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Yasuhisa Asano - One of the best experts on this subject based on the ideXlab platform.
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Chapter 9 – Enzymes in the Aldoxime–Nitrile Pathway: Versatile Tools in Biocatalysis
Future Directions in Biocatalysis, 2017Co-Authors: Yasuhisa Asano, Seiji OkazakiAbstract:The discovery and exploitation of Enzymes in the aldoxime–nitrile pathway: nitrile hydratase, amidase, nitrilase, aldoxime dehydratase, etc. are described in this chapter, along with the use of methodologies, such as organic chemistry, microbial screening by enrichment and acclimation culture techniques, Enzyme Purification, gene cloning, molecular screening by polymerase chain reaction, etc.
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opine dehydrogenase secondary amine dicarboxylic acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion Bibliography Keywords: amino acid dehydrogenase; enzymatic synthesis; Enzyme Purification and properties; opine compound; opine dehydrogenase; secondary amine dicarboxylic acid
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Encyclopedia of Industrial Biotechnology - Opine Dehydrogenase, Secondary Amine Dicarboxylic Acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion References Keywords: amino acid dehydrogenase; enzymatic synthesis; Enzyme Purification and properties; opine compound; opine dehydrogenase; secondary amine dicarboxylic acid
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Enzymes in aldoxime-nitrile pathway: versatile tools in biocatalysis
Future Directions in Biocatalysis, 2007Co-Authors: Yasuhisa AsanoAbstract:Abstract The discovery and exploitation of Enzymes in aldoxime–nitrile pathway: nitrile hydratase, amidase, nitrilase, aldoxime dehydratase, etc., are shown along with the use of methodologies, such as organic chemistry, microbial screening by enrichment and acclimation culture techniques, Enzyme Purification, gene cloning, molecular screening by polymerase chain reaction (PCR).
Yasuo Kato - One of the best experts on this subject based on the ideXlab platform.
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opine dehydrogenase secondary amine dicarboxylic acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion Bibliography Keywords: amino acid dehydrogenase; enzymatic synthesis; Enzyme Purification and properties; opine compound; opine dehydrogenase; secondary amine dicarboxylic acid
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Encyclopedia of Industrial Biotechnology - Opine Dehydrogenase, Secondary Amine Dicarboxylic Acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion References Keywords: amino acid dehydrogenase; enzymatic synthesis; Enzyme Purification and properties; opine compound; opine dehydrogenase; secondary amine dicarboxylic acid
Elias Basile Tambourgi - One of the best experts on this subject based on the ideXlab platform.
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expanded bed adsorption of an alkaline lipase from pseudomona cepacia
Journal of Chromatography B, 2009Co-Authors: Giovana Da Silva Padilha, Jose Carlos Curvelosantana, Ranulfo Monte Alegre, Elias Basile TambourgiAbstract:Abstract An extracellular lipase was isolated from Pseudomona cepacia by expanded bed adsorption on an Amberlite 410 ion-exchange resin. Enzyme characterization and hydrodynamic study of a chromatography column were done. Enzyme Purification was done at three condition of expanded bed height ( H ): at one and half (6 cm), at two (8 cm) and at three (12 cm) times the fixed bed height ( H 0 = 4 cm). The results showed that the experimental data was fitted to the Richardson and Zaki equation, and the comparison between the experimental and calculated terminal velocities showed low relative error. In Enzyme Purification for better condition, a Purification factor of about 80 times was found at 6 cm of expanded bed height, or 1.5 times of expansion degree. Purified lipase had an optimal pH and a temperature of 8 and 37 °C, respectively.
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Expanded bed adsorption of an alkaline lipase from Pseudomona cepacia.
Journal of chromatography. B Analytical technologies in the biomedical and life sciences, 2009Co-Authors: Giovana Da Silva Padilha, José Carlos Curvelo-santana, Ranulfo Monte Alegre, Elias Basile TambourgiAbstract:An extracellular lipase was isolated from Pseudomona cepacia by expanded bed adsorption on an Amberlite 410 ion-exchange resin. Enzyme characterization and hydrodynamic study of a chromatography column were done. Enzyme Purification was done at three condition of expanded bed height (H): at one and half (6cm), at two (8cm) and at three (12cm) times the fixed bed height (H(0)=4cm). The results showed that the experimental data was fitted to the Richardson and Zaki equation, and the comparison between the experimental and calculated terminal velocities showed low relative error. In Enzyme Purification for better condition, a Purification factor of about 80 times was found at 6cm of expanded bed height, or 1.5 times of expansion degree. Purified lipase had an optimal pH and a temperature of 8 and 37 degrees C, respectively.
Folke Tjerneld - One of the best experts on this subject based on the ideXlab platform.
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Application of temperature-induced phase partitioning at ambient temperature for Enzyme Purification.
