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Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles
Rhodococcus rhodochrous NCIMB 11216 produced nitrile hydratase (320 nkat mg of protein(−1)) and amidase activity (38.4 nkat mg of protein(−1)) when grown on a medium containing propionitrile. These enzymes were able to hydrolyze nitrile groups of both granular polyacrylonitriles (PAN) and acrylic fi...
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American Society for Microbiology
2000
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pubmed-920342002-09-12 Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles Tauber, M. M. Cavaco-Paulo, A. Robra, K.-H. Gübitz, G. M. Appl Environ Microbiol Enzymology and Protein Engineering Rhodococcus rhodochrous NCIMB 11216 produced nitrile hydratase (320 nkat mg of protein(−1)) and amidase activity (38.4 nkat mg of protein(−1)) when grown on a medium containing propionitrile. These enzymes were able to hydrolyze nitrile groups of both granular polyacrylonitriles (PAN) and acrylic fibers. Nitrile groups of PAN40 (molecular mass, 40 kDa) and PAN190 (molecular mass, 190 kDa) were converted into the corresponding carbonic acids to 1.8 and 1.0%, respectively. In contrast, surfacial nitrile groups of acrylic fibers were only converted to the corresponding amides. X-ray photoelectron spectroscopy analysis showed that 16% of the surfacial nitrile groups were hydrolyzed by the R. rhodochrous enzymes. Due to the enzymatic modification, the acrylic fibers became more hydrophilic and thus, adsorption of dyes was enhanced. This was indicated by a 15% increase in the staining level (K/S value) for C.I. Basic Blue 9. American Society for Microbiology 2000-04 /pmc/articles/PMC92034/ /pubmed/10742253 Text en Copyright © 2000, American Society for Microbiology |
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US National Library of Medicine |
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PubMed Central |
| language |
en |
| format |
Article |
| topic |
Enzymology and Protein Engineering |
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Enzymology and Protein Engineering Tauber, M. M. Cavaco-Paulo, A. Robra, K.-H. Gübitz, G. M. Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| description |
Rhodococcus rhodochrous NCIMB 11216 produced nitrile hydratase (320 nkat mg of protein(−1)) and amidase activity (38.4 nkat mg of protein(−1)) when grown on a medium containing propionitrile. These enzymes were able to hydrolyze nitrile groups of both granular polyacrylonitriles (PAN) and acrylic fibers. Nitrile groups of PAN40 (molecular mass, 40 kDa) and PAN190 (molecular mass, 190 kDa) were converted into the corresponding carbonic acids to 1.8 and 1.0%, respectively. In contrast, surfacial nitrile groups of acrylic fibers were only converted to the corresponding amides. X-ray photoelectron spectroscopy analysis showed that 16% of the surfacial nitrile groups were hydrolyzed by the R. rhodochrous enzymes. Due to the enzymatic modification, the acrylic fibers became more hydrophilic and thus, adsorption of dyes was enhanced. This was indicated by a 15% increase in the staining level (K/S value) for C.I. Basic Blue 9. |
| author |
Tauber, M. M. Cavaco-Paulo, A. Robra, K.-H. Gübitz, G. M. |
| author_facet |
Tauber, M. M. Cavaco-Paulo, A. Robra, K.-H. Gübitz, G. M. |
| author_sort |
Tauber, M. M. |
| title |
Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| title_short |
Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| title_full |
Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| title_fullStr |
Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| title_full_unstemmed |
Nitrile Hydratase and Amidase from Rhodococcus rhodochrous Hydrolyze Acrylic Fibers and Granular Polyacrylonitriles |
| title_sort |
nitrile hydratase and amidase from rhodococcus rhodochrous hydrolyze acrylic fibers and granular polyacrylonitriles |
| publisher |
American Society for Microbiology |
| publisher_facet |
American Society for Microbiology |
| publishDate |
2000 |
| url |
https://ncbi.nlm.nih.gov/pmc/articles/PMC92034/ https://ncbi.nlm.nih.gov/pubmed/10742253 |
| _version_ |
1759029656965611520 |