Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc
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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ftfrontimediafig:oai:figshare.com:article/20783509 2024-09-15T17:43:19+00:00 Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc Xiaoqian Gu Luying Zhao Jiaojiao Tan Qian Zhang Liping Fu Jiang Li 2022-09-02T04:25:17Z https://doi.org/10.3389/fmicb.2022.972272.s001 https://figshare.com/articles/dataset/Data_Sheet_1_Characterization_of_a_novel_-agarase_from_Antarctic_macroalgae-associated_bacteria_metagenomic_library_and_anti-inflammatory_activity_of_the_enzymatic_hydrolysates_doc/20783509 unknown doi:10.3389/fmicb.2022.972272.s001 https://figshare.com/articles/dataset/Data_Sheet_1_Characterization_of_a_novel_-agarase_from_Antarctic_macroalgae-associated_bacteria_metagenomic_library_and_anti-inflammatory_activity_of_the_enzymatic_hydrolysates_doc/20783509 CC BY 4.0 Microbiology Microbial Genetics Microbial Ecology Mycology metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Dataset 2022 ftfrontimediafig https://doi.org/10.3389/fmicb.2022.972272.s001 2024-08-19T06:19:49Z 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°C and 6.0, respectively. Fe 3+ and Cu 2+ 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 α (TNF-α). 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. Dataset Antarc* Antarctic Antarctica King George Island Frontiers: Figshare |
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Open Polar |
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Frontiers: Figshare |
op_collection_id |
ftfrontimediafig |
language |
unknown |
topic |
Microbiology Microbial Genetics Microbial Ecology Mycology metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory |
spellingShingle |
Microbiology Microbial Genetics Microbial Ecology Mycology metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory Xiaoqian Gu Luying Zhao Jiaojiao Tan Qian Zhang Liping Fu Jiang Li Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
topic_facet |
Microbiology Microbial Genetics Microbial Ecology Mycology metagenomic agarase biochemical characterization agaro-oligosaccharides anti-inflammatory |
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°C and 6.0, respectively. Fe 3+ and Cu 2+ 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 α (TNF-α). 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 |
Dataset |
author |
Xiaoqian Gu Luying Zhao Jiaojiao Tan Qian Zhang Liping Fu Jiang Li |
author_facet |
Xiaoqian Gu Luying Zhao Jiaojiao Tan Qian Zhang Liping Fu Jiang Li |
author_sort |
Xiaoqian Gu |
title |
Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
title_short |
Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
title_full |
Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
title_fullStr |
Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
title_full_unstemmed |
Data_Sheet_1_Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
title_sort |
data_sheet_1_characterization of a novel β-agarase from antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.doc |
publishDate |
2022 |
url |
https://doi.org/10.3389/fmicb.2022.972272.s001 https://figshare.com/articles/dataset/Data_Sheet_1_Characterization_of_a_novel_-agarase_from_Antarctic_macroalgae-associated_bacteria_metagenomic_library_and_anti-inflammatory_activity_of_the_enzymatic_hydrolysates_doc/20783509 |
genre |
Antarc* Antarctic Antarctica King George Island |
genre_facet |
Antarc* Antarctic Antarctica King George Island |
op_relation |
doi:10.3389/fmicb.2022.972272.s001 https://figshare.com/articles/dataset/Data_Sheet_1_Characterization_of_a_novel_-agarase_from_Antarctic_macroalgae-associated_bacteria_metagenomic_library_and_anti-inflammatory_activity_of_the_enzymatic_hydrolysates_doc/20783509 |
op_rights |
CC BY 4.0 |
op_doi |
https://doi.org/10.3389/fmicb.2022.972272.s001 |
_version_ |
1810490243173842944 |