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Application of Immobilized Enzyme as Catalysts in Chemical Synthesis
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Application of Immobilized Enzyme as Catalysts in Chemical Synthesis

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

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 38997

Special Issue Editors

Prof. Dr. Jose M. Guisan

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Guest Editor
Department of Biocatalysis, Institute of Catalysis, Spanish Research Council, ICP-CSIC, Campus UAM, 28049 Madrid, Spain
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 Issues, Collections and Topics in MDPI journals
Dr. Gloria Fernandez-Lorente

E-Mail Website
Guest Editor
Institute of Food Science Research (CIAL-CSIC), C/Nicolás Cabrera, 9, Campus de Cantoblanco, 28049 Madrid, Spain
Interests: enzyme engineering; enzyme biotransformations; food chemistry; analytical chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue will be focused on the report of any relevant chemical syntheses catalyzed by immobilized enzymes. In addition to that, special emphasis will be focused on (i) modulation of enzyme properties (activity, selectivity and stability) via immobilization and post-immobilization techniques; (ii) use of immobilized enzymes in non-conventional media (ionic liquids, organic solvents, etc.); (iii) use of immobilized enzymes in solvent-free systems; (iv) Sequential enzyme cascades: Co-immobilization and co-localization of two or more enzymes; (v) synthesis involving cofactor regeneration; (vi) design of immobilized enzyme reactors: Basket reactors, continuous flow reactors, etc.; (vii) chemo-enzymatic synthesis; (viii) asymmetric and enantioselective synthesis; (ix) re-use or continuous use of immobilized biocatalysts; (x) immobilization of enzymes that had been improved via biological techniques, etc.  

Prof. Dr. Jose M. Guisan
Dr. Gloria Fernandez-Lorente
Guest Editors

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Keywords

  • enzymes in chemical synthesis
  • modulation of enzyme properties
  • sequential enzymatic synthesis
  • continuous flow reactors
  • immobilization of improved enzyme variants

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Published Papers (11 papers)

