Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates
An agarase gene (aga1904) that codes a protein with 640 amino acids was obtained from the metagenomic library of macroalgae-associated bacteria collected from King George Island, Antarctica. Gene aga1904 was expressed in Escherichia coli BL21 (DE3) and recombinant Aga1904 was purified by His Bind Pu...
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Online Access: | http://ir.qdio.ac.cn/handle/337002/180623 http://ir.qdio.ac.cn/handle/337002/180624 https://doi.org/10.3389/fmicb.2022.972272 |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/180624 2023-05-15T13:53:42+02:00 Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates Gu, Xiaoqian Zhao, Luying Tan, Jiaojiao Zhang, Qian Fu, Liping Li, Jiang 2022-09-02 http://ir.qdio.ac.cn/handle/337002/180623 http://ir.qdio.ac.cn/handle/337002/180624 https://doi.org/10.3389/fmicb.2022.972272 英语 eng FRONTIERS MEDIA SA FRONTIERS IN MICROBIOLOGY http://ir.qdio.ac.cn/handle/337002/180623 http://ir.qdio.ac.cn/handle/337002/180624 doi:10.3389/fmicb.2022.972272 metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Microbiology 期刊论文 2022 ftchinacasciocas https://doi.org/10.3389/fmicb.2022.972272 2023-01-16T16:14:28Z An agarase gene (aga1904) that codes a protein with 640 amino acids was obtained from the metagenomic library of macroalgae-associated bacteria collected from King George Island, Antarctica. Gene aga1904 was expressed in Escherichia coli BL21 (DE3) and recombinant Aga1904 was purified by His Bind Purification kit. The optimal temperature and pH for the activity of Aga1904 were 50 degrees C and 6.0, respectively. Fe3+ and Cu2+ significantly inhibited the activity of Aga1904. The V-max and K-m values of recombinant Aga1904 were 108.70 mg/ml min and 6.51 mg/ml, respectively. The degradation products of Aga1904 against agarose substrate were mainly neoagarobiose, neoagarotetraose, and neoagarohexaose analyzed by thin layer chromatography. The cellular immunoassay of enzymatic hydrolysates was subsequently carried out, and the results showed that agaro-oligosaccharides dominated by neoagarobiose significantly inhibited key pro-inflammatory markers including, nitric oxide (NO), interleukins 6 (IL-6), and tumor necrosis factor alpha (TNF-alpha). This work provides a promising candidate for development recombinant industrial enzyme to prepare agaro-oligosaccharides, and paved up a new path for the exploitation of natural anti-inflammatory agent in the future. Report Antarc* Antarctic Antarctica King George Island Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Antarctic King George Island Frontiers in Microbiology 13 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Microbiology |
spellingShingle |
metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Microbiology Gu, Xiaoqian Zhao, Luying Tan, Jiaojiao Zhang, Qian Fu, Liping Li, Jiang Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
topic_facet |
metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Microbiology |
description |
An agarase gene (aga1904) that codes a protein with 640 amino acids was obtained from the metagenomic library of macroalgae-associated bacteria collected from King George Island, Antarctica. Gene aga1904 was expressed in Escherichia coli BL21 (DE3) and recombinant Aga1904 was purified by His Bind Purification kit. The optimal temperature and pH for the activity of Aga1904 were 50 degrees C and 6.0, respectively. Fe3+ and Cu2+ significantly inhibited the activity of Aga1904. The V-max and K-m values of recombinant Aga1904 were 108.70 mg/ml min and 6.51 mg/ml, respectively. The degradation products of Aga1904 against agarose substrate were mainly neoagarobiose, neoagarotetraose, and neoagarohexaose analyzed by thin layer chromatography. The cellular immunoassay of enzymatic hydrolysates was subsequently carried out, and the results showed that agaro-oligosaccharides dominated by neoagarobiose significantly inhibited key pro-inflammatory markers including, nitric oxide (NO), interleukins 6 (IL-6), and tumor necrosis factor alpha (TNF-alpha). This work provides a promising candidate for development recombinant industrial enzyme to prepare agaro-oligosaccharides, and paved up a new path for the exploitation of natural anti-inflammatory agent in the future. |
format |
Report |
author |
Gu, Xiaoqian Zhao, Luying Tan, Jiaojiao Zhang, Qian Fu, Liping Li, Jiang |
author_facet |
Gu, Xiaoqian Zhao, Luying Tan, Jiaojiao Zhang, Qian Fu, Liping Li, Jiang |
author_sort |
Gu, Xiaoqian |
title |
Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
title_short |
Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
title_full |
Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
title_fullStr |
Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
title_full_unstemmed |
Characterization of a novel beta-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
title_sort |
characterization of a novel beta-agarase from antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates |
publisher |
FRONTIERS MEDIA SA |
publishDate |
2022 |
url |
http://ir.qdio.ac.cn/handle/337002/180623 http://ir.qdio.ac.cn/handle/337002/180624 https://doi.org/10.3389/fmicb.2022.972272 |
geographic |
Antarctic King George Island |
geographic_facet |
Antarctic King George Island |
genre |
Antarc* Antarctic Antarctica King George Island |
genre_facet |
Antarc* Antarctic Antarctica King George Island |
op_relation |
FRONTIERS IN MICROBIOLOGY http://ir.qdio.ac.cn/handle/337002/180623 http://ir.qdio.ac.cn/handle/337002/180624 doi:10.3389/fmicb.2022.972272 |
op_doi |
https://doi.org/10.3389/fmicb.2022.972272 |
container_title |
Frontiers in Microbiology |
container_volume |
13 |
_version_ |
1766259075936419840 |