J. Thomas, Martha Daniela Burich, P. Bandeira, Alfredo Ricardo Marques de Oliveira, Leandro Piovan
Abstract Enzymatic kinetic resolution reactions are a well-established way to achieve optically active compounds. When enzymatic reactions are combined to continuous-flow methodologies, other benefits are added, including reproducibility, optimized energy use, minimized waste generation, among others. In this context, we herein report a case study involving lipase-mediated transesterification by acylation and deacylation reactions of secondary alcohols/esters in batch and continuous-flow modes. Acylation reactions were performed with high values of enantiomeric excess (72 up to >99%) and enantioselectivity (E > 200) for both batch and continuous-flow modes. On the other hand, for deacylation reactions using n-butanol as nucleophile, enatiomeric excess ranged between 38 to >99% and E from 6 to >200 were observed for batch mode. For deacylation reactions in continuous-flow mode, results were disappointing, as in some cases, very low or no conversion was observed. Enantiomeric excess ranged from 16 to >99% and enantioselectivity from 5 to >200 were observed. In terms of productivity, continuous-flow mode reactions were superior in both strategies (acylation: r from 1.1 up to 18.1-fold higher, deacylation: 2.8 up to 7.4- fold higher in continuous-flow than in batch mode).
{"title":"Biocatalysis in continuous-flow mode: A case-study in the enzymatic kinetic resolution of secondary alcohols via acylation and deacylation reactions mediated by Novozym 435®","authors":"J. Thomas, Martha Daniela Burich, P. Bandeira, Alfredo Ricardo Marques de Oliveira, Leandro Piovan","doi":"10.1515/boca-2017-0003","DOIUrl":"https://doi.org/10.1515/boca-2017-0003","url":null,"abstract":"Abstract Enzymatic kinetic resolution reactions are a well-established way to achieve optically active compounds. When enzymatic reactions are combined to continuous-flow methodologies, other benefits are added, including reproducibility, optimized energy use, minimized waste generation, among others. In this context, we herein report a case study involving lipase-mediated transesterification by acylation and deacylation reactions of secondary alcohols/esters in batch and continuous-flow modes. Acylation reactions were performed with high values of enantiomeric excess (72 up to >99%) and enantioselectivity (E > 200) for both batch and continuous-flow modes. On the other hand, for deacylation reactions using n-butanol as nucleophile, enatiomeric excess ranged between 38 to >99% and E from 6 to >200 were observed for batch mode. For deacylation reactions in continuous-flow mode, results were disappointing, as in some cases, very low or no conversion was observed. Enantiomeric excess ranged from 16 to >99% and enantioselectivity from 5 to >200 were observed. In terms of productivity, continuous-flow mode reactions were superior in both strategies (acylation: r from 1.1 up to 18.1-fold higher, deacylation: 2.8 up to 7.4- fold higher in continuous-flow than in batch mode).","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"93 1","pages":"27 - 36"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87500796","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M. Ferraroni, A. Westphal, M. Borsari, J. A. Tamayo-Ramos, F. Briganti, L. Graaff, W. Berkel
Abstract The ascomycete Aspergillus niger produces several multicopper oxidases, but their biocatalytic properties remain largely unknown. Elucidation of the crystal structure of A. niger laccase McoG at 1.7 Å resolution revealed that the C-terminal tail of this glycoprotein blocks the T3 solvent channel and that a peroxide ion bridges the two T3 copper atoms. Remarkably, McoG contains a histidine (His253) instead of the common aspartate or glutamate expected to be involved in catalytic proton transfer with phenolic compounds. The crystal structure of H253D at 1.5 Å resolution resembles the wild type structure. McoG and the H253D, H253A and H253N variants have similar activities with 2,2’-azino-bis(3- ethylbenzothiazoline-6-sulphonic acid or N,N-dimethyl-p-phenylenediamine sulphate. However, the activities of H253A and H253N with 2-amino-4-methylphenol and 2-amino-4-methoxyphenol are strongly reduced compared to that of wild type. The redox potentials and electron transfer rates (ks) of wild type and variants were determined (McoG wt E°’ is +453 mV), and especially the reduced ks values of H253A and H253N show strong correlation with their low activity on phenolic compounds. In summary, our results suggest that the His253 adaptation of McoG can be beneficial for the conversion of phenolic compounds.