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Research

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13 pages, 2580 KiB  
Article
Stabilization of Lecitase Ultra® by Immobilization and Fixation of Bimolecular Aggregates. Release of Omega-3 Fatty Acids by Enzymatic Hydrolysis of Krill Oil
by Daniel Andrés-Sanz, Cristina Fresan, Gloria Fernández-Lorente, Javier Rocha-Martín and Jose M. Guisán
Catalysts 2021, 11(9), 1067; https://doi.org/10.3390/catal11091067 - 31 Aug 2021
Cited by 2 | Viewed by 2718
Abstract
Lecitase Ultra® solutions are mainly composed of bimolecular aggregates of two open structures of the enzyme. The immobilization and fixation of these bimolecular aggregates onto support surfaces is here proposed as a novel protocol for the immobilization and stabilization of Lecitase. The [...] Read more.
Lecitase Ultra® solutions are mainly composed of bimolecular aggregates of two open structures of the enzyme. The immobilization and fixation of these bimolecular aggregates onto support surfaces is here proposed as a novel protocol for the immobilization and stabilization of Lecitase. The resulting derivatives of Lecitase aggregates were much more stable than the diluted solutions of the enzyme. The most stable of them was obtained by covalent immobilization of the bimolecular aggregate: 300-fold more stable than the diluted enzyme and 75-fold more stable than open Lecitase adsorbed onto hydrophobic supports. The bimolecular aggregate that adsorbed onto polyethyleneimine-agarose exhibited the best combination of activity and stability for the hydrolysis of krill oil. Omega-3 acids are in the sn-2 position of the krill oil, but they are also released by a phospholipase A1 because of migration issues. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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12 pages, 4761 KiB  
Article
Green and High Effective Scale Inhibitor Based on Ring-Opening Graft Modification of Polyaspartic Acid
by Yongsheng Zhou, Jie Wang and Yan Fang
Catalysts 2021, 11(7), 802; https://doi.org/10.3390/catal11070802 - 30 Jun 2021
Cited by 17 | Viewed by 3412
Abstract
Polyaspartic acid (PASP)-based green scale inhibitor has great potential application in water treatment. Here, we first synthesized PASP in ionic liquid. Then, an effective PASP-based green scale inhibitor was synthesized by ring-opening graft modification of PASP with both aspartic acid (ASP) and monoethanolamine [...] Read more.
Polyaspartic acid (PASP)-based green scale inhibitor has great potential application in water treatment. Here, we first synthesized PASP in ionic liquid. Then, an effective PASP-based green scale inhibitor was synthesized by ring-opening graft modification of PASP with both aspartic acid (ASP) and monoethanolamine (MEA). Its chemical composition was characterized by gel chromatography (GPC), Fourier transform infrared spectroscopy (FTIR), and 1H nuclear magnetic resonance (1H NMR). Scale inhibition efficiency was measured by static scale inhibition tests. The results showed that the new PASP-based scale inhibitor has high scale inhibition to both CaCO3 and Ca3(PO4)2. When the concentration was increased to 2 mg/L, the inhibition efficiency of the new PASP-based scale inhibitor was 99% for CaCO3, while when the concentration was raised to only 4 mg/L, its inhibition efficiency increased to 100% for Ca3(PO4)2. Scanning electronic microscopy (SEM) and X-ray diffraction (XRD) were used to analyze the changes of crystal structure for CaCO3 and Ca3(PO4)2 after adding the new PASP-based scale inhibitor. The crystal size of CaCO3 and Ca3(PO4)2 became smaller and the crystal form became amorphous after adding the modified PASPs compared with adding pure PASP. Moreover, the modified PASP showed good biodegradation performance. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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13 pages, 907 KiB  
Article
Sugarcane Bagasse Saccharification by Enzymatic Hydrolysis Using Endocellulase and β-glucosidase Immobilized on Different Supports
by Wilson G. Morais Junior, Thályta F. Pacheco, Shipeng Gao, Pedro A. Martins, José M. Guisán and Nídia S. Caetano
Catalysts 2021, 11(3), 340; https://doi.org/10.3390/catal11030340 - 7 Mar 2021
Cited by 28 | Viewed by 4489
Abstract
The saccharification of sugarcane bagasse by enzymatic hydrolysis is one of the most promising processes for obtaining fermentable sugar to be used in the production of second-generation ethanol. The objective of this work was to study the immobilization and stabilization of two commercial [...] Read more.
