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Catalysts
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Recent Advances in Biocatalysis and Metabolic Engineering
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Recent Advances in Biocatalysis and Metabolic Engineering

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 36476

Special Issue Editors

Prof. Dr. Yung-Chuan Liu

E-Mail Website
Guest Editor
Department of Chemical Engineering, National Chung Hsing University, Taichung 402, Taiwan
Interests: fermentation technology; protein engineering; immunoassay; membrane technology; molecular engineering
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Si-Yu Li

E-Mail Website
Guest Editor
Department of Chemical Engineering, National Chung Hsing University, 145, Hsing-Da Rd., Taichung 40227, Taiwan
Interests: metabolic engineering; microbial fermentation; biochemicals production; biofuels production; bioresources engineering
Special Issues, Collections and Topics in MDPI journals
Dr. Nien-Jen Hu

E-Mail Website
Guest Editor
Graduate Institute of Biochemistry, National Chung Hsing University, Taichung, Taiwan
Interests: protein engineering; structural biology of enzymes; functional peptides; lipases; cell signalling; membrane biology

Special Issue Information

Dear Colleagues,

Biocatalysts (enzymes) are proteins possessing catalytic functions capable of high enantioselective and high yield under mild reaction conditions. The wide applications of enzymes can be found in the fields of pharmaceutics, food, cosmetics, detergents, and biofuel. The subjects concerning enzyme production cover strain screening, recombinant strain construction, fermentation, enzyme separation and purification, enzyme extraction, biotransformation, enzyme immobilization, and enzyme bioreactors. Enzyme process development also includes enzyme kinetic analysis, enzyme process design, and optimization.

In addition to enzyme production and process development, this Special Issue also aims to include recent progress in the subjects concerning synthetic biology and metabolic engineering. Synthetic biology is a multidisciplinary research filed aiming to redesign and fabricate novel biological products, components, and systems that do not exist in nature for practical applications. Synthetic biologists usually exploit top–down and bottom–up approaches, the former of which involves genetic engineering to introduce novel function in the living cells, and the latter of which assembles the various biological components to construct an artificial biosystem. In the past two decades, with the abundance of genetic information and the availability of chemically synthetic DNA, researchers and industries have created organisms with modified genomes for the production of biofuels, renewable chemicals, secondary metabolites, and pharmaceutical intermediates. This rapidly-growing topic is of tremendous economic potential and has drawn the worldwide attention of the biotech industry. On the other hand, metabolic engineering is one of the promising fields that have been applied in biofuels, biomaterials, and CO2 fixation. Metabolic engineering involves DNA techniques, enzyme catalysis, cellular regulation and cellular energy balance. Metabolic engineering regarding other different applications are also involved. Therefore, both original research and review articles covering the subject of advanced biocatalyst process, synthetic biology, and metabolic engineering are welcome for inclusion in the Special Issue.

Prof. Dr. Yung-Chuan Liu
Prof. Dr. Si-Yu Li
Assist. Prof. Dr. Nien-Jen Hu
Guest Editors

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 submissions that pass pre-check are 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 2700 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

  • Enzyme
  • Biocatalyst
  • Enzyme process design
  • Enzyme kinetics
  • Enzyme purification
  • Enzyme immobilization
  • Biotransformation
  • Applied protein engineering
  • Designed nucleotide system
  • Bioremediation
  • Biosensors
  • Natural product synthesis
  • Biofuels
  • Biomaterials
  • CO2 fixation
  • Metabolic engineering

Published Papers (13 papers)

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Editorial

Jump to: Research, Review

5 pages, 202 KiB  
Editorial
Recent Advances in Biocatalysis and Metabolic Engineering
by Nien-Jen Hu, Si-Yu Li and Yung-Chuan Liu
Catalysts 2021, 11(9), 1052; https://doi.org/10.3390/catal11091052 - 30 Aug 2021
Cited by 2 | Viewed by 2035
Abstract
Biocatalysis refers to the utilization of enzymes, either in purified form, or existed as part of crude cell lysate or intact cells, to catalyze single- or multi-step chemical reactions, converting synthetic molecules or natural metabolites into high-value products [...] Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)

