspergillus oryzae in a microfluidic device. The β-galactosidase was immobilized by a polymer coating grown by Plasma Enhanced Chemical Vapor Deposition (PEVCD). Combined with a microchannel patterned in the silicone, a microreactor was obtained with which the diffusion through the plasma polymerized layer and the hydrolysis of a synthetic substrate, the resorufin-β-d-galactopyranoside, were studied. A study of the efficiency of the immobilization procedure was investigated after several uses and kinetic parameters of immobilized β-galactosidase were calculated and compared with those of soluble enzyme. Simulation and a modelling approach were also initiated to understand phenomena that influenced enzyme behavior in the physical immobilization method. Thus, the catalytic performances of immobilized enzymes were directly influenced by immobilization conditions and particularly by the diffusion behavior and availability of substrate molecules in the enzyme microenvironment. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Open AccessArticle Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS)
Catalysts 2016, 6(12), 189; doi:10.3390/catal6120189
Received: 24 October 2016 / Revised: 23 November 2016 / Accepted: 27 November 2016 / Published: 30 November 2016
Cited by 2 | PDF Full-text (2832 KB) | HTML Full-text | XML Full-text
Abstract
The β-galactosidase from Bacillus circulans was covalently attached to aldehyde-activated (glyoxal) agarose beads and assayed for the continuous production of galactooligosaccharides (GOS) in a packed-bed reactor (PBR). The immobilization was fast (1 h) and the activity of the resulting biocatalyst was 97.4 U/g
[...] Read more.
The β-galactosidase from Bacillus circulans was covalently attached to aldehyde-activated (glyoxal) agarose beads and assayed for the continuous production of galactooligosaccharides (GOS) in a packed-bed reactor (PBR). The immobilization was fast (1 h) and the activity of the resulting biocatalyst was 97.4 U/g measured with o-nitrophenyl-β-d-galactopyranoside (ONPG). The biocatalyst showed excellent operational stability in 14 successive 20 min reaction cycles at 45 °C in a batch reactor. A continuous process for GOS synthesis was operated for 213 h at 0.2 mL/min and 45 °C using 100 g/L of lactose as a feed solution. The efficiency of the PBR slightly decreased with time; however, the maximum GOS concentration (24.2 g/L) was obtained after 48 h of operation, which corresponded to 48.6% lactose conversion and thus to maximum transgalactosylation activity. HPAEC-PAD analysis showed that the two major GOS were the trisaccharide Gal-β(1→4)-Gal-β(1→4)-Glc and the tetrasaccharide Gal-β(1→4)-Gal-β(1→4)-Gal-β(1→4)-Glc. The PBR was also assessed in the production of GOS from milk as a feed solution. The stability of the bioreactor was satisfactory during the first 8 h of operation; after that, a decrease in the flow rate was observed, probably due to partial clogging of the column. This work represents a step forward in the continuous production of GOS employing fixed-bed reactors with immobilized β-galactosidases. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Open AccessArticle Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface
Catalysts 2016, 6(11), 174; doi:10.3390/catal6110174
Received: 22 September 2016 / Revised: 26 October 2016 / Accepted: 27 October 2016 / Published: 8 November 2016
Cited by 2 | PDF Full-text (2587 KB) | HTML Full-text | XML Full-text
Abstract
In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used
[...] Read more.
In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used and the influence of membrane surface conditions on the activities of immobilized lipases was evaluated. Water contact angle measurement as well as field emission scanning electron microscopy were used to characterize the morphology of the modified membranes. The results showed an improvement in the adsorption capacity (26.0 mg/m2) and activity retention (68.2%) of the immobilized lipases on the PBAP-modified PPMM. Moreover, the lipases immobilized on the modified PPMM showed better thermal and pH stability. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessArticle Enhancing the Enzymatic Activity of a Heme-Dependent Peroxidase through Genetic Modification
Catalysts 2016, 6(11), 166; doi:10.3390/catal6110166
Received: 28 August 2016 / Revised: 14 October 2016 / Accepted: 18 October 2016 / Published: 27 October 2016
Cited by 1 | PDF Full-text (3971 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
A heme-dependent peroxidase (HDP) catalyzes the ortho-hydroxylation of l-tyrosine to l-3,4-dihydroxyphenylalanine (l-DOPA) in the presence of hydrogen peroxide. l-DOPA can be used for the treatment of Parkinson's disease. In this work, to improve the catalytic efficiency, the heme-dependent
[...] Read more.
A heme-dependent peroxidase (HDP) catalyzes the ortho-hydroxylation of l-tyrosine to l-3,4-dihydroxyphenylalanine (l-DOPA) in the presence of hydrogen peroxide. l-DOPA can be used for the treatment of Parkinson's disease. In this work, to improve the catalytic efficiency, the heme-dependent peroxidase has been genetically modified with an elastin-like polypeptide (ELP). bicinchoninic acid (BCA) assay demonstrated that HDP-ELP has a higher solubility in aqueous solutions than HDP. Circular dichroism (CD) spectra showed that HDP-ELP has a higher stability than HDP. Enzyme kinetics has been investigated over a range of substrate concentrations. It has been demonstrated that HDP-ELP exhibited a catalytic efficiency 2.4 times that of HDP. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessArticle Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials
Catalysts 2016, 6(10), 149; doi:10.3390/catal6100149
Received: 9 June 2016 / Revised: 30 July 2016 / Accepted: 21 September 2016 / Published: 24 September 2016
Cited by 4 | PDF Full-text (2207 KB) | HTML Full-text | XML Full-text
Abstract
Lipase from Aspergillus niger was “doubly immobilized” with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results
[...] Read more.
Lipase from Aspergillus niger was “doubly immobilized” with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 μL of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Review