The saccharification of sugarcane bagasse by enzymatic hydrolysis is one of the most promising processes for obtaining fermentable sugar to be used in the production of second-generation ethanol. The objective of this work was to study the immobilization and stabilization of two commercial enzymes: Endocellulase (E-CELBA) in dextran coated iron oxide magnetic nanoparticles activated with aldehyde groups (DIOMNP) and β-glucosidase (E-BGOSPC) in glyoxyl agarose (GLA) so that their immobilized derivatives could be applied in the saccharification of pretreated sugarcane bagasse. This was the first time that the pretreated sugarcane bagasse was saccharified by cascade reaction using a endocellulase immobilized on dextran coated Fe2O3 with aldehyde groups combined with a β-glucosidase immobilized on glyoxyl agarose. Both enzymes were successfully immobilized (more than 60% after reduction with sodium borohydride) and presented higher thermal stability than free enzymes at 60, 70, and 80 °C. The enzymatic hydrolysis of the sugarcane bagasse was carried out with 15 U of each enzyme per gram of bagasse in a solid-liquid ratio of 1:20 for 48 h at 50 °C. Under these conditions, 39.06 ± 1.18% of the cellulose present in the pretreated bagasse was hydrolyzed, producing 14.11 ± 0.47 g/L of reducing sugars (94.54% glucose). In addition, DIOMNP endo-cellulase derivative maintained 61.40 ± 1.17% of its enzymatic activity after seven reuse cycles, and GLA β-glucosidase derivative maintained up to 58.20 ± 1.55% of its enzymatic activity after nine reuse cycles. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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27 pages, 6375 KiB  
Article
Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol
by Nadya Dencheva, Sandra Oliveira, Joana Braz, Dariya Getya, Marc Malfois, Zlatan Denchev and Ivan Gitsov
Catalysts 2021, 11(2), 239; https://doi.org/10.3390/catal11020239 - 11 Feb 2021
Cited by 11 | Viewed by 2798
Abstract
Herewith we report the first attempt towards non-covalent immobilization of Trametes versicolor laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and [...] Read more.
Herewith we report the first attempt towards non-covalent immobilization of Trametes versicolor laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe3O4 cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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17 pages, 2042 KiB  
Article
Interesterification of Egg-Yolk Phosphatidylcholine with p-Methoxycinnamic Acid Catalyzed by Immobilized Lipase B from Candida Antarctica
by Magdalena Rychlicka and Anna Gliszczyńska
Catalysts 2020, 10(10), 1181; https://doi.org/10.3390/catal10101181 - 14 Oct 2020
Cited by 5 | Viewed by 2646
Abstract
The p-methoxycinnamic acid (p-MCA) is one of the most popular phenylpropanoids, the beneficial impact of which on the human health is well documented in the literature. This compound has shown many valuable activities including anticancer, antidiabetic, and neuro- and hepatoprotective. [...] Read more.
The p-methoxycinnamic acid (p-MCA) is one of the most popular phenylpropanoids, the beneficial impact of which on the human health is well documented in the literature. This compound has shown many valuable activities including anticancer, antidiabetic, and neuro- and hepatoprotective. However, its practical application is limited by its low bioavailability resulting from rapid metabolism in the human body. The latest strategy, aimed at overcoming these limitations, is based on the production of more stability in systemic circulation bioconjugates with phospholipids. Therefore, the aim of this research was to develop the biotechnological method for the synthesis of phospholipid derivatives of p-methoxycinnamic acid, which can play a role of new nutraceuticals. We developed and optimized enzymatic interesterification of phosphatidylcholine (PC) with ethyl p-methoxycinnamate (Ep-MCA). Novozym 435 and a binary solvent system of toluene/chloroform 9:1 (v/v) were found to be the effective biocatalyst and reaction medium for the synthesis of structured p-MCA phospholipids, respectively. The effects of the other reaction parameters, such as substrate molar ratio, enzyme dosage, and reaction time, on the degree of incorporation of p-MCA into PC were evaluated by use of an experimental factorial design method. The results showed that substrate molar ratio and biocatalyst load have significant effects on the synthesis of p-methoxycinnamoylated phospholipids. The optimum conditions were: Reaction time of three days, 30% (w/w) of Novozym 435, and 1/10 substrate molar ratio PC/Ep-MCA. Under these parameters, p-methoxycinnamoylated lysophosphatidylcholine (p-MCA-LPC) and p-methoxycinnamoylated phosphatidylcholine (p-MCA-PC) were obtained in isolated yields of 32% and 3% (w/w), respectively. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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18 pages, 3204 KiB  
Article
Co-Immobilization and Co-Localization of Oxidases and Catalases: Catalase from Bordetella Pertussis Fused with the Zbasic Domain
by Paz García-García, Javier Rocha-Martin, Jose M. Guisan and Gloria Fernandez-Lorente
Catalysts 2020, 10(7), 810; https://doi.org/10.3390/catal10070810 - 21 Jul 2020
Cited by 7 | Viewed by 2814
Abstract
Oxidases catalyze selective oxidations by using molecular oxygen as an oxidizing agent. This process promotes the release of hydrogen peroxide, an undesirable byproduct. The instantaneous elimination of hydrogen peroxide can be achieved by co-immobilization and co-localization of the oxidase and an auxiliary catalase [...] Read more.