Research

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12 pages, 3315 KiB  
Article
One-Pot Bi-Enzymatic Cascade Synthesis of Novel Ganoderma Triterpenoid Saponins
by Te-Sheng Chang, Chien-Min Chiang, Tzi-Yuan Wang, Yu-Li Tsai, Yu-Wei Wu, Huei-Ju Ting and Jiumn-Yih Wu
Catalysts 2021, 11(5), 580; https://doi.org/10.3390/catal11050580 - 30 Apr 2021
Cited by 5 | Viewed by 2226
Abstract
Ganoderma lucidum is a medicinal fungus whose numerous triterpenoids are its main bioactive constituents. Although hundreds of Ganoderma triterpenoids have been identified, Ganoderma triterpenoid glycosides, also named triterpenoid saponins, have been rarely found. Ganoderic acid A (GAA), a major Ganoderma triterpenoid, was synthetically [...] Read more.
Ganoderma lucidum is a medicinal fungus whose numerous triterpenoids are its main bioactive constituents. Although hundreds of Ganoderma triterpenoids have been identified, Ganoderma triterpenoid glycosides, also named triterpenoid saponins, have been rarely found. Ganoderic acid A (GAA), a major Ganoderma triterpenoid, was synthetically cascaded to form GAA-15-O-β-glucopyranoside (GAA-15-G) by glycosyltransferase (BtGT_16345) from Bacillus thuringiensis GA A07 and subsequently biotransformed into a series of GAA glucosides by cyclodextrin glucanotransferase (Toruzyme® 3.0 L) from Thermoanaerobacter sp. The optimal reaction conditions for the second-step biotransformation of GAA-15-G were found to be 20% of maltose; pH 5; 60 °C. A series of GAA glucosides (GAA-G2, GAA-G3, and GAA-G4) could be purified with preparative high-performance liquid chromatography (HPLC) and identified by mass and nucleic magnetic resonance (NMR) spectral analysis. The major product, GAA-15-O-[α-glucopyranosyl-(1→4)-β-glucopyranoside] (GAA-G2), showed over 4554-fold higher aqueous solubility than GAA. The present study demonstrated that multiple Ganoderma triterpenoid saponins could be produced by sequential actions of BtGT_16345 and Toruzyme®, and the synthetic strategy that we proposed might be applied to many other Ganoderma triterpenoids to produce numerous novel Ganoderma triterpenoid saponins in the future. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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9 pages, 1397 KiB  
Article
Fed-Batch Cultivation and Adding Supplements to Increase Yield of β-1,3-1,4-Glucanase by Genetically Engineered Escherichia coli
by Lijuan Zhong, Zheng Liu and Yinghua Lu
Catalysts 2021, 11(2), 269; https://doi.org/10.3390/catal11020269 - 18 Feb 2021
Cited by 1 | Viewed by 2130
Abstract
The aim of this study was to analyze the major influence factors of culture medium on the expression level of β-1,3-1,4-glucanase, and to further develop an optimized process for the extracellular production of β-glucanase at a bioreactor scale (7 L) with a genetically [...] Read more.
The aim of this study was to analyze the major influence factors of culture medium on the expression level of β-1,3-1,4-glucanase, and to further develop an optimized process for the extracellular production of β-glucanase at a bioreactor scale (7 L) with a genetically engineered Escherichia coli (E. coli) JM109-pLF3. In this study, batch cultivation and fed-batch cultivation including the constant rate feeding strategy and the DO-stat (DO: Dissolved Oxygen) feeding strategy were conducted. At a 7 L bioreactor scale for batch cultivation, biomass reached 3.14 g/L and the maximum β-glucanase activity was 506.94 U/mL. Compared with batch cultivation, the addition of glycerol, complex nitrogen and complete medium during fed-batch cultivation increased the production of biomass and β-1,3-1,4-glucanase. The maximum biomass and β-glucanase activity, which were 7.67 g/L and 1680 U/mL, respectively, that is, 2.45 and 3.31 times higher than those obtained with batch cultivation, were obtained by feeding a complex nitrogen source at a constant rate of 1.11 mL/min. Therefore, these nutritional supplements and strategies can be used as a reference to enhance the production of other bioproducts from E. coli. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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9 pages, 1728 KiB  
Article
Regioselective Hydroxylation of Oleanolic Acid Catalyzed by Human CYP3A4 to Produce Hederagenenin, a Chiral Metabolite
