DOI . ORG {
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Title[redir]:
Characterization of recombinant protein ferritin from Pyropia yezoensis (rPyFer) and its biological activities | Food Science and Biotechnology
Description:
Ferritins are iron-binding proteins that are basically participated in iron storage, detoxification, and immune response. In the present study, ferritin gene from the marine red algae Pyropia yezoensis was cloned into a pET21d expression vector. High-efficiency transformation was performed in Escherichia coli BL21, the recombinant protein was expressed by induction with 0.1 mM isopropyl-β-D-thiogalactoside and purified via ammonium sulfate precipitation, anion exchange and size exclusion chromatography. The purified recombinant ferritin from P. yezoensis (rPyFer) was characterized and analyzed for its antimicrobial activity against both Gram-negative and Gram-positive bacterial cultures and exhibited significant antibacterial activity against Gram-positive cultures. The recombinant protein was also analyzed for its iron-uptake and radical-scavenging activities; rPyFer exhibited significant iron-uptake activity at low concentrations, and its radical-scavenging activity increased in a dose-dependent manner. This research will contribute to the development of new therapeutic proteins from marine algae.
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Keywords {🔍}
article, google, scholar, cas, ferritin, iron, protein, activity, recombinant, expression, content, research, choi, characterization, yezoensis, marine, access, zhang, privacy, cookies, pyropia, proteins, algae, antioxidant, fish, information, publish, search, food, rpyfer, younhee, ferritins, storage, response, gene, coli, biochem, shellfish, immunol, magnesium, springer, data, log, journal, science, biological, activities, published, october, ulagesan,
Topics {✒️}
1 mm isopropyl-β-d-thiogalactoside minimum inhibitory concentrations month download article/chapter youn-hee choi radical-scavenging activity increased iron-binding proteins recombinant protein ferritin recombinant h-chain ferritins marine brown algae gram-positive bacterial cultures related subjects human ferritin l-chain h-chain deletion mutants antioxidant activity applying article food science jeong-wook choi smith jm therapeutic proteins recombinant protein iron-binding protein antioxidant response element marine algae marine bio-materials full article pdf purified recombinant ferritin privacy choices/manage cookies pyropia yezoensis ferro-oxidase activity radical-scavenging activities gram-positive cultures free radical bio antioxidant activity national research foundation check access instant access ferritin subunits involved blue-green alga ferritin iron uptake recombinant ferritin pet21d expression vector european economic area ammonium sulfate precipitation size exclusion chromatography dose-dependent manner ferric reducing ability heat shock method iptg inducible promoters chlamydomonas reinhardtii chloroplasts potential paleoceanographic applications t7 rna polymerase
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headline:Characterization of recombinant protein ferritin from Pyropia yezoensis (rPyFer) and its biological activities
description:Ferritins are iron-binding proteins that are basically participated in iron storage, detoxification, and immune response. In the present study, ferritin gene from the marine red algae Pyropia yezoensis was cloned into a pET21d expression vector. High-efficiency transformation was performed in Escherichia coli BL21, the recombinant protein was expressed by induction with 0.1 mM isopropyl-β-D-thiogalactoside and purified via ammonium sulfate precipitation, anion exchange and size exclusion chromatography. The purified recombinant ferritin from P. yezoensis (rPyFer) was characterized and analyzed for its antimicrobial activity against both Gram-negative and Gram-positive bacterial cultures and exhibited significant antibacterial activity against Gram-positive cultures. The recombinant protein was also analyzed for its iron-uptake and radical-scavenging activities; rPyFer exhibited significant iron-uptake activity at low concentrations, and its radical-scavenging activity increased in a dose-dependent manner. This research will contribute to the development of new therapeutic proteins from marine algae.
datePublished:2020-10-06T00:00:00Z
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Pyropia yezoensis
Ferritin
Equine spleen ferritin
Marine algae
Antioxidant activity
Minimum inhibitory concentration
Food Science
Nutrition
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description:Ferritins are iron-binding proteins that are basically participated in iron storage, detoxification, and immune response. In the present study, ferritin gene from the marine red algae Pyropia yezoensis was cloned into a pET21d expression vector. High-efficiency transformation was performed in Escherichia coli BL21, the recombinant protein was expressed by induction with 0.1 mM isopropyl-β-D-thiogalactoside and purified via ammonium sulfate precipitation, anion exchange and size exclusion chromatography. The purified recombinant ferritin from P. yezoensis (rPyFer) was characterized and analyzed for its antimicrobial activity against both Gram-negative and Gram-positive bacterial cultures and exhibited significant antibacterial activity against Gram-positive cultures. The recombinant protein was also analyzed for its iron-uptake and radical-scavenging activities; rPyFer exhibited significant iron-uptake activity at low concentrations, and its radical-scavenging activity increased in a dose-dependent manner. This research will contribute to the development of new therapeutic proteins from marine algae.
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Pyropia yezoensis
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Equine spleen ferritin
Marine algae
Antioxidant activity
Minimum inhibitory concentration
Food Science
Nutrition
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