Abstract Laccases are blue copper oxidases, found in some plants and secreted by a wide range of ligninolytic fungi. These enzymes are well known for their ability in oxidizing several organic compounds, mainly phenolics and aromatic amines, at the expenses of molecular oxygen. Therefore, they could find application in the field of enzymatic bioremediation of many industrial wastewaters, and in particular to bleach and/or detoxify dye-containing effluents. Not all industrial dyes behave as laccase substrates, but this limitation is often overcome by the judicious use of redox mediators. These could substantially widen the application range of laccases as bioremediation tools. The present study encompasses the main properties of the most used industrial dyes as related to their chemical classification, fungal laccases and their molecular and catalytic features, the use of redox mediators, limitations and perspectives of the use of fungal laccases for industrial dye bleaching.
{"title":"Fungal laccases as tools for biodegradation of industrial dyes","authors":"P. Zucca, G. Cocco, F. Sollai, E. Sanjust","doi":"10.1515/boca-2015-0007","DOIUrl":"https://doi.org/10.1515/boca-2015-0007","url":null,"abstract":"Abstract Laccases are blue copper oxidases, found in some plants and secreted by a wide range of ligninolytic fungi. These enzymes are well known for their ability in oxidizing several organic compounds, mainly phenolics and aromatic amines, at the expenses of molecular oxygen. Therefore, they could find application in the field of enzymatic bioremediation of many industrial wastewaters, and in particular to bleach and/or detoxify dye-containing effluents. Not all industrial dyes behave as laccase substrates, but this limitation is often overcome by the judicious use of redox mediators. These could substantially widen the application range of laccases as bioremediation tools. The present study encompasses the main properties of the most used industrial dyes as related to their chemical classification, fungal laccases and their molecular and catalytic features, the use of redox mediators, limitations and perspectives of the use of fungal laccases for industrial dye bleaching.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"49 1","pages":"108 - 82"},"PeriodicalIF":0.0,"publicationDate":"2016-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72597171","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 A single-step synthesis of (R)-α-methyl- 4-pyridinemethanol from (RS)-α-methyl-4- pyridinemethanol by stereoinversion using whole cells of Candida parapsilosis is reported. Among the various strains of Candida species examined, C. parapsilosis demonstrated to have the best oxidoreductase system for stereoinversion of (RS)-α-methyl-4-pyridinemethanol. The effect of various physicochemical parameters on the stereoinversion process, were studied. Under optimized conditions approximately 97% enantiomeric excess of (R)-α-methyl-4-pyridinemethanol (eeR) was obtained with 99% yield was obtained. The optimized parameters were determined to be a substrate concentration of 5 mM, pH 8.0, 30°C incubation temperature, and a reaction time of 48 h. The reactions were also carried out in different organic solvents, and maximum stereoinversion was obtained in 1,4-dioxane with 78.4% eeR and 74.7% yield, which are lower than those in phosphate buffer. This whole cell catalysis for the preparation of (R)-α-methyl-4- pyridinemethanol is an example of a green, enantiopure synthesis of secondary alcohols. Graphical Abstract
摘要报道了利用假丝酵母菌全细胞立体转化法，一步合成(RS)-α-甲基-4-吡啶乙醇。在所检测的念珠菌中，C. parapsilosis具有最佳的(RS)-α-甲基-4-吡啶乙醇立体转化氧化还原酶系统。研究了不同理化参数对立体转化过程的影响。在优化条件下，(R)-α-甲基-4-吡啶乙醇(eeR)的对映体含量约为97%，收率为99%。优化条件为底物浓度为5 mM, pH为8.0，反应温度为30℃，反应时间为48 h。在不同的有机溶剂中进行了反应，在1,4-二氧六环中获得的立体转化效果最好，转化率为78.4%，收率为74.7%，低于磷酸盐缓冲液。这种全细胞催化制备(R)-α-甲基-4-吡啶乙醇的方法是一个绿色、对映纯合成仲醇的例子。图形抽象
{"title":"Biocatalytic deracemization: An efficient one-pot synthesis of (R)-α-methyl-4-pyridinemethanol using whole cells of Candida parapsilosis","authors":"Saptarshi Ghosh, Linga Banoth, U. Banerjee","doi":"10.1515/boca-2015-0004","DOIUrl":"https://doi.org/10.1515/boca-2015-0004","url":null,"abstract":"Abstract A single-step synthesis of (R)-α-methyl- 4-pyridinemethanol from (RS)-α-methyl-4- pyridinemethanol by stereoinversion using whole cells of Candida parapsilosis is reported. Among the various strains of Candida species examined, C. parapsilosis demonstrated to have the best oxidoreductase system for stereoinversion of (RS)-α-methyl-4-pyridinemethanol. The effect of various physicochemical parameters on the stereoinversion process, were studied. Under optimized conditions approximately 97% enantiomeric excess of (R)-α-methyl-4-pyridinemethanol (eeR) was obtained with 99% yield was obtained. The optimized parameters were determined to be a substrate concentration of 5 mM, pH 8.0, 30°C incubation temperature, and a reaction time of 48 h. The reactions were also carried out in different organic solvents, and maximum stereoinversion was obtained in 1,4-dioxane with 78.4% eeR and 74.7% yield, which are lower than those in phosphate buffer. This whole cell catalysis for the preparation of (R)-α-methyl-4- pyridinemethanol is an example of a green, enantiopure synthesis of secondary alcohols. Graphical Abstract","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"8 1","pages":"59 - 66"},"PeriodicalIF":0.0,"publicationDate":"2015-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86034346","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 We review recent developments in the use of short peptides in the design of minimalistic biocatalysts focusing on ester hydrolysis. A number of designed peptide nanostructures are shown to have (modest) catalytic activity. Five features are discussed and illustrated by literature examples, including primary peptide sequence, nanosurfaces/scaffolds, binding pockets, multivalency and the presence of metal ions. Some of these are derived from natural enzymes, but others, such as multivalency of active sites on designed nanofibers, may give rise to new features not found in natural enzymes. Remarkably, it is shown that each of these design features give rise to similar rate enhancements in ester hydrolysis. Overall, there has been significant progress in the development of fundamental understanding of the factors that influence binding and activity in recent years, holding promise for increasingly rational design of peptide based biocatalysts.