by Ngoc Tan Cao, Ngoc Anh Nguyen, Thien-Kim Le, Gun Su Cha, Ki Deok Park and Chul-Ho Yun
Catalysts 2021, 11(2), 267; https://doi.org/10.3390/catal11020267 - 17 Feb 2021
Cited by 3 | Viewed by 2187
Abstract
Oleanolic acid (OA) is a pentacyclic triterpenoid widely found in plants and foods as an aglycone of triterpenoid saponins or as a free acid. OA exhibits beneficial activities for humans, including antitumor, antivirus, and hepatoprotection properties without apparent toxicity. The metabolites produced by [...] Read more.
Oleanolic acid (OA) is a pentacyclic triterpenoid widely found in plants and foods as an aglycone of triterpenoid saponins or as a free acid. OA exhibits beneficial activities for humans, including antitumor, antivirus, and hepatoprotection properties without apparent toxicity. The metabolites produced by the cytochrome P450 (P450) enzymes are critical for the evaluation of the efficacy and safety of drugs. In this study, the potential metabolites of OA were investigated by P450-catalyzed oxidation reactions. Among the various tested human P450s, only human CYP3A4 was active for the hydroxylation of OA. The major metabolite was characterized by a set of analyses using HPLC, LC–MS, and NMR. It was found to be 4-epi-hederagenenin, a chiral product, by regioselective hydroxylation of the methyl group at the C-23 position. These results indicated that CYP3A4 can hydroxylate an OA substrate to make 4-epi-hederagenenin. Possible drug–food interactions are discussed. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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17 pages, 4033 KiB  
Article
Magnetic Cross-Linked Enzyme Aggregates of a Transpeptidase-Specialized Variant (N450D) of Bacillus licheniformis γ-Glutamyl Transpeptidase: An Efficient and Stable Biocatalyst for l-Theanine Synthesis
by Meng-Chun Chi, Yu-Fen Huang, Bo-Yuan Lu, Min-Guan Lin, Tzu-Fan Wang and Long-Liu Lin
Catalysts 2021, 11(2), 243; https://doi.org/10.3390/catal11020243 - 12 Feb 2021
Cited by 10 | Viewed by 2746
Abstract
γ-Glutamyl transpeptidase (GGT) catalyzes the transfer of glutathione’s γ-glutamyl group and related γ-glutamyl amides to water, amino acids or peptides, and utilizes a conserved Thr residue to process its own polypeptide chain into a large and a small subunit that then assemble to [...] Read more.
γ-Glutamyl transpeptidase (GGT) catalyzes the transfer of glutathione’s γ-glutamyl group and related γ-glutamyl amides to water, amino acids or peptides, and utilizes a conserved Thr residue to process its own polypeptide chain into a large and a small subunit that then assemble to produce a catalytically competent enzyme. In this study, the magnetic cross-linked enzyme aggregates (mCLEAs) of a transpeptidase-specialized variant (N450D) of Bacillus licheniformis GGT were successfully prepared with optimized process parameters viz.1.25:1 (v/v) of isopropanol to N450D (0.3 mg/mL) ratio/0.02:1 (w/w) of enzyme to 3-aminopropyl triethoxysilane (APTES)-coated magnetic nanoparticle ratio/20 mM of glutaraldehyde. The prepared magnetic nanoparticles and immobilized enzyme (N450D-mCLEAs) were characterized by X-ray diffraction (XRD) and Fourier transform infrared (FTIR) spectroscopy, field-emission scanning electron microscope integrated with energy dispersive X-ray spectroscopy (FESEM/EDS), and superparamagnetic analysis. As compared with free enzyme, N450D-mCLEAs displayed significantly higher heat resistance at temperatures of 55 and 60 °C, and had a greater stability over a storage period of one month. The immobilized enzyme could also be reused for 10 consecutive biocatalytic cycles with no significant reduction in the percent yield of l-theanine. Conclusively, this immobilization strategy surely provides a meaningful glance of developing N450D-mediated biocatalysis for the production of physiologically important γ-glutamyl compounds. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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15 pages, 3382 KiB  
Article
Electrocatalytic Oxidation of Glucose on Boron and Nitrogen Codoped Graphene Quantum Dot Electrodes in Alkali Media
by Siyong Gu, Chien-Te Hsieh, Chih-Peng Kao, Chun-Chieh Fu, Yasser Ashraf Gandomi, Ruey-Shin Juang and Kenneth David Kihm
Catalysts 2021, 11(1), 101; https://doi.org/10.3390/catal11010101 - 13 Jan 2021
Cited by 16 | Viewed by 2944
Abstract
