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Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time

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dc.contributor.author Frederick, J
dc.contributor.author Brady, D
dc.contributor.author Weber, B
dc.contributor.author Sewell, T
dc.date.accessioned 2009-04-14T12:29:13Z
dc.date.available 2009-04-14T12:29:13Z
dc.date.issued 2008-07
dc.identifier.citation Frederick, J. 2008. Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time. 46th Conference of the Microscopy Society of Southern Africa. University of Botswana, Gaborone, Botswana, 21-25 July 2008, pp 1 en
dc.identifier.uri http://hdl.handle.net/10204/3307
dc.description 46th Conference of the Microscopy Society of Southern Africa. University of Botswana, Gaborone, Botswana, 21-25 July 2008 en
dc.description.abstract A versatile nitrile-degrading bacterium, Rhodococcus rhodochrous ATCCBAA-870, was isolated through enrichment culturing of soil samples from Johannesburg, South Africa. The researchers have previously shown that Rhodococcus rhodochrous ATCCBAA-870 possesses nitrile-hydrolysing enzymes capable of metabolising a wide range of aliphatic and aromatic nitriles and amides. The biocatalyst expressed a two enzyme system with sequential nitrile-converting activity. Nitrilase enzymes catalyse the hydrolysis of a nitrile into its corresponding carboxylic acid and ammonia, and have become important industrial enzymes as a result of the products they afford. Successful commercial examples of nitrile bioconversion include production of nicotinic acid and acrylic acid. Both experimental and results are shown in the poster en
dc.language.iso en en
dc.publisher 46th Conference of the Microscopy Society of Southern Africa en
dc.subject Nitrilase enzymes en
dc.subject Rhodococcus rhodochrous ATCC BAA-870 en
dc.subject Carboxylic acid en
dc.subject Fibre formation en
dc.subject Microscopy Society of Southern Africa en
dc.title Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time en
dc.type Conference Presentation en
dc.identifier.apacitation Frederick, J., Brady, D., Weber, B., & Sewell, T. (2008). Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time. 46th Conference of the Microscopy Society of Southern Africa. http://hdl.handle.net/10204/3307 en_ZA
dc.identifier.chicagocitation Frederick, J, D Brady, B Weber, and T Sewell. "Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time." (2008): http://hdl.handle.net/10204/3307 en_ZA
dc.identifier.vancouvercitation Frederick J, Brady D, Weber B, Sewell T, Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time; 46th Conference of the Microscopy Society of Southern Africa; 2008. http://hdl.handle.net/10204/3307 . en_ZA
dc.identifier.ris TY - Conference Presentation AU - Frederick, J AU - Brady, D AU - Weber, B AU - Sewell, T AB - A versatile nitrile-degrading bacterium, Rhodococcus rhodochrous ATCCBAA-870, was isolated through enrichment culturing of soil samples from Johannesburg, South Africa. The researchers have previously shown that Rhodococcus rhodochrous ATCCBAA-870 possesses nitrile-hydrolysing enzymes capable of metabolising a wide range of aliphatic and aromatic nitriles and amides. The biocatalyst expressed a two enzyme system with sequential nitrile-converting activity. Nitrilase enzymes catalyse the hydrolysis of a nitrile into its corresponding carboxylic acid and ammonia, and have become important industrial enzymes as a result of the products they afford. Successful commercial examples of nitrile bioconversion include production of nicotinic acid and acrylic acid. Both experimental and results are shown in the poster DA - 2008-07 DB - ResearchSpace DP - CSIR KW - Nitrilase enzymes KW - Rhodococcus rhodochrous ATCC BAA-870 KW - Carboxylic acid KW - Fibre formation KW - Microscopy Society of Southern Africa LK - https://researchspace.csir.co.za PY - 2008 T1 - Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time TI - Nitrilase from rhodococcus rhodochrous ATCC BAA-870: fibre formation over time UR - http://hdl.handle.net/10204/3307 ER - en_ZA


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