{"title":"Structure and function of Aspergillus niger laccase McoG","authors":"M. Ferraroni, A. Westphal, M. Borsari, J. A. Tamayo-Ramos, F. Briganti, L. Graaff, W. Berkel","doi":"10.1515/boca-2017-0001","DOIUrl":"https://doi.org/10.1515/boca-2017-0001","url":null,"abstract":"Abstract The ascomycete Aspergillus niger produces several multicopper oxidases, but their biocatalytic properties remain largely unknown. Elucidation of the crystal structure of A. niger laccase McoG at 1.7 Å resolution revealed that the C-terminal tail of this glycoprotein blocks the T3 solvent channel and that a peroxide ion bridges the two T3 copper atoms. Remarkably, McoG contains a histidine (His253) instead of the common aspartate or glutamate expected to be involved in catalytic proton transfer with phenolic compounds. The crystal structure of H253D at 1.5 Å resolution resembles the wild type structure. McoG and the H253D, H253A and H253N variants have similar activities with 2,2’-azino-bis(3- ethylbenzothiazoline-6-sulphonic acid or N,N-dimethyl-p-phenylenediamine sulphate. However, the activities of H253A and H253N with 2-amino-4-methylphenol and 2-amino-4-methoxyphenol are strongly reduced compared to that of wild type. The redox potentials and electron transfer rates (ks) of wild type and variants were determined (McoG wt E°’ is +453 mV), and especially the reduced ks values of H253A and H253N show strong correlation with their low activity on phenolic compounds. In summary, our results suggest that the His253 adaptation of McoG can be beneficial for the conversion of phenolic compounds.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"5 1","pages":"1 - 21"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81147281","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Magdalena de Jesús Rostro-Alanis, Elena I. Mancera-Andrade, Mayra Beatriz Gómez Patiño, D. Arrieta-Báez, B. Cardenas, S. Martínez-Chapa, Roberto Parra Saldivar
Abstract The field of nanobiocatalysis has experienced a rapid growth due to recent advances in nanotechnology. However, biocatalytic processes are often limited by the lack of stability of the enzymes and their short lifetime. Therefore, immobilization is key to the successful implementation of industrial processes based on enzymes. Immobilization of enzymes on functionalized nanostructured materials could give higher stability to nanobiocatalysts while maintaining free enzyme activity and easy recyclability under various conditions. This review will discuss recent developments in nanobiocatalysis to improve the stability of the enzyme using various nanostructured materials such as mesoporous materials, nanofibers, nanoparticles, nanotubes, and individual nanoparticles enzymes. Also, this review summarizes the recent evolution of nanostructured biocatalysts with an emphasis on those formed with polymers. Based on the synthetic procedures used, established methods fall into two important categories: “grafting onto” and “grafting from”. The fundamentals of each method in enhancing enzyme stability and the use of these new nanobiocatalysts as tools for different applications in different areas are discussed.
{"title":"Nanobiocatalysis: Nanostructured materials – a minireview","authors":"Magdalena de Jesús Rostro-Alanis, Elena I. Mancera-Andrade, Mayra Beatriz Gómez Patiño, D. Arrieta-Báez, B. Cardenas, S. Martínez-Chapa, Roberto Parra Saldivar","doi":"10.1515/boca-2016-0001","DOIUrl":"https://doi.org/10.1515/boca-2016-0001","url":null,"abstract":"Abstract The field of nanobiocatalysis has experienced a rapid growth due to recent advances in nanotechnology. However, biocatalytic processes are often limited by the lack of stability of the enzymes and their short lifetime. Therefore, immobilization is key to the successful implementation of industrial processes based on enzymes. Immobilization of enzymes on functionalized nanostructured materials could give higher stability to nanobiocatalysts while maintaining free enzyme activity and easy recyclability under various conditions. This review will discuss recent developments in nanobiocatalysis to improve the stability of the enzyme using various nanostructured materials such as mesoporous materials, nanofibers, nanoparticles, nanotubes, and individual nanoparticles enzymes. Also, this review summarizes the recent evolution of nanostructured biocatalysts with an emphasis on those formed with polymers. Based on the synthetic procedures used, established methods fall into two important categories: “grafting onto” and “grafting from”. The fundamentals of each method in enhancing enzyme stability and the use of these new nanobiocatalysts as tools for different applications in different areas are discussed.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"70 1","pages":"1 - 24"},"PeriodicalIF":0.0,"publicationDate":"2016-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74365649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Abstract The design of a specific reaction medium capable to enhance activity, stability, and productivity of biocatalysts has been a recurring topic of study during the last three decades. The remarkable properties and valuable applications of enzymes, especially lipases, have inspiried different strategies for improving their performance in near-anhydrous media. As lipases are the most frequently used enzymes in organic synthesis, understanding the influence of reaction media on their activity and selectivity is crucial. In this paper, we review the key features of lipases and demonstrate how medium-engineering is a useful tool to modulate the activity and selectivity of lipase-catalyzed reactions.
