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  1. Article ; Online: Enhanced CO

    You, Seung Kyou / Ko, Young Jin / Shin, Sang Kyu / Hwang, Dong-Hyeuk / Kang, Dae Hee / Park, Hyeon Min / Han, Sung Ok

    Bioresource technology

    2020  Volume 318, Page(s) 124072

    Abstract: Photosynthesis of C. vulgaris shows slow growth and low lipid production due to the low solubility of ... ...

    Abstract Photosynthesis of C. vulgaris shows slow growth and low lipid production due to the low solubility of CO
    MeSH term(s) Biofuels ; Carbon Dioxide ; Carbonic Anhydrases ; Chlorella vulgaris ; Lipids
    Chemical Substances Biofuels ; Lipids ; Carbon Dioxide (142M471B3J) ; Carbonic Anhydrases (EC 4.2.1.1)
    Language English
    Publishing date 2020-09-03
    Publishing country England
    Document type Journal Article
    ZDB-ID 1065195-0
    ISSN 1873-2976 ; 0960-8524
    ISSN (online) 1873-2976
    ISSN 0960-8524
    DOI 10.1016/j.biortech.2020.124072
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    Z 3258: Show issues

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  2. Article: Enhanced CO2 fixation and lipid production of Chlorella vulgaris through the carbonic anhydrase complex

    You, Seung Kyou / Ko, Young Jin / Shin, Sang Kyu / Hwang, Dong-hyeuk / Kang, Dae Hee / Park, Hyeon Min / Han, Sung Ok

    Bioresource technology. 2020 Dec., v. 318

    2020  

    Abstract: Photosynthesis of C. vulgaris shows slow growth and low lipid production due to the low solubility of CO₂, and it is thus necessary to increase the dissolved inorganic carbon source to solve this problem. In this study, carbonic anhydrase (CA) was fused ... ...

    Abstract Photosynthesis of C. vulgaris shows slow growth and low lipid production due to the low solubility of CO₂, and it is thus necessary to increase the dissolved inorganic carbon source to solve this problem. In this study, carbonic anhydrase (CA) was fused with dockerin to form a CA complex by cohesion-dockerin interaction. The CA complex was displayed on the surface of C. vulgaris by a cellulose binding module. The CA complex increased activity and stability compared to those of a single enzyme. Additionally, C. vulgaris showed an average of 1.6-fold rapid growth during log phase through the influence of the CA complex. The bicarbonate produced by the CA complex increased the lipid production about 1.7-fold (23.3%), compared to 13.6% for the control group. The present results suggest that the CA complex successfully enhances the CO₂ fixation, which should be an essential study for 4th generation biofuels.
    Keywords Chlorella vulgaris ; bicarbonates ; biofuels ; carbon dioxide ; carbon dioxide fixation ; carbonate dehydratase ; cellulose ; dissolved inorganic carbon ; lipids ; photosynthesis ; solubility ; technology
    Language English
    Dates of publication 2020-12
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1065195-0
    ISSN 1873-2976 ; 0960-8524
    ISSN (online) 1873-2976
    ISSN 0960-8524
    DOI 10.1016/j.biortech.2020.124072
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  3. Article ; Online: Signal amplification by a self-assembled biosensor system designed on the principle of dockerin-cohesin interactions in a cellulosome complex.

    Hyeon, Jeong Eun / Kang, Dae Hee / Han, Sung Ok

    