Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources
Hydantoin cleaving bacterial isolates were recovered from terrestrial soil samples originating from different geographic sources (Antarctica, South Africa and China) using culture-based screening methods (selective agar plates and shake flask cultures supplemented with hydantoins). Thirty-two bacter...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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Online Access: | https://kar.kent.ac.uk/7337/ https://doi.org/10.1016/j.molcatb.2006.01.017 |
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ftkentuniv:oai:kar.kent.ac.uk:7337 2024-06-09T07:39:27+00:00 Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources Durr, R. Vielhauer, O. Burton, S. G. Cowan, D. A. Punal, A. Brandao, P. F. B. Bull, A. T. Syldatk, C. 2006-05 https://kar.kent.ac.uk/7337/ https://doi.org/10.1016/j.molcatb.2006.01.017 unknown Elsevier Durr, R., Vielhauer, O., Burton, S. G., Cowan, D. A., Punal, A., Brandao, P. F. B., Bull, A. T., Syldatk, C. (2006) Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources. Journal of Molecular Catalysis B-Enzymatic, 39 (1-4). pp. 160-165. ISSN 1381-1177. (doi:10.1016/j.molcatb.2006.01.017 <https://doi.org/10.1016/j.molcatb.2006.01.017>) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:7337 </7337>) Q Science Article PeerReviewed 2006 ftkentuniv https://doi.org/10.1016/j.molcatb.2006.01.017 2024-05-16T04:17:29Z Hydantoin cleaving bacterial isolates were recovered from terrestrial soil samples originating from different geographic sources (Antarctica, South Africa and China) using culture-based screening methods (selective agar plates and shake flask cultures supplemented with hydantoins). Thirty-two bacterial isolates possessing the capability to transform the model substrates benzylhydantoin and dihydrouracil to the corresponding N-carbamoyl-amino acids were successfully cultured. Amplification and sequencing of the 16S rDNA revealed that the isolates belonged to the genera Arthrobacter, Burkholderia, Bacillus, Delftia, Enterobacter, Flavobacterium, Ochrobactrum, Pseudomonas and Stenotrophomonas, with one isolate assigned to the family Microbacteriacae. We have shown that microorganisms with hydantoinase activity are: (i) distributed in various geographically distinct environmental habitats, (ii) distributed worldwide and (iii) found in certain bacterial genera. Furthermore, we have demonstrated the presence of hydantoinase activity in genera in which hydantoinase activity has not previously been reported. Article in Journal/Newspaper Antarc* Antarctica University of Kent: KAR - Kent Academic Repository Journal of Molecular Catalysis B: Enzymatic 39 1-4 160 165 |
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University of Kent: KAR - Kent Academic Repository |
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ftkentuniv |
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unknown |
topic |
Q Science |
spellingShingle |
Q Science Durr, R. Vielhauer, O. Burton, S. G. Cowan, D. A. Punal, A. Brandao, P. F. B. Bull, A. T. Syldatk, C. Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
topic_facet |
Q Science |
description |
Hydantoin cleaving bacterial isolates were recovered from terrestrial soil samples originating from different geographic sources (Antarctica, South Africa and China) using culture-based screening methods (selective agar plates and shake flask cultures supplemented with hydantoins). Thirty-two bacterial isolates possessing the capability to transform the model substrates benzylhydantoin and dihydrouracil to the corresponding N-carbamoyl-amino acids were successfully cultured. Amplification and sequencing of the 16S rDNA revealed that the isolates belonged to the genera Arthrobacter, Burkholderia, Bacillus, Delftia, Enterobacter, Flavobacterium, Ochrobactrum, Pseudomonas and Stenotrophomonas, with one isolate assigned to the family Microbacteriacae. We have shown that microorganisms with hydantoinase activity are: (i) distributed in various geographically distinct environmental habitats, (ii) distributed worldwide and (iii) found in certain bacterial genera. Furthermore, we have demonstrated the presence of hydantoinase activity in genera in which hydantoinase activity has not previously been reported. |
format |
Article in Journal/Newspaper |
author |
Durr, R. Vielhauer, O. Burton, S. G. Cowan, D. A. Punal, A. Brandao, P. F. B. Bull, A. T. Syldatk, C. |
author_facet |
Durr, R. Vielhauer, O. Burton, S. G. Cowan, D. A. Punal, A. Brandao, P. F. B. Bull, A. T. Syldatk, C. |
author_sort |
Durr, R. |
title |
Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
title_short |
Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
title_full |
Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
title_fullStr |
Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
title_full_unstemmed |
Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
title_sort |
distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources |
publisher |
Elsevier |
publishDate |
2006 |
url |
https://kar.kent.ac.uk/7337/ https://doi.org/10.1016/j.molcatb.2006.01.017 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Durr, R., Vielhauer, O., Burton, S. G., Cowan, D. A., Punal, A., Brandao, P. F. B., Bull, A. T., Syldatk, C. (2006) Distribution of hydantoinase activity in bacterial isolates from geographically distinct environmental sources. Journal of Molecular Catalysis B-Enzymatic, 39 (1-4). pp. 160-165. ISSN 1381-1177. (doi:10.1016/j.molcatb.2006.01.017 <https://doi.org/10.1016/j.molcatb.2006.01.017>) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:7337 </7337>) |
op_doi |
https://doi.org/10.1016/j.molcatb.2006.01.017 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
39 |
container_issue |
1-4 |
container_start_page |
160 |
op_container_end_page |
165 |
_version_ |
1801379650842132480 |