{"title":"Short Peptides in Minimalistic Biocatalyst Design","authors":"K. Duncan, R. Ulijn","doi":"10.1515/boca-2015-0005","DOIUrl":"https://doi.org/10.1515/boca-2015-0005","url":null,"abstract":"Abstract We review recent developments in the use of short peptides in the design of minimalistic biocatalysts focusing on ester hydrolysis. A number of designed peptide nanostructures are shown to have (modest) catalytic activity. Five features are discussed and illustrated by literature examples, including primary peptide sequence, nanosurfaces/scaffolds, binding pockets, multivalency and the presence of metal ions. Some of these are derived from natural enzymes, but others, such as multivalency of active sites on designed nanofibers, may give rise to new features not found in natural enzymes. Remarkably, it is shown that each of these design features give rise to similar rate enhancements in ester hydrolysis. Overall, there has been significant progress in the development of fundamental understanding of the factors that influence binding and activity in recent years, holding promise for increasingly rational design of peptide based biocatalysts.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"20 6","pages":"67 - 81"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91441163","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 This paper addresses the effects of the concentration of lipases, temperature and solvent on the enzymatic acetylation of primary amines. (±)-Heptan-2-amine 1, (±)-4-phenylbutan-2-amine 2, (±)-1,2,3,4-tetrahydronaphthalen-1-amine 3 and (±)-2-methylcyclohexan-1-amine 4 were acetylated using 11 lipases to obtain amides under orbital shaking and microwave radiation. Under microwave radiation the same amines were acetylated only using the CALB. (±)-Heptan-2-amine 1 was subjected to kinetic resolution, under orbital shaking for 7 h employing CALB and ethyl acetate as acylating agent, and converted into (R)-N- (heptan-2-yl)acetamide 5 (c = 42%, 88% eep, hexane c = 52%, 81% eep, isopropyl ether; c = 40%, 65% eep, toluene). The reaction was fast (15 s) under microwave radiation in hexane and yielded acetamide 4 in high conversion (c = 91%), but without selectivity (5% eep).
{"title":"Biocatalytic Acetylation of Primary Amines by Lipases under Orbital Shaking and Microwave Radiation","authors":"Yara Jaqueline Kerber Araújo, A. Porto","doi":"10.1515/boca-2015-0003","DOIUrl":"https://doi.org/10.1515/boca-2015-0003","url":null,"abstract":"Abstract This paper addresses the effects of the concentration of lipases, temperature and solvent on the enzymatic acetylation of primary amines. (±)-Heptan-2-amine 1, (±)-4-phenylbutan-2-amine 2, (±)-1,2,3,4-tetrahydronaphthalen-1-amine 3 and (±)-2-methylcyclohexan-1-amine 4 were acetylated using 11 lipases to obtain amides under orbital shaking and microwave radiation. Under microwave radiation the same amines were acetylated only using the CALB. (±)-Heptan-2-amine 1 was subjected to kinetic resolution, under orbital shaking for 7 h employing CALB and ethyl acetate as acylating agent, and converted into (R)-N- (heptan-2-yl)acetamide 5 (c = 42%, 88% eep, hexane c = 52%, 81% eep, isopropyl ether; c = 40%, 65% eep, toluene). The reaction was fast (15 s) under microwave radiation in hexane and yielded acetamide 4 in high conversion (c = 91%), but without selectivity (5% eep).","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"189 1","pages":"49 - 58"},"PeriodicalIF":0.0,"publicationDate":"2015-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77551309","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}
Beatriz Vega, Beatriz Reyes, Paula Rodríguez, Wilson Sierra, David J. Gonzalez, P. Menéndez
Abstract This report describes the high yield biotransformation of 1,8-cineole by the strain Gymnopilus spectabilis 7423, a common fungus isolated from the Eucalyptus tree. The biotransformation was conducted under resting cell conditions and different parameters were tested in order to achieve up to 90% bioconversion. Only two regioisomers were detected, and they were identified as 3-α-hydroxy-1,8-cineole and 2-α-hydroxy-1,8- cineole obtained in a 82:8 ratio.