Oxidases catalyze selective oxidations by using molecular oxygen as an oxidizing agent. This process promotes the release of hydrogen peroxide, an undesirable byproduct. The instantaneous elimination of hydrogen peroxide can be achieved by co-immobilization and co-localization of the oxidase and an auxiliary catalase inside the porous structure of solid support. In this paper, we proposed that catalase from Bordetella pertussis fused with a small domain (Zbasic) as an excellent auxiliary enzyme. The enzyme had a specific activity of 23 U/mg, and this was almost six-fold higher than the one of the commercially available catalases from bovine liver. The Zbasic domain was fused to the four amino termini of this tetrameric enzyme. Two domains were close in one hemisphere of the enzyme molecule, and the other two were close in the opposite hemisphere. In this way, each hemisphere contained 24 residues with a positive charge that was very useful for the purification of the enzyme via cationic exchange chromatography. In addition to this, each hemisphere contained 10 Lys residues that were very useful for a rapid and intense multipoint covalent attachment on highly activated glyoxyl supports. In fact, 190 mg of the enzyme was immobilized on one gram of glyoxyl-10% agarose gel. The ratio catalase/oxidase able to instantaneously remove more than 93% of the released hydrogen peroxide was around 5–6 mg of catalase per mg of oxidase. Thirty milligrams of amine oxidase and 160 mg of catalase were co-immobilized and co-localized per gram of glyoxyl-agarose 10BCL (10% beads cross-linked) support. This biocatalyst eliminated biogenic amines (putrescine) 80-fold faster than a biocatalyst of the same oxidase co-localized with the commercial catalase from bovine liver. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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11 pages, 2774 KiB  
Article
Polymer Membrane with Glycosylated Surface by a Chemo-Enzymatic Strategy for Protein Affinity Adsorption
by Yan Fang, Ting He, Hao Gao, Lingling Fan, Jingyuan Liu, Binrui Li, Haowei Zhang and Huiyu Bai
Catalysts 2020, 10(4), 415; https://doi.org/10.3390/catal10040415 - 9 Apr 2020
Cited by 4 | Viewed by 2191
Abstract
Membranes with glycosylated surfaces are naturally biomimetic and not only have excellent surface hydrophilicity and biocompatibility, but have a specific recognition to target biomacromolecules due to the unique chemo-biological properties of their surface carbohydrates; however, they cannot be easily chemically produced on large [...] Read more.
Membranes with glycosylated surfaces are naturally biomimetic and not only have excellent surface hydrophilicity and biocompatibility, but have a specific recognition to target biomacromolecules due to the unique chemo-biological properties of their surface carbohydrates; however, they cannot be easily chemically produced on large scales due to the complex preparation process. This manuscript describes the fabrication of a polypropylene membrane with a glycosylated surface by a chemo-enzymatic strategy. First, hydroxyl (OH) groups were introduced onto the surface of microporous polypropylene membrane (MPPM) by UV-induced grafting polymerization of oligo(ethylene glycol) methacrylate (OEGMA). Then, glycosylation of the OH groups with galactose moieties was achieved via an enzymatic transglycosylation by β-galactosidase (Gal) recombinanted from E. coli. The fabricated glycosylated membrane showed surprisingly specific affinity adsorption to lectin ricinus communis agglutinin (RCA120). The chemo-enzymatic route is easy and green, and it would be expected to have wide applications for large-scale preparation of polymer membranes with glycosylated surfaces. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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20 pages, 3024 KiB  
Article
Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM
by Katerine S. Moreira, Lourembergue S. Moura Júnior, Rodolpho R. C. Monteiro, André L. B. de Oliveira, Camila P. Valle, Tiago M. Freire, Pierre B. A. Fechine, Maria C. M. de Souza, Gloria Fernandez-Lorente, José M. Guisan and José C. S. dos Santos
Catalysts 2020, 10(4), 414; https://doi.org/10.3390/catal10040414 - 9 Apr 2020
Cited by 80 | Viewed by 5251
Abstract
Residual oil from babassu (Orbignya sp.), a low-cost raw material, was used in the enzymatic esterification for biodiesel production, using lipase B from Candida antarctica (Novozym® 435) and ethanol. For the first time in the literature, residual babassu oil and Novozym [...] Read more.
Residual oil from babassu (Orbignya sp.), a low-cost raw material, was used in the enzymatic esterification for biodiesel production, using lipase B from Candida antarctica (Novozym® 435) and ethanol. For the first time in the literature, residual babassu oil and Novozym® 435 are being investigated to obtain biodiesel. In this communication, response surface methodology (RSM) and a central composite design (CCD) were used to optimize the esterification and study the effects of four factors (molar ratio (1:1–1:16, free fatty acids (FFAs) /alcohol), temperature (30–50 °C), biocatalyst content (0.05–0.15 g) and reaction time (2–6 h)) in the conversion into fatty acid ethyl esters. Under optimized conditions (1:18 molar ratio (FFAs/alcohol), 0.14 g of Novozym® 435, 48 °C and 4 h), the conversion into ethyl esters was 96.8%. It was found that after 10 consecutive cycles of esterification under optimal conditions, Novozym® 435 showed a maximum loss of activity of 5.8%, suggesting a very small change in the support/enzyme ratio proved by Fourier Transform Infrared (FTIR) spectroscopy and insignificant changes in the surface of Novozym® 435 proved by scanning electron microscopy (SEM) after the 10 consecutive cycles of esterification. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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14 pages, 4207 KiB  