A novel solvothermal technique has been developed in the presence of C/N/B precursor for synthesizing B-N-coped graphene quantum dots (GQDs) as non-metal electrocatalysts towards the catalytic glucose oxidation reaction (GOR). Both N-doped GQD and B-N-codoped GQD particles (~4.0 nm) possess a similar oxidation [...] Read more.
A novel solvothermal technique has been developed in the presence of C/N/B precursor for synthesizing B-N-coped graphene quantum dots (GQDs) as non-metal electrocatalysts towards the catalytic glucose oxidation reaction (GOR). Both N-doped GQD and B-N-codoped GQD particles (~4.0 nm) possess a similar oxidation and amidation level. The B-N-codoped GQD contains a B/C ratio of 3.16 at.%, where the B dopants were formed through different bonding types (i.e., N‒B, C‒B, BC2O, and BCO2) inserted into or decorated on the GQDs. The cyclic voltammetry measurement revealed that the catalytic activity of B-N-codoped GQD catalyst is significantly higher compared to the N-doped GQDs (~20% increase). It was also shown that the GOR activity was substantially enhanced due to the synergistic effect of B and N dopants within the GQD catalysts. Based on the analysis of Tafel plots, the B-N-codoped-GQD catalyst electrode displays an ultra-high exchange current density along with a reduced Tafel slope. The application of B-N-codoped GQD electrodes significantly enhances the catalytic activity and results in facile reaction kinetics towards the glucose oxidation reaction. Accordingly, the novel design of GQD catalyst demonstrated in this work sets the stage for designing inexpensive GQD-based catalysts as an alternative for precious metal catalysts commonly used in bio-sensors, fuel cells, and other electrochemical devices. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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17 pages, 2624 KiB  
Article
Co-Immobilization of Xylanase and Scaffolding Protein onto an Immobilized Metal Ion Affinity Membrane
by Ho-Lam Wong, Nien-Jen Hu, Tzong-Yuan Juang and Yung-Chuan Liu
Catalysts 2020, 10(12), 1408; https://doi.org/10.3390/catal10121408 - 02 Dec 2020
Cited by 12 | Viewed by 2289
Abstract
Lignocellulosic biomass conversion technology seeks to convert agricultural waste to sugars through the use of various cellulases and hemicellulases. In practice, the application of free enzymes might increase the cost of the process due to difficulties with recovery of the enzymes and products. [...] Read more.
Lignocellulosic biomass conversion technology seeks to convert agricultural waste to sugars through the use of various cellulases and hemicellulases. In practice, the application of free enzymes might increase the cost of the process due to difficulties with recovery of the enzymes and products. Immobilization might be an effective approach for recovering the hydrolysis products and improving the stability and reusability of the enzymes. In this study, we used a recombinant genetic engineering approach to construct a scaffold protein gene (CipA) and a xylanase gene (XynC) fused to a dockerin gene (DocT). After expressing CipA and XynC-DocT (XynCt) genes using E. coli hosts, the crude extracts were collected. An immobilized metal ion affinity membrane/Co2+ ion (IMAM-Co2+) system was prepared to adsorb CipA in its crude extract, thereby allowing simultaneous purification and immobilization of CipA protein. A similar approach was applied for the adsorption of XynCt protein, exploiting the interaction between the cohesin units in IMAM-Co2+-CipA and the dockerin unit in XynCt. The activity of the xylanase unit was enhanced in the presence of Co2+ for both the free XynCt enzymes and the immobilized CipA-XynCt. The heat resistance and stability over a wide range of values of pH of the immobilized CipA-XynCt were superior to those of the free XynCt. Furthermore, the immobilized CipA-XynCt retained approximately 80% of its initial activity after seven reaction cycles. The values of Km and νmax of IMAM-Co2+-CipA-XynCt (1.513 mg/mL and 3.831 U/mg, respectively) were the best among those of the other tested forms of XynCt. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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15 pages, 1666 KiB  
Article
Tryptophan Fluorescence and Time-Lag Hydrolysis of Peptide Bonds during Degradation of β-Lactoglobulin by Trypsin
by Mikhail M. Vorob’ev