{"title":"Medium-engineering: a useful tool for modulating lipase activity and selectivity","authors":"E. Castillo, L. Casas-Godoy, G. Sandoval","doi":"10.1515/boca-2015-0013","DOIUrl":"https://doi.org/10.1515/boca-2015-0013","url":null,"abstract":"Abstract The design of a specific reaction medium capable to enhance activity, stability, and productivity of biocatalysts has been a recurring topic of study during the last three decades. The remarkable properties and valuable applications of enzymes, especially lipases, have inspiried different strategies for improving their performance in near-anhydrous media. As lipases are the most frequently used enzymes in organic synthesis, understanding the influence of reaction media on their activity and selectivity is crucial. In this paper, we review the key features of lipases and demonstrate how medium-engineering is a useful tool to modulate the activity and selectivity of lipase-catalyzed reactions.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"134 1","pages":"178 - 188"},"PeriodicalIF":0.0,"publicationDate":"2016-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83752910","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Susana Velasco-Lozano, F. López‐Gallego, J. C. Mateos-Díaz, E. Favela‐Torres
Abstract Structural and functional catalytic characteristics of cross-linked enzyme aggregates (CLEA) are reviewed. Firstly, advantages of enzyme immobilization and existing types of immobilization are described. Then, a wide description of the factors that modify CLEA activity, selectivity and stability is presented. Nowadays CLEA offers an economic, simple and easy tool to reuse biocatalysts, improving their catalytic properties and stability. This immobilization methodology has been widely and satisfactorily tested with a great variety of enzymes and has demonstrated its potential as a future tool to optimize biocatalytic processes.
{"title":"Cross-linked enzyme aggregates (CLEA) in enzyme improvement – a review","authors":"Susana Velasco-Lozano, F. López‐Gallego, J. C. Mateos-Díaz, E. Favela‐Torres","doi":"10.1515/boca-2015-0012","DOIUrl":"https://doi.org/10.1515/boca-2015-0012","url":null,"abstract":"Abstract Structural and functional catalytic characteristics of cross-linked enzyme aggregates (CLEA) are reviewed. Firstly, advantages of enzyme immobilization and existing types of immobilization are described. Then, a wide description of the factors that modify CLEA activity, selectivity and stability is presented. Nowadays CLEA offers an economic, simple and easy tool to reuse biocatalysts, improving their catalytic properties and stability. This immobilization methodology has been widely and satisfactorily tested with a great variety of enzymes and has demonstrated its potential as a future tool to optimize biocatalytic processes.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"1 1","pages":"166 - 177"},"PeriodicalIF":0.0,"publicationDate":"2016-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88704856","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Abstract Microfluidic reaction devices are a very promising technology for chemical and biochemical processes. In microreactors, the micro dimensions, coupled with a high surface area/volume ratio, permit rapid heat exchange and mass transfer, resulting in higher reaction yields and reaction rates than in conventional reactors. Moreover, the lower energy consumption and easier separation of products permit these systems to have a lower environmental impact compared to macroscale, conventional reactors. Due to these benefits, the use of microreactors is increasing in the biocatalysis field, both by using enzymes in solution and their immobilized counterparts. Following an introduction to the most common applications of microreactors in chemical processes, a broad overview will be given of the latest applications in biocatalytic processes performed in microreactors with free or immobilized enzymes. In particular, attention is given to the nature of the materials used as a support for the enzymes and the strategies employed for their immobilization. Mathematical and engineering aspects concerning fluid dynamics in microreactors were also taken into account as fundamental factors for the optimization of these systems.
