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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Bibliographic Details
Main Authors: Xiaoqian Gu, Luying Zhao, Jiaojiao Tan, Qian Zhang, Liping Fu, Jiang Li
Format: Dataset
Language:unknown
Published: 2022
Subjects:
Online Access: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
id ftfrontimediafig:oai:figshare.com:article/20783509
record_format openpolar
spelling 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
institution Open Polar
collection 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