{"title":"3-Hydroxycineole bioproduction from 1,8-cineole using Gymnopilus spectabilis 7423 under resting cell conditions","authors":"Beatriz Vega, Beatriz Reyes, Paula Rodríguez, Wilson Sierra, David J. Gonzalez, P. Menéndez","doi":"10.1515/boca-2015-0002","DOIUrl":"https://doi.org/10.1515/boca-2015-0002","url":null,"abstract":"Abstract This report describes the high yield biotransformation of 1,8-cineole by the strain Gymnopilus spectabilis 7423, a common fungus isolated from the Eucalyptus tree. The biotransformation was conducted under resting cell conditions and different parameters were tested in order to achieve up to 90% bioconversion. Only two regioisomers were detected, and they were identified as 3-α-hydroxy-1,8-cineole and 2-α-hydroxy-1,8- cineole obtained in a 82:8 ratio.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"203 1","pages":"44 - 48"},"PeriodicalIF":0.0,"publicationDate":"2015-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77019618","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}
K. Salcedo, Eduardo Torres-Ramírez, Iliana Haces, M. Ayala
Abstract Chloroperoxidase from Caldariomyces fumago was immobilized in Eupergit® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.
{"title":"Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase","authors":"K. Salcedo, Eduardo Torres-Ramírez, Iliana Haces, M. Ayala","doi":"10.1515/boca-2015-0001","DOIUrl":"https://doi.org/10.1515/boca-2015-0001","url":null,"abstract":"Abstract Chloroperoxidase from Caldariomyces fumago was immobilized in Eupergit® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"179 1","pages":"33 - 43"},"PeriodicalIF":0.0,"publicationDate":"2015-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76615942","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 focus of this review paper is on the design and implementation of smart ‘Sense-and-Treat’ systems using enzyme-biocatalytic systems. These systems were used to perform biomolecular computing and they were functionally integrated with signal responsive materials aiming towards their biomedical use. Electrode interfaces, functionalized with signal-responsive materials, find applications in biocomputing, biosensing, and, specifically, triggered release of bioactive substances. ‘Sense-and-Treat’ systems require multiple components working together, including biosensors, actuators, and filters, in order to achieve closed-loop and autonomous operation. In general, biochemical logic networks were developed to process single biochemical or chemical inputs as well as multiple inputs, responding to nonphysiological (for concept demonstration purposes) and physiological signals (for injury detection or diagnosis). Actuation of drug-mimicking release was performed using the responsive material iron-cross-linked alginate with entrapped biomolecular species, responding to physical, chemical or biochemical signals.
{"title":"Biocomputing, Biosensing and Bioactuation Based on Enzyme Biocatalyzed Reactions","authors":"S. Mailloux, E. Katz","doi":"10.2478/boca-2014-0002","DOIUrl":"https://doi.org/10.2478/boca-2014-0002","url":null,"abstract":"Abstract The focus of this review paper is on the design and implementation of smart ‘Sense-and-Treat’ systems using enzyme-biocatalytic systems. These systems were used to perform biomolecular computing and they were functionally integrated with signal responsive materials aiming towards their biomedical use. Electrode interfaces, functionalized with signal-responsive materials, find applications in biocomputing, biosensing, and, specifically, triggered release of bioactive substances. ‘Sense-and-Treat’ systems require multiple components working together, including biosensors, actuators, and filters, in order to achieve closed-loop and autonomous operation. In general, biochemical logic networks were developed to process single biochemical or chemical inputs as well as multiple inputs, responding to nonphysiological (for concept demonstration purposes) and physiological signals (for injury detection or diagnosis). Actuation of drug-mimicking release was performed using the responsive material iron-cross-linked alginate with entrapped biomolecular species, responding to physical, chemical or biochemical signals.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"43 1","pages":"13 - 32"},"PeriodicalIF":0.0,"publicationDate":"2014-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77404707","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 Lipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry. Graphical Abstract
{"title":"Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C","authors":"Daniele Spinelli, S. Coppi, R. Basosi, R. Pogni","doi":"10.2478/boca-2014-0001","DOIUrl":"https://doi.org/10.2478/boca-2014-0001","url":null,"abstract":"Abstract Lipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry. Graphical Abstract","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"70 1","pages":"1 - 12"},"PeriodicalIF":0.0,"publicationDate":"2014-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77197099","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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