Catalysts 2020, 10(12), 1368; https://doi.org/10.3390/catal10121368 - 24 Nov 2020
Cited by 5 | Viewed by 2190
Abstract
The opening of protein globules and corresponding exposure of their internal peptide bonds, the so-called demasking effect, is required for successful hydrolysis of peptide bonds by proteases. Under the proteolytic action of trypsin on β-lactoglobulin (β-LG), the evolution of tryptophan fluorescence spectra showed [...] Read more.
The opening of protein globules and corresponding exposure of their internal peptide bonds, the so-called demasking effect, is required for successful hydrolysis of peptide bonds by proteases. Under the proteolytic action of trypsin on β-lactoglobulin (β-LG), the evolution of tryptophan fluorescence spectra showed that the demasking process consists of two stages with different demasking rate constants for each stage. It was found that the ratio of these constants depends on the concentration of trypsin and changes are approximately threefold when the concentration of trypsin changes in the range of 0.3–15 mg/L. Simulation of hydrolysis taking into account the demasking effect demonstrated how the apparent first-order rate constants obtained experimentally are related to the true hydrolysis rate constants and demasking parameters. The lag phase in the kinetic curves corresponding to the hydrolysis of various peptide bonds in β-LG was also analyzed. The increased lag times indicated sites that are hydrolyzed by a two-stage demasking mechanism. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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19 pages, 2299 KiB  
Article
A Bioorthogonally Synthesized and Disulfide-Containing Fluorescence Turn-On Chemical Probe for Measurements of Butyrylcholinesterase Activity and Inhibition in the Presence of Physiological Glutathione
by Ming-Mao Gong, Chia-Yen Dai, Scott Severance, Chi-Ching Hwang, Bo-Kai Fang, Heng-Bo Lin, Chien-Hui Huang, Chi-Wi Ong, Jeh-Jeng Wang, Pei-Lun Lee and Tzu-Pin Wang
Catalysts 2020, 10(10), 1169; https://doi.org/10.3390/catal10101169 - 12 Oct 2020
Cited by 5 | Viewed by 2627
Abstract
Butyrylcholinesterase (BChE) is a biomarker in human blood. Aberrant BChE activity has been associated with human diseases. Here we developed a fluorescence resonance energy transfer (FRET) chemical probe to specifically quantify BChE activity in serum, while simultaneously discriminating against glutathione (GSH). The FRET [...] Read more.
Butyrylcholinesterase (BChE) is a biomarker in human blood. Aberrant BChE activity has been associated with human diseases. Here we developed a fluorescence resonance energy transfer (FRET) chemical probe to specifically quantify BChE activity in serum, while simultaneously discriminating against glutathione (GSH). The FRET chemical probe 11 was synthesized from a key trifunctional bicyclononyne exo-6 and derivatives of 5-(2-aminoethylamino)-1-naphthalenesulfonic acid (EDANS) and 4-[4-(dimethylamino)phenylazo]benzoic acid (DABCYL). EDANS fluorescence visualization and kinetic analysis of 11 in the presence of diverse compounds confirmed the outstanding reactivity and specificity of 11 with thiols. The thiol-dependent fluorescence turn-on property of 11 was attributed to a general base-catalyzed SN2 nucleophilic substitution mechanism and independent of metal ions. Moreover, all thiols, except GSH, reacted swiftly with 11. Kinetic studies of 11 in the presence of covalently modified GSH derivatives corroborated that the steric hindrance of 11 imposing on GSH was the likely cause of the distinguished reactivity. Since GSH commonly interferes in assays measuring BChE activity in blood samples, the 11-based fluorescent assay was employed to directly quantify BChE activity without GSH interference, and delivered a linear range of 4.3–182.2 U L−1 for BChE activity with detection limit of 4.3 U L−1, and accurately quantified serum BChE activity in the presence of 10 μM GSH. Finally, the 11-based assay was exploited to determine Ki of 5 nM for tacrine inhibition on BChE catalysis. We are harnessing the modulated characteristics of 6 to synthesize advanced chemical probes able to more sensitively screen for BChE inhibitors and quantify BChE activity in serum. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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Review