Article
Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization
by Fang Wang, Rong Li, Hui Jian, Zihao Huang, Yingwu Wang, Zheng Guo and Renjun Gao
Catalysts 2020, 10(4), 410; https://doi.org/10.3390/catal10040410 - 8 Apr 2020
Cited by 4 | Viewed by 2639
Abstract
In recent years, the development and application of site-specific immobilization technology for proteins have undergone significant advances, which avoids the unwanted and random covalent linkage between the support and active site of protein in the covalent immobilization. Formylglycine generating enzyme (FGE) can transform [...] Read more.
In recent years, the development and application of site-specific immobilization technology for proteins have undergone significant advances, which avoids the unwanted and random covalent linkage between the support and active site of protein in the covalent immobilization. Formylglycine generating enzyme (FGE) can transform the cysteine from a conversed 6-amino-acid sequence CXPXR into formylglycine with an aldehyde group (also termed as “aldehyde tag”). Based on the frame of pET-28a, the His-tags were replaced with aldehyde tags. Afterward, a set of plasmids were constructed for site-specific covalent immobilization, their His-tags were knock out (DH), or were replaced at different positions: N-terminal (NQ), C-terminal (CQ), or both (DQ) respectively. Three different enzymes, thermophilic acyl aminopeptidase (EC 3.4.19.1) from Sulfolobus tokodaii (ST0779), thermophilic dehalogenase (EC 3.8.1.2) from Sulfolobus tokodaii (ST2570), and Lipase A (EC 3.1.1.3) from Bacillus subtilis (BsLA) were chosen as model enzymes to connect with these plasmid systems. The results showed that different aldehyde-tagged enzymes can be successfully covalently attached to different carriers modified with an amino group, proving the universality of the method. The new immobilized enzyme also presented better thermostability and reutilization than those of the free enzyme. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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12 pages, 2026 KiB  
Article
Interfacial Biocatalytic Performance of Nanofiber-Supported β-Galactosidase for Production of Galacto-Oligosaccharides
by Mailin Misson, Bo Jin, Sheng Dai and Hu Zhang
Catalysts 2020, 10(1), 81; https://doi.org/10.3390/catal10010081 - 6 Jan 2020
Cited by 9 | Viewed by 2817
Abstract
Molecular distribution, structural conformation and catalytic activity at the interface between enzyme and its immobilising support are vital in the enzymatic reactions for producing bioproducts. In this study, a nanobiocatalyst assembly, β-galactosidase immobilized on chemically modified electrospun polystyrene nanofibers (PSNF), was synthesized for [...] Read more.
Molecular distribution, structural conformation and catalytic activity at the interface between enzyme and its immobilising support are vital in the enzymatic reactions for producing bioproducts. In this study, a nanobiocatalyst assembly, β-galactosidase immobilized on chemically modified electrospun polystyrene nanofibers (PSNF), was synthesized for converting lactose into galacto-oligosaccharides (GOS). Characterization results using scanning electron microscopy (SEM) and fluorescence analysis of fluorescein isothiocyanat (FITC) labelled β-galactosidase revealed homogenous enzyme immobilization, thin layer structural conformation and biochemical functionalities of the nanobiocatalyst assembly. The β-galactosidase/PSNF assembly displayed enhanced enzyme catalytic performance at a residence time of around 1 min in a disc-stacked column reactor. A GOS yield of 41% and a lactose conversion of 88% was achieved at the initial lactose concentration of 300 g/L at this residence time. This system provided a controllable contact time of products and substrates on the nanofiber surface and could be used for products which are sensitive to the duration of nanobiocatalysis. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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Review

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29 pages, 2634 KiB  
Review
Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization
by Francisco T. T. Cavalcante, Antônio L. G. Cavalcante, Isamayra G. de Sousa, Francisco S. Neto and José C. S. dos Santos
Catalysts 2021, 11(10), 1222; https://doi.org/10.3390/catal11101222 - 11 Oct 2021
Cited by 94 | Viewed by 5901
Abstract
The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application [...] Read more.
The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level. Full article
(This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis)
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