{"title":"Enzymatic microreactors in biocatalysis: history, features, and future perspectives","authors":"E. Laurenti, Ardson dos Santos Vianna Jr.","doi":"10.1515/boca-2015-0008","DOIUrl":"https://doi.org/10.1515/boca-2015-0008","url":null,"abstract":"Abstract Microfluidic reaction devices are a very promising technology for chemical and biochemical processes. In microreactors, the micro dimensions, coupled with a high surface area/volume ratio, permit rapid heat exchange and mass transfer, resulting in higher reaction yields and reaction rates than in conventional reactors. Moreover, the lower energy consumption and easier separation of products permit these systems to have a lower environmental impact compared to macroscale, conventional reactors. Due to these benefits, the use of microreactors is increasing in the biocatalysis field, both by using enzymes in solution and their immobilized counterparts. Following an introduction to the most common applications of microreactors in chemical processes, a broad overview will be given of the latest applications in biocatalytic processes performed in microreactors with free or immobilized enzymes. In particular, attention is given to the nature of the materials used as a support for the enzymes and the strategies employed for their immobilization. Mathematical and engineering aspects concerning fluid dynamics in microreactors were also taken into account as fundamental factors for the optimization of these systems.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"25 1","pages":"148 - 165"},"PeriodicalIF":0.0,"publicationDate":"2016-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83767912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Fernando García-Guevara, M. Avelar, M. Ayala, L. Segovia
Abstract The protein design toolbox has been greatly improved by the addition of enzyme computational simulations. Not only do they warrant a more ambitious and thorough exploration of sequence space, but a much higher number of variants and protein-ligand systems can be analyzed in silico compared to experimental engineering methods. Modern computational tools are being used to redesign and also for de novo generation of enzymes. These approaches are contingent on a deep understanding of the reaction mechanism and the enzyme’s three-dimensional structure coordinates, but the wealth of information produced by these analyses leads to greatly improved or even totally new types of catalysis.
{"title":"Computational Tools Applied to Enzyme Design − a review","authors":"Fernando García-Guevara, M. Avelar, M. Ayala, L. Segovia","doi":"10.1515/boca-2015-0009","DOIUrl":"https://doi.org/10.1515/boca-2015-0009","url":null,"abstract":"Abstract The protein design toolbox has been greatly improved by the addition of enzyme computational simulations. Not only do they warrant a more ambitious and thorough exploration of sequence space, but a much higher number of variants and protein-ligand systems can be analyzed in silico compared to experimental engineering methods. Modern computational tools are being used to redesign and also for de novo generation of enzymes. These approaches are contingent on a deep understanding of the reaction mechanism and the enzyme’s three-dimensional structure coordinates, but the wealth of information produced by these analyses leads to greatly improved or even totally new types of catalysis.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"22 1","pages":"109 - 117"},"PeriodicalIF":0.0,"publicationDate":"2016-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77145466","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ana Maria Mouad, A. L. L. de Oliveira, H. Debonsi, A. Porto
Abstract Four endophytic fungi isolated from the marine red alga Bostrychia radicans identified as Botryosphaeria sp. CBMAI 1197, Eutypella sp. CBMAI 1196, Hidropisphaera sp. CBMAI 1194 and Xylaria sp. CBMAI 1195 catalyzed the asymmetric bioreduction of fluoroacetophenone derivatives 1-3 to the corresponding fluorophenylalcohols 1a-3a. In the reduction reactions of 2,2,2-trifluoro-1-phenylethanone 1, all the marine fungi produced exclusively the (S)-2,2,2-trifluoro- 1-phenylethanol 1a with > 99% ee. The fungus Botryosphaeria sp. CBMAI 1197 exhibited the best enzymatic potential, leading to the highest conversion values (up to > 99%). The biocatalyst Botryosphaeria sp. CBMAI 1197 also presented active enzymes in reactions with the substrates 1-(2-(trifluoromethyl)phenyl) ethanone (2) and 1-(2,4,5-trifluorophenyl)ethanone (3), producing the respective chiral alcohols S-2a and R-3a with > 99% ee. Additionally, the fungus Hidropisphaera sp. CBMAI 1194 yielded 100% of conversion of the ketone 3 to the corresponding S-alcohol 3a, with 53% ee.