Journal of Chromatography A, 1994Co-Authors: Patricia Alred, Antoni Kozlowski, J M Harris, Folke TjerneldAbstract:Aqueous two-phase partition and temperature-induced phase separation using a non-ionic, random copolymer composed of 20% ethylene oxide, 80% propylene oxide (EO20 PO80) has been used for Purification of glucose-6-phosphate dehydrogenase, hexokinase and 3-phosphoglycerate kinase from bakers' yeast. This EO20PO80 copolymer has a cloud point of 18 degrees C, at which temperature it phase separates from water. Enzymes were first partitioned at 4 degrees C in an initial EO20PO80-dextran T500 aqueous two-phase system. This system had an upper copolymer-rich phase and a lower dextran-rich phase. After phase separation had occurred the upper EO20PO80-rich phase was removed and placed at 24 degrees C. This resulted in formation of a new two-phase system with an upper water phase and a lower phase containing 98% copolymer and 2% water. Enzymes were recovered exclusively in upper water phase leaving a polymer-rich lower phase free of contamination. The phase diagram for the system EO20PO80 and dextran T500 at 4 degrees C has been determined.
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Enzyme Purification using temperature-induced phase formation.
Bioseparation, 1991Co-Authors: P A Harris, Gunnar Karlström, Folke TjerneldAbstract:A new type of aqueous two-phase system composed of an ethylene oxide and propylene oxide random co-polymer, UCON 50-HB-5100, as the upper phase polymer and either dextran or hydroxypropyl starch as the lower phase polymer has been characterized and used to purify 3-phosphoglycerate kinase (EC 2.7.2.3) and hexokinase (EC 2.7.1.1) from bakers' yeast. The UCON 50-HB-5100 polymer has a cloud point of 55 degrees C at which temperature it phase separates from water. This cloud point can be lowered to 40 degrees C by the addition of 0.2 M sodium sulfate salt. The low cloud point of this UCON polymer makes it possible to obtain the target Enzymes in a water and buffer solution, and to recover and recycle the UCON 50-HB-5100 polymer. The phase diagrams for the systems UCON 50-HB-5100/Dextran T500 and UCON 50-HB-5100/hydroxypropyl starch have been determined. Yeast homogenate was first partitioned in a system composed of a top phase containing UCON 50-HB-5100 and a bottom phase containing either dextran or hydroxypropyl starch. The top phase containing the Enzyme free of cell debris was removed and the temperature increased above the cloud point of the UCON until a new two phase system composed of water as the top phase and a concentrated liquid UCON 50-HB-5100 bottom phase was formed. The water phase containing the Enzyme was removed and the bottom phase containing the UCON 50-HB-5100 could be recycled to perform a second extraction.
Lawrence P Wackett - One of the best experts on this subject based on the ideXlab platform.
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atrazine chlorohydrolase from pseudomonas sp strain adp gene sequence Enzyme Purification and protein characterization
Journal of Bacteriology, 1996Co-Authors: Mervyn L De Souza, Michael J Sadowsky, Lawrence P WackettAbstract:Pseudomonas sp. strain ADP metabolizes atrazine to carbon dioxide and ammonia via the intermediate hydroxyatrazine. The genetic potential to produce hydroxyatrazine was previously attributed to a 1.9-kb AvaI DNA fragment from strain ADP (M. L. de Souza, L. P. Wackett, K. L. Boundy-Mills, R. T. Mandelbaum, and M. J. Sadowsky, Appl. Environ. Microbiol. 61:3373-3378, 1995). In this study, sequence analysis of the 1.9-kb AvaI fragment indicated that a single open reading frame, atzA, encoded an activity transforming atrazine to hydroxyatrazine. The open reading frame for the chlorohydrolase was determined by sequencing to be 1,419 nucleotides and encodes a 473-amino-acid protein with a predicted subunit molecular weight of 52,421. The deduced amino acid sequence matched the first 10 amino acids determined by protein microsequencing. The protein AtzA was purified to homogeneity by ammonium sulfate precipitation and anion-exchange chromatography. The subunit and holoEnzyme molecular weights were 60,000 and 245,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography, respectively. The purified Enzyme in H2(18)O yielded [18O]hydroxyatrazine, indicating that AtzA is a chlorohydrolase and not an oxygenase. The most related protein sequence in GenBank was that of TrzA, 41% identity, from Rhodococcus corallinus NRRL B-15444R. TrzA catalyzes the deamination of melamine and the dechlorination of deethylatrazine and desisopropylatrazine but is not active with atrazine. AtzA catalyzes the dechlorination of atrazine, simazine, and desethylatrazine but is not active with melamine, terbutylazine, or desethyldesisopropylatrazine. Our results indicate that AtzA is a novel atrazine-dechlorinating Enzyme with fairly restricted substrate specificity and contributes to the microbial hydrolysis of atrazine to hydroxyatrazine in soils and groundwater.