Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21
An agar-degrading bacterium, designated as Pseudoalteromonas sp. NJ21, was isolated from an Antarctic sediment sample. The agarase gene aga1161 from Pseudoalteromonas sp. NJ21 consisting of a 2 382-bp coding region was cloned. The gene encodes a 793-amino acids protein and was found to possess chara...
Published in: | Chinese Journal of Oceanology and Limnology |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/25403 2023-05-15T13:40:37+02:00 Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 Li Jiang Sha Yujie 2015-03-01 http://ir.qdio.ac.cn/handle/337002/25403 https://doi.org/10.1007/s00343-015-4072-3 英语 eng CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY http://ir.qdio.ac.cn/handle/337002/25403 doi:10.1007/s00343-015-4072-3 Antarctic Bacterium Pseudoalteromonas Agarase Expression Enzymatic Characterization Article 期刊论文 2015 ftchinacasciocas https://doi.org/10.1007/s00343-015-4072-3 2022-06-27T05:36:55Z An agar-degrading bacterium, designated as Pseudoalteromonas sp. NJ21, was isolated from an Antarctic sediment sample. The agarase gene aga1161 from Pseudoalteromonas sp. NJ21 consisting of a 2 382-bp coding region was cloned. The gene encodes a 793-amino acids protein and was found to possess characteristic features of the Glyco_hydro_42 family. The recombinant agarase (rAga1161) was overexpressed in Escherichia coli and purified as a fusion protein. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant agarase were 30-40A degrees C and 8.0, respectively. rAga1161 was found to maintain as much as 80% of its maximum activity at 10A degrees C, which is typical of a coldadapted enzyme. The pattern of agar hydrolysis demonstrated that the enzyme is an beta-agarase, producing neoagarobiose (NA2) as the final main product. Furthermore, this work is the first proof of an agarolytic activity in Antarctic bacteria and these results indicate the potential for the Antarctic agarase as a catalyst in medicine, food and cosmetic industries. Article in Journal/Newspaper Antarc* Antarctic Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Antarctic The Antarctic Chinese Journal of Oceanology and Limnology 33 2 319 327 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Antarctic Bacterium Pseudoalteromonas Agarase Expression Enzymatic Characterization |
spellingShingle |
Antarctic Bacterium Pseudoalteromonas Agarase Expression Enzymatic Characterization Li Jiang Sha Yujie Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
topic_facet |
Antarctic Bacterium Pseudoalteromonas Agarase Expression Enzymatic Characterization |
description |
An agar-degrading bacterium, designated as Pseudoalteromonas sp. NJ21, was isolated from an Antarctic sediment sample. The agarase gene aga1161 from Pseudoalteromonas sp. NJ21 consisting of a 2 382-bp coding region was cloned. The gene encodes a 793-amino acids protein and was found to possess characteristic features of the Glyco_hydro_42 family. The recombinant agarase (rAga1161) was overexpressed in Escherichia coli and purified as a fusion protein. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant agarase were 30-40A degrees C and 8.0, respectively. rAga1161 was found to maintain as much as 80% of its maximum activity at 10A degrees C, which is typical of a coldadapted enzyme. The pattern of agar hydrolysis demonstrated that the enzyme is an beta-agarase, producing neoagarobiose (NA2) as the final main product. Furthermore, this work is the first proof of an agarolytic activity in Antarctic bacteria and these results indicate the potential for the Antarctic agarase as a catalyst in medicine, food and cosmetic industries. |
format |
Article in Journal/Newspaper |
author |
Li Jiang Sha Yujie |
author_facet |
Li Jiang Sha Yujie |
author_sort |
Li Jiang |
title |
Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
title_short |
Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
title_full |
Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
title_fullStr |
Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
title_full_unstemmed |
Expression and enzymatic characterization of a cold-adapted beta-agarase from Antarctic bacterium Pseudoalteromonas sp NJ21 |
title_sort |
expression and enzymatic characterization of a cold-adapted beta-agarase from antarctic bacterium pseudoalteromonas sp nj21 |
publishDate |
2015 |
url |
http://ir.qdio.ac.cn/handle/337002/25403 https://doi.org/10.1007/s00343-015-4072-3 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY http://ir.qdio.ac.cn/handle/337002/25403 doi:10.1007/s00343-015-4072-3 |
op_doi |
https://doi.org/10.1007/s00343-015-4072-3 |
container_title |
Chinese Journal of Oceanology and Limnology |
container_volume |
33 |
container_issue |
2 |
container_start_page |
319 |
op_container_end_page |
327 |
_version_ |
1766137527710777344 |