Special Issue "State of the Art and Future Trends in Nanostructured Biocatalysis"

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

Deadline for manuscript submissions: 15 December 2019.

Special Issue Editor

Guest Editor
Prof. Dr. Peter Grunwald Website E-Mail
Institut für Physikalische Chemie, Grindelallee 117-20146 Hamburg, Germany
Interests: biocatalysis; enzymatic analysis; Environmental biotechnology

Special Issue Information

Dear Colleagues,

According to a definition provided by the Royal Society, as a key technology of the 21st century, nanotechnology refers to the design, characterization, production, and application of structures, devices, and systems by controlling shape and size at the nanometer scale. Applied to biocatalysis, a subarea of enzyme biotechnology, nanobiocatalysis has rapidly developed in the recent past. It combines advances in nanotechnology such as the generation of various nanoscale materials and their physicochemical/optical properties with the excellent characteristics of biocatalysts into an innovative technology.

An important application field is the immobilization of enzymes onto the surface of nanostructured supports (e.g., organic/inorganic (magnetic) NPs, carbon-based nanotubes, mesoporous materials, nanofiber membranes, virus-like particles, etc.) for the sustainable production of goods and chemicals, including biodiesel. In contrast to bulk solid materials, these carriers are characterized by a high surface, resulting in a significantly reduced mass transfer limitation and comparatively high enzyme loading. In addition, they often contribute to a stabilization of the fragile molecules by providing a biocompatible surrounding using immobilization strategies such as “grafting onto” and “grafting from” and other strategies (e.g., the formation of single-enzyme nanoparticles).

Quantum dot (QD)-based photoelectrochemical sensors for analyte detection and the analysis of biospecific interactions, and FRET reporter molecules employed, for example, for the identification of enzyme functions make use of the unique electronic and surface-related properties of these colloidal semiconductive nanoparticles. Enzymatic bioelectrocatalysis with electron transfer between an enzyme and a nano-porous electrode is the principle of many biosensor devices used for analytical purposes, as well as enzymatic biofuel cells that convert chemical energy into electrical power.

Nanobiocatalysis also has an impact in the medical area, in connection with the administration and controlled release of drugs, and finds application in proteomic analysis. Biocomputing nanoplatforms serve as therapeutics and diagnostics. Finally, it is possible to synthesize inorganic nanoparticles that mimic natural enzymes. These artificial enzymes are superior to their natural counterparts in terms of stability and cost efficiency.

Prof. Dr. Peter Grunwald
Guest Editor

Manuscript Submission Information

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Keywords

  • biocatalysis
  • nanostructured materials
  • carbon-based nanoparticles
  • quantum dots
  • nanobiocatalysis
  • immobilization
  • single enzyme nanoparticles
  • bioelectronics
  • biosensors
  • biocomputing
  • therapeutic applications
  • bioconversions

Published Papers (7 papers)