{"title":"Bioreduction of fluoroacetophenone derivatives by endophytic fungi isolated from the marine red alga Bostrychia radicans","authors":"Ana Maria Mouad, A. L. L. de Oliveira, H. Debonsi, A. Porto","doi":"10.1515/boca-2015-0011","DOIUrl":"https://doi.org/10.1515/boca-2015-0011","url":null,"abstract":"Abstract Four endophytic fungi isolated from the marine red alga Bostrychia radicans identified as Botryosphaeria sp. CBMAI 1197, Eutypella sp. CBMAI 1196, Hidropisphaera sp. CBMAI 1194 and Xylaria sp. CBMAI 1195 catalyzed the asymmetric bioreduction of fluoroacetophenone derivatives 1-3 to the corresponding fluorophenylalcohols 1a-3a. In the reduction reactions of 2,2,2-trifluoro-1-phenylethanone 1, all the marine fungi produced exclusively the (S)-2,2,2-trifluoro- 1-phenylethanol 1a with > 99% ee. The fungus Botryosphaeria sp. CBMAI 1197 exhibited the best enzymatic potential, leading to the highest conversion values (up to > 99%). The biocatalyst Botryosphaeria sp. CBMAI 1197 also presented active enzymes in reactions with the substrates 1-(2-(trifluoromethyl)phenyl) ethanone (2) and 1-(2,4,5-trifluorophenyl)ethanone (3), producing the respective chiral alcohols S-2a and R-3a with > 99% ee. Additionally, the fungus Hidropisphaera sp. CBMAI 1194 yielded 100% of conversion of the ketone 3 to the corresponding S-alcohol 3a, with 53% ee.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"26 1","pages":"141 - 147"},"PeriodicalIF":0.0,"publicationDate":"2016-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87934719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
G. Rebollar-Pérez, J. Campos-Terán, N. Ornelas-Soto, A. Méndez-Albores, E. Torres
Abstract In recent years, the continuous and accumulative discharge of toxic and contaminating compounds to the environment makes necessary to propose precise and quick methods for their detection and quantitation. Especially when one considers that the environmental impact of some of these emerging contaminants has not been clearly determined. Enzyme-based biosensors are an interesting alternative when inspecting different pollutants present in the environment in a quick, efficient, automatized, and economic way. Oxidative enzymes such as peroxidases and polyphenol oxidases (laccases and tyrosinases) are versatile and highly functional enzymes used for analyte recognition. Therefore, these enzymes are considered attractive and interesting biomolecules to act as recognition elements in biosensors. In this regard, detection of pollutants such as pesticides, phenols, heavy metals, and pharmaceutical compounds by using oxidative enzymes as recognition elements in biosensors is a versatile field, and it is the focus of the present review.