Jump to: Editorial, Research

20 pages, 2239 KiB  
Review
Contemporary Enzyme-Based Methods for Recombinant Proteins In Vitro Phosphorylation
by Marcela Slovakova and Zuzana Bilkova
Catalysts 2021, 11(8), 1007; https://doi.org/10.3390/catal11081007 - 20 Aug 2021
Cited by 6 | Viewed by 2905
Abstract
Phosphorylation is a reversible, enzyme-controlled posttranslational process affecting approximately one-third of all proteins in eukaryotic cells at any given time. Any deviation in the degree and/or site of phosphorylation leads to an abnormal conformation of proteins, resulting in a decline or loss of [...] Read more.
Phosphorylation is a reversible, enzyme-controlled posttranslational process affecting approximately one-third of all proteins in eukaryotic cells at any given time. Any deviation in the degree and/or site of phosphorylation leads to an abnormal conformation of proteins, resulting in a decline or loss of their function. Knowledge of phosphorylation-related pathways is essential for understanding the understanding of the disease pathogenesis and for the design of new therapeutic strategies. Recent availability of various kinases at an affordable price differs in activity, specificity, and stability and provides the opportunity of studying and modulating this reaction in vitro. We can exploit this knowledge for other applications. There is an enormous potential to produce fully decorated and active recombinant proteins, either for biomedical or cosmetic applications. Closely related is the possibility to exploit current achievements and develop new safe and efficacious vaccines, drugs, and immunomodulators. In this review, we outlined the current enzyme-based possibilities for in vitro phosphorylation of peptides and recombinant proteins and the added value that immobilized kinases provide. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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20 pages, 3215 KiB  
Review
Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials
by M. Asunción Molina, Victoria Gascón-Pérez, Manuel Sánchez-Sánchez and Rosa M. Blanco
Catalysts 2021, 11(8), 1002; https://doi.org/10.3390/catal11081002 - 20 Aug 2021
Cited by 20 | Viewed by 4273
Abstract
The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific [...] Read more.
The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific community to develop very different strategies for the immobilization of enzymes in/on MOFs. This review focuses on one of these strategies, namely, the one-pot enzyme immobilization within sustainable MOFs, which is particularly enticing as the resultant biocomposite Enzyme@MOFs have the potential to be: (i) prepared in situ, that is, in just one step; (ii) may be synthesized under sustainable conditions: with water as the sole solvent at room temperature with moderate pHs, etc.; (iii) are able to retain high enzyme loading; (iv) have negligible protein leaching; and (v) give enzymatic activities approaching that given by the corresponding free enzymes. Moreover, this methodology seems to be near-universal, as success has been achieved with different MOFs, with different enzymes and for different applications. So far, the metal ions forming the MOF materials have been chosen according to their low price, low toxicity and, of course, their possibility for generating MOFs at room temperature in water, in order to close the cycle of economic, environmental and energy sustainability in the synthesis, application and disposal life cycle. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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25 pages, 5012 KiB  
Review
Clostridium thermocellum as a Promising Source of Genetic Material for Designer Cellulosomes: An Overview
by Dung Minh Ha-Tran, Trinh Thi My Nguyen and Chieh-Chen Huang
Catalysts 2021, 11(8), 996; https://doi.org/10.3390/catal11080996 - 19 Aug 2021
Cited by 5 | Viewed by 2828
Abstract