Jump to: Research

Open AccessReview Improving the Stability of Cold-Adapted Enzymes by Immobilization
Catalysts 2017, 7(4), 112; doi:10.3390/catal7040112
Received: 13 January 2017 / Revised: 30 March 2017 / Accepted: 4 April 2017 / Published: 12 April 2017
Cited by 1 | PDF Full-text (629 KB) | HTML Full-text | XML Full-text
Abstract
Cold-adapted enzymes have gained considerable attention as biocatalysts that show high catalytic activity at low temperatures. However, the use of cold-adapted enzymes at ambient temperatures has been hindered by their low thermal stabilities caused by their inherent structural flexibilities. Accordingly, protein engineering and
[...] Read more.
Cold-adapted enzymes have gained considerable attention as biocatalysts that show high catalytic activity at low temperatures. However, the use of cold-adapted enzymes at ambient temperatures has been hindered by their low thermal stabilities caused by their inherent structural flexibilities. Accordingly, protein engineering and immobilization have been employed to improve the thermal stability of cold-adapted enzymes. Immobilization has been shown to increase the thermal stability of cold-adapted enzymes at the critical temperatures at which denaturation begins. This review summarizes progress in immobilization of cold-adapted enzymes as a strategy to improve their thermal and organic solvent stabilities. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Open AccessReview How to Lengthen the Long-Term Stability of Enzyme Membranes: Trends and Strategies
Catalysts 2017, 7(2), 36; doi:10.3390/catal7020036
Received: 19 December 2016 / Revised: 17 January 2017 / Accepted: 19 January 2017 / Published: 24 January 2017
Cited by 2 | PDF Full-text (1661 KB) | HTML Full-text | XML Full-text
Abstract
In this review, factors that contribute to enhancing the stability of immobilized enzyme membranes have been indicated, and the solutions to each factor, based on examples, are discussed. The factors are divided into two categories: one is dependent on the improvement of enzyme
[...] Read more.
In this review, factors that contribute to enhancing the stability of immobilized enzyme membranes have been indicated, and the solutions to each factor, based on examples, are discussed. The factors are divided into two categories: one is dependent on the improvement of enzyme properties, and the other, on the development of supporting materials. Improvement of an enzyme itself would effectively improve its properties. However, some novel materials or novel preparation methods are required for improving the properties of supporting materials. Examples have been provided principally aimed at improvements in membrane stability. Full article
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
Figures

Figure 1

Journal Contact

MDPI AG
Catalysts Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
E-Mail: 
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to Catalysts Edit a special issue Review for Catalysts
logo
loading...
Back to Top