{"title":"Biosensors based on oxidative enzymes for detection of environmental pollutants","authors":"G. Rebollar-Pérez, J. Campos-Terán, N. Ornelas-Soto, A. Méndez-Albores, E. Torres","doi":"10.1515/boca-2015-0010","DOIUrl":"https://doi.org/10.1515/boca-2015-0010","url":null,"abstract":"Abstract In recent years, the continuous and accumulative discharge of toxic and contaminating compounds to the environment makes necessary to propose precise and quick methods for their detection and quantitation. Especially when one considers that the environmental impact of some of these emerging contaminants has not been clearly determined. Enzyme-based biosensors are an interesting alternative when inspecting different pollutants present in the environment in a quick, efficient, automatized, and economic way. Oxidative enzymes such as peroxidases and polyphenol oxidases (laccases and tyrosinases) are versatile and highly functional enzymes used for analyte recognition. Therefore, these enzymes are considered attractive and interesting biomolecules to act as recognition elements in biosensors. In this regard, detection of pollutants such as pesticides, phenols, heavy metals, and pharmaceutical compounds by using oxidative enzymes as recognition elements in biosensors is a versatile field, and it is the focus of the present review.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"36 1","pages":"118 - 129"},"PeriodicalIF":0.0,"publicationDate":"2016-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79373717","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sachin B. Mulik, Saptarshi Ghosh, Jayeeta Bhaumik, U. Banerjee
Abstract The present study describes an efficient chemoenzymatic synthesis of enantiopure (S)-Practolol, a selective β-adrenergic receptor blocker. Prior to the synthesis of the target, a synthetic protocol for (RS)-N-4-(3-chloro-2-hydroxypropoxy)phenylacetamide, an essential precursor, was developed. Various commercial lipases were screened for the kinetic resolution of (RS)- N-4-(3-chloro-2-hydroxypropoxy)phenylacetamide using toluene as solvent and vinyl acetate as an acyl donor. Among various lipases screened, Pseudomonas cepacia sol-gel AK showed the highest enantioselectivity (96% enantiomeric excess with 50% conversion), affording (S)-1-(4-acetamidophenoxy)-3-chloropropan-2-yl acetate. Optimization of the reaction parameters was carried out in order to find the best-suited conditions for the biocatalysis. Furthermore, the enantiopure intermediate was hydrolyzed and the resulting product was reacted with isopropylamine to afford (S)-Practolol. This biocatalytic procedure depicts a green technology for the synthesis of (S)-Practolol with better yield and enantiomeric excess.
摘要本研究描述了一种高效的化学酶合成对映纯(S)-Practolol，一种选择性β-肾上腺素受体阻滞剂。在合成目标之前，开发了一种重要前体(RS)- n -4-(3-氯-2-羟基丙氧基)苯乙酰胺的合成方案。以甲苯为溶剂，醋酸乙烯为酰基给体，筛选了多种商用脂肪酶对(RS)- N-4-(3-氯-2-羟基丙氧基)苯乙酰胺的动力学分解。在筛选的各种脂肪酶中，洋葱假单胞菌溶胶-凝胶AK表现出最高的对映体选择性(96%的对映体过剩，50%的转化率)，提供(S)-1-(4-乙酰氨基苯氧基)-3-氯丙-2-乙酸酯。对反应参数进行了优化，以寻找最适宜的生物催化条件。再将对映纯中间体水解，产物与异丙胺反应生成(S)-普practolol。这一生物催化过程描述了一种绿色合成(S)-Practolol的技术，具有较高的产率和对映体过量。
{"title":"Biocatalytic synthesis of (S)-Practolol, a selective β-blocker","authors":"Sachin B. Mulik, Saptarshi Ghosh, Jayeeta Bhaumik, U. Banerjee","doi":"10.1515/boca-2015-0006","DOIUrl":"https://doi.org/10.1515/boca-2015-0006","url":null,"abstract":"Abstract The present study describes an efficient chemoenzymatic synthesis of enantiopure (S)-Practolol, a selective β-adrenergic receptor blocker. Prior to the synthesis of the target, a synthetic protocol for (RS)-N-4-(3-chloro-2-hydroxypropoxy)phenylacetamide, an essential precursor, was developed. Various commercial lipases were screened for the kinetic resolution of (RS)- N-4-(3-chloro-2-hydroxypropoxy)phenylacetamide using toluene as solvent and vinyl acetate as an acyl donor. Among various lipases screened, Pseudomonas cepacia sol-gel AK showed the highest enantioselectivity (96% enantiomeric excess with 50% conversion), affording (S)-1-(4-acetamidophenoxy)-3-chloropropan-2-yl acetate. Optimization of the reaction parameters was carried out in order to find the best-suited conditions for the biocatalysis. Furthermore, the enantiopure intermediate was hydrolyzed and the resulting product was reacted with isopropylamine to afford (S)-Practolol. This biocatalytic procedure depicts a green technology for the synthesis of (S)-Practolol with better yield and enantiomeric excess.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"3 1","pages":"130 - 140"},"PeriodicalIF":0.0,"publicationDate":"2016-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84674008","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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