Plant biomass-based biofuels have gradually substituted for conventional energy sources thanks to their obvious advantages, such as renewability, huge quantity, wide availability, economic feasibility, and sustainability. However, to make use of the large amount of carbon sources stored in the plant cell wall, [...] Read more.
Plant biomass-based biofuels have gradually substituted for conventional energy sources thanks to their obvious advantages, such as renewability, huge quantity, wide availability, economic feasibility, and sustainability. However, to make use of the large amount of carbon sources stored in the plant cell wall, robust cellulolytic microorganisms are highly demanded to efficiently disintegrate the recalcitrant intertwined cellulose fibers to release fermentable sugars for microbial conversion. The Gram-positive, thermophilic, cellulolytic bacterium Clostridium thermocellum possesses a cellulolytic multienzyme complex termed the cellulosome, which has been widely considered to be nature’s finest cellulolytic machinery, fascinating scientists as an auspicious source of saccharolytic enzymes for biomass-based biofuel production. Owing to the supra-modular characteristics of the C. thermocellum cellulosome architecture, the cellulosomal components, including cohesin, dockerin, scaffoldin protein, and the plentiful cellulolytic and hemicellulolytic enzymes have been widely used for constructing artificial cellulosomes for basic studies and industrial applications. In addition, as the well-known microbial workhorses are naïve to biomass deconstruction, several research groups have sought to transform them from non-cellulolytic microbes into consolidated bioprocessing-enabling microbes. This review aims to update and discuss the current progress in these mentioned issues, point out their limitations, and suggest some future directions. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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20 pages, 2715 KiB  
Review
Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity
by Lingxia Xu, Jianzhong Sun, Majjid A. Qaria, Lu Gao and Daochen Zhu
Catalysts 2021, 11(8), 955; https://doi.org/10.3390/catal11080955 - 10 Aug 2021
Cited by 24 | Viewed by 3990
Abstract
Dye decoloring peroxidases (DyPs) were named after their high efficiency to decolorize and degrade a wide range of dyes. DyPs are a type of heme peroxidase and are quite different from known heme peroxidases in terms of amino acid sequences, protein structure, catalytic [...] Read more.
Dye decoloring peroxidases (DyPs) were named after their high efficiency to decolorize and degrade a wide range of dyes. DyPs are a type of heme peroxidase and are quite different from known heme peroxidases in terms of amino acid sequences, protein structure, catalytic residues, and physical and chemical properties. DyPs oxidize polycyclic dyes and phenolic compounds. Thus they find high application potentials in dealing with environmental problems. The structure and catalytic characteristics of DyPs of different families from the amino acid sequence, protein structure, and enzymatic properties, and analyzes the high-efficiency degradation ability of some DyPs in dye and lignin degradation, which vary greatly among DyPs classes. In addition, application prospects of DyPs in biomedicine and other fields are also discussed briefly. At the same time, the research strategy based on genetic engineering and synthetic biology in improving the stability and catalytic activity of DyPs are summarized along with the important industrial applications of DyPs and associated challenges. Moreover, according to the current research findings, bringing DyPs to the industrial level may require improving the catalytic efficiency of DyP, increasing production, and enhancing alkali resistance and toxicity. Full article
(This article belongs to the Special Issue Recent Advances in Biocatalysis and Metabolic Engineering)
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