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Research

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Open AccessArticle
Genetically Modified M13 Bacteriophage Nanonets for Enzyme Catalysis and Recovery
Catalysts 2019, 9(9), 723; https://doi.org/10.3390/catal9090723 - 27 Aug 2019
Abstract
Enzyme-based biocatalysis exhibits multiple advantages over inorganic catalysts, including the biocompatibility and the unchallenged specificity of enzymes towards their substrate. The recovery and repeated use of enzymes is essential for any realistic application in biotechnology, but is not easily achieved with current strategies. [...] Read more.
Enzyme-based biocatalysis exhibits multiple advantages over inorganic catalysts, including the biocompatibility and the unchallenged specificity of enzymes towards their substrate. The recovery and repeated use of enzymes is essential for any realistic application in biotechnology, but is not easily achieved with current strategies. For this purpose, enzymes are often immobilized on inorganic scaffolds, which could entail a reduction of the enzymes’ activity. Here, we show that immobilization to a nano-scaled biological scaffold, a nanonetwork of end-to-end cross-linked M13 bacteriophages, ensures high enzymatic activity and at the same time allows for the simple recovery of the enzymes. The bacteriophages have been genetically engineered to express AviTags at their ends, which permit biotinylation and their specific end-to-end self-assembly while allowing space on the major coat protein for enzyme coupling. We demonstrate that the phages form nanonetwork structures and that these so-called nanonets remain highly active even after re-using the nanonets multiple times in a flow-through reactor. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Open AccessArticle
Biomimetic Mineralization of Cytochrome c Improves the Catalytic Efficiency and Confers a Functional Multi-Enzyme Composite
Catalysts 2019, 9(8), 648; https://doi.org/10.3390/catal9080648 - 29 Jul 2019
Abstract
The encapsulated enzyme system by metal-organic frameworks (MOFs) exhibits great potential in biofuel cells, pharmaceuticals, and biocatalysis. However, the catalytic efficiency and the enzymatic activity are severely hampered due to enzyme leaching and deficiency of storage stability. In this study, we immobilized cytochrome [...] Read more.
The encapsulated enzyme system by metal-organic frameworks (MOFs) exhibits great potential in biofuel cells, pharmaceuticals, and biocatalysis. However, the catalytic efficiency and the enzymatic activity are severely hampered due to enzyme leaching and deficiency of storage stability. In this study, we immobilized cytochrome c (Cyt c) into dimethylimidazole-copper (Cu(Im)2) by biomimetic mineralization, and constructed a bioinorganic hybrid material, termed Cyt c@Cu(Im)2. Encapsulated Cyt c in Cu(Im)2 with a nanosheet structure exhibited significantly improved catalytic efficiency, enzymatic activity and kinetic performance. The catalytic efficiency (kcat/Km) for Cyt c@Cu(Im)2 was ~20-fold higher compared to that of free Cyt c. Moreover, the increased activity was not affected by long-term storage. Based on this system, we further constructed a multi-enzyme composite with glucose-oxidase (GOx), termed GOx-Cyt c@Cu(Im)2, which exhibited greatly improved enzymatic activity, stability, and excellent selectivity for the detection of low concentrations of glucose. This strategy may provide new insights into the design of enzymes with high activity and stability, as well as the construction of multi-enzyme systems. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Open AccessArticle
Minimally Invasive Glucose Monitoring Using a Highly Porous Gold Microneedles-Based Biosensor: Characterization and Application in Artificial Interstitial Fluid
Catalysts 2019, 9(7), 580; https://doi.org/10.3390/catal9070580 - 30 Jun 2019
Abstract
In this paper, we present the first highly porous gold (h-PG) microneedles-based second-generation biosensor for minimally invasive monitoring of glucose in artificial interstitial fluid (ISF). A highly porous microneedles-based electrode was prepared by a simple electrochemical self-templating method that involves two steps, gold [...] Read more.
In this paper, we present the first highly porous gold (h-PG) microneedles-based second-generation biosensor for minimally invasive monitoring of glucose in artificial interstitial fluid (ISF). A highly porous microneedles-based electrode was prepared by a simple electrochemical self-templating method that involves two steps, gold electrodeposition and hydrogen bubbling at the electrode, which were realized by applying a potential of −2 V versus a saturated calomel electrode (SCE). The highly porous gold surface of the microneedles was modified by immobilization of 6-(ferrocenyl)hexanethiol (FcSH) as a redox mediator and subsequently by immobilization of a flavin adenine dinucleotide glucose dehydrogenase (FAD-GDH) enzyme using a drop-casting method. The microneedles-based FcSH/FAD-GDH biosensor allows for the detection of glucose in artificial interstitial fluid with an extended linear range (0.1–10 mM), high sensitivity (50.86 µA cm−2 mM−1), stability (20% signal loss after 30 days), selectivity (only ascorbic acid showed a response about 10% of glucose signal), and a short response time (3 s). These properties were favourably compared to other microneedles-based glucose biosensors reported in the literature. Finally, the microneedle-arrays-based second-generation biosensor for glucose detection was tested in artificial interstitial fluid opportunely spiked with different concentrations of glucose (simulating healthy physiological conditions while fasting and after lunch) and by placing the electrode into a simulated chitosan/agarose hydrogel skin model embedded in the artificial ISF (continuous glucose monitoring). The obtained current signals had a lag-time of about 2 min compared to the experiments in solution, but they fit perfectly into the linearity range of the biosensor (0.1–10 mM). These promising results show that the proposed h-PG microneedles-based sensor could be used as a wearable, disposable, user-friendly, and automated diagnostic tool for diabetes patients. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Open AccessArticle
Revealing the Active Site of Gold Nanoparticles for the Peroxidase-Like Activity: The Determination of Surface Accessibility
Catalysts 2019, 9(6), 517; https://doi.org/10.3390/catal9060517 - 11 Jun 2019
Abstract
Despite the fact that the enzyme-like activities of nanozymes (i.e., nanomaterial-based artificial enzymes) are highly associated with their surface properties, little is known about the catalytic active sites. Here, we used the sulfide ion (S2−)-induced inhibition of peroxidase-like activity to explore [...] Read more.
Despite the fact that the enzyme-like activities of nanozymes (i.e., nanomaterial-based artificial enzymes) are highly associated with their surface properties, little is known about the catalytic active sites. Here, we used the sulfide ion (S2−)-induced inhibition of peroxidase-like activity to explore active sites of gold nanoparticles (AuNPs). The inhibition mechanism was based on the interaction with Au(I) to form Au2S, implying that the Au(I) might be the active site of AuNPs for the peroxidase-like activity. X-ray photoelectron spectroscopy (XPS) analysis showed that the content of Au(I) on the surface of AuNPs significantly decreased after the addition of S2−, which might be contributed to the more covalent Au–S bond in the formation of Au2S. Importantly, the variations of Au(I) with and without the addition of S2− for different surface-capped AuNPs were in good accordance with their corresponding peroxidase-like activities. These results confirmed that the accessible Au(I) on the surface was the main requisite for the peroxidase-like activity of AuNPs for the first time. In addition, the use of S2− could assist to determine available active sites for different surface modified AuNPs. This work not only provides a new method to evaluate the surface accessibility of colloidal AuNPs but also gains insight on the design of efficient AuNP-based peroxidase mimics. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Open AccessArticle
Suitability of Recombinant Lipase Immobilised on Functionalised Magnetic Nanoparticles for Fish Oil Hydrolysis
Catalysts 2019, 9(5), 420; https://doi.org/10.3390/catal9050420 - 03 May 2019
Abstract
Recombinant Bacillus subtilis lipase was immobilised on magnetic nanoparticles by a facile covalent method and applied to fish oil hydrolysis. High loading of enzyme to the functionalised nanoparticle was achieved with a protein binding efficiency of 95%. Structural changes of the confined enzyme [...] Read more.
Recombinant Bacillus subtilis lipase was immobilised on magnetic nanoparticles by a facile covalent method and applied to fish oil hydrolysis. High loading of enzyme to the functionalised nanoparticle was achieved with a protein binding efficiency of 95%. Structural changes of the confined enzyme on the surface of the nanoparticles was investigated using transmission electron microscopy and spectroscopic techniques (attenuated total reflectance-Fourier transform infrared and circular dichroism). The biocatalytic potential of immobilised lipase was compared with that of free enzyme and biochemically characterised with respect to different parameters such as pH, temperature, substrate concentrations and substrate specificity. The thermal stability of functionalised nanoparticle bound enzyme was doubled that of free enzyme. Immobilised lipase retained more than 50% of its initial biocatalytic activity after recyclability for twenty cycles. The ability to the immobilised thermostable lipase to concentrate omega-3 fatty acids from fish oil was investigated. Using synthetic substrate, the immobilised enzyme showed 1.5 times higher selectivity for docosahexaenoic acid (DHA), and retained the same degree of selectivity for eicosapentaenoic acid (EPA), when compared to the free enzyme. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Open AccessArticle
Synthesis and Characterization of Te Nanotubes Decorated with Pt Nanoparticles for a Fuel Cell Anode/Cathode Working at a Neutral pH
Catalysts 2019, 9(4), 328; https://doi.org/10.3390/catal9040328 - 03 Apr 2019
Abstract
In fuel-cell technology development, one of the most important objectives is to minimize the amount of Pt, the most employed material as an oxygen reduction and methanol oxidation electro-catalyst. In this paper, we report the synthesis and characterization of Te nanotubes (TeNTs) decorated [...] Read more.
In fuel-cell technology development, one of the most important objectives is to minimize the amount of Pt, the most employed material as an oxygen reduction and methanol oxidation electro-catalyst. In this paper, we report the synthesis and characterization of Te nanotubes (TeNTs) decorated with Pt nanoparticles, readily prepared from stirred aqueous solutions of PtCl2 containing a suspension of TeNTs, and ethanol acting as a reducing agent, avoiding the use of any hydrophobic surfactants such as capping stabilizing substance. The obtained TeNTs decorated with Pt nanoparticles (TeNTs/PtNPs) have been fully characterized by X-ray diffraction (XRD), transmission electron microscopy (TEM), selected area diffraction patterns (SAD), X-ray photoelectron spectroscopy (XPS), and cyclic voltammetry (CV). We demonstrated that the new material can be successfully employed in fuel cells, either as an anodic (for methanol oxidation reaction) or a cathodic (for oxygen reduction reaction) electrode, with high efficiency in terms of related mass activities and on-set improvement. Remarkably, the cell operates in aqueous electrolyte buffered at pH 7.0, thus, avoiding acidic or alkaline conditions that might lead to, for example, Pt dissolution (at low pH), and paving the way for the development of biocompatible devices and on-chip fuel cells. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Review

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Open AccessReview
Cerium- and Iron-Oxide-Based Nanozymes in Tissue Engineering and Regenerative Medicine
Catalysts 2019, 9(8), 691; https://doi.org/10.3390/catal9080691 - 15 Aug 2019
Abstract
Nanoparticulate materials displaying enzyme-like properties, so-called nanozymes, are explored as substitutes for natural enzymes in several industrial, energy-related, and biomedical applications. Outstanding high stability, enhanced catalytic activities, low cost, and availability at industrial scale are some of the fascinating features of nanozymes. Furthermore, [...] Read more.
Nanoparticulate materials displaying enzyme-like properties, so-called nanozymes, are explored as substitutes for natural enzymes in several industrial, energy-related, and biomedical applications. Outstanding high stability, enhanced catalytic activities, low cost, and availability at industrial scale are some of the fascinating features of nanozymes. Furthermore, nanozymes can also be equipped with the unique attributes of nanomaterials such as magnetic or optical properties. Due to the impressive development of nanozymes during the last decade, their potential in the context of tissue engineering and regenerative medicine also started to be explored. To highlight the progress, in this review, we discuss the two most representative nanozymes, namely, cerium- and iron-oxide nanomaterials, since they are the most widely studied. Special focus is placed on their applications ranging from cardioprotection to therapeutic angiogenesis, bone tissue engineering, and wound healing. Finally, current challenges and future directions are discussed. Full article
(This article belongs to the Special Issue State of the Art and Future Trends in Nanostructured Biocatalysis)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Synthesis and Characterization of Te Nanotubes Decorated with Pt Nanoparticles for Fuel Cell Anode/Cathode Working at Neutral pH
Author:
Maria Rachele Guascito *, Daniela Chirizzi, Emanuela Filippo, Francesco Milano and Antonio Tepore
Affiliation:
Dipartimento di Scienze e Tecnologie Biologiche e Ambientali, Università del Salento, 73100 Lecce, Italy
Correspondence:
[email protected]

Title: Recent Advances in Enzyme-nanostructured Biocatalysts with Enhanced Activity
Authors:
Galong Li * and Haiming Fan
Affiliation:
College of Chemistry and Materials ScienceNorthwest University, Xi’an, China
Correspondence:
[email protected]

Title: Nanostructued Enzyme Aggregates as Molecular Machine for Concerted Biocatalytic Reactions
Authors: An-Ping Zeng * and Uwe Jandt
Affiliation: Institute of Bioprocess and Biosystems Engineering, Hamburg University of Technology, Hamburg, Germany
Correspondence: [email protected]

Title: Nanoparticle Enzyme Mimics and Prebiotic Synthesis
Author:
Wolfgang Tremel
Affiliation:
Johannes Gutenberg-Universität, Institut für Anorganische Chemie und Analytische Chemie, Duesbergweg 10-14, D-55099 Mainz, Germany
Correspondence:
[email protected]
Abstract: Metabolism is a feature of life and crucial for molecular and cellular function. A key question concerning the origin of life is how molecular machineries could have functioned in the absence of enzymatic and genetic networks. Prebiotic chemistry is likely to involve catalytic transformations of small inorganic and organic molecules into more complex and biologically functional molecules. In today´s organisms, enzymes are the dominant catalysts, but enzymes are unlikely to have formed spontaneously on earth. Thus, the very first forms of life must have managed with other, available catalysts. Life in its present form depends on metal ions. Approximately one-third of all known enzymes are metalloenzymes, which are involved in electron transfer reactions (e.g. cytochromes) or act as storage or transport proteins. This strong dependence on metals probably reflects the early environment from which cellular life originated, when biopolymers were not present on prebiotic earth. Chemical reactions leading to the first cells must have made use of other catalysts that were superseded by today´s systems at a later stage. We discuss the potential role of nanoparticle enzyme mimics to address two important questions: (1) How did life begin through the evolutionary transition from geochemical to biochemical processes and (2) is it possible to realize a similar transition de novo in the laboratory?

Title: Development of a Four-enzyme Magnetic Nanobiocatalyst for Cellulose Hydrolysis
Author:
Haris Stamatis
Affiliation:
Laboratory of Biotechnology,Department of Biological Applications & Technologies,University of Ioannina,45110 Ioannina, Greece
Correspondence:
[email protected]

Title: Nanozymes for Tissue Engineering Applications
Author: Leticia Hosta-Rigau
Affiliation: Technical University of Denmark, Department of Health Technology, Produktionstorvet Building 423, Room 010,2800 Kgs. Lyngby, Denmark
Correspondence: [email protected]

Title: Selectivity and Sustainability of Electroenzymatic Process for Glucose Conversion to Gluconic Acid
Authors:
Varnicic M. a, Zasheva N.I. b, Haak E. c, Sundmacher K. a,b and Vidakovic-Koch T. a,*
Affiliation: a Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstr. 1, 39106 Magdeburg, Germany; b Otto-von-Guericke-University Magdeburg, Chair for Process Systems Engineering, Universitätsplatz 2, 39106 Magdeburg, Germany; c Otto-von-Guericke- University Magdeburg, Institut für Chemie, 39106 Magdeburg, Germany
Correspondence:
[email protected]
Abstract:
Electroenzymatic processes are interesting solutions for the development of new processes based on renewable feedstocks, renewable energies and green catalysts. High-selectivity and sustainability of these processes are usually assumed. In this contribution, these two aspects were studied in more details. In a membrane-less electroenzymatic reactor 97% product selectivity at 80% glucose conversion to gluconic acid was determined. With the help of nuclear magnetic resonance spectroscopy, two main side products were identified. The yields of D-arabinose and formic acid can be controlled by the flow rate and the electroenzymatic reactor mode of operation (fuel cell or ion-pumping). The possible pathways for the side product formation have been discussed. The electroenzymatic cathode was found to be responsible for a decrease in selectivity. The choice of the enzymatic catalyst on the cathode side led to 100% selectivity of gluconic acid at somewhat reduced conversion. Furthermore, sustainability of the electroenzymatic process is estimated based on several sustainability indicators. Although some indicators (like Space Time Yield) are favorable for electroenzymatic process, the E-factor of electroenzymatic process has to improve significantly in order to compete with the fermentation process. This can be achieved by an increase of a cycle time and/or enzyme utilization which is currently low.

Title: Progress and Trend on the Regulation Methods for Nanozyme Activity and Selectivity
Author:
Tianran Lin
Affiliation: State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, College of Chemistry and Pharmaceutical Science of Guangxi Normal University, Guilin 541004, China
Correspondence:
[email protected]

Title:
Hybrid Enzyme-nanostructure Biocatalysts Containing Wired Oxidoreductases: A Review
Author: Dalius Ratautas
Affiliation: Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Saulėtekio al. 11, LT-10223 Vilnius, Lithuania
Correspondence: [email protected]

Title:
Thymine-Hg2+ Thymine Coordination Chemistry Induced Entropy Driven Catalytic Reaction to Form Hemin/G-quadruplex-HRP-mimicking DNAzyme for Colorimetric and Visual Determination of Hg2+
Author: Wen Yun
Correspondence: [email protected]

Title:
Direct Electron Transfer-type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes (Tentative)
Author: Taiki Adachi, Yuki Kitazumi, Osamu Shirai, and Kenji Kano*
Affiliation: Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan
Abstract: Direct electron transfer (DET)-type bioelectrocatalysis, which couples the electrode reaction and the catalytic function of the redox enzyme without mediators, is one of the most intriguing subjects studied over the past decades. In order to realize the DET-type bioelectrocatalysis and to improve the performance, the nanostructure of the electrode surface has to be carefully tuned for the enzyme. In addition, the enzyme can also be tuned by protein engineering approach for the DET-type reaction. This review summarizes the resent progresses in this field of the research, while taking into consideration of the importance of nanostructure of electrodes as well as redox enzymes.
Correspondence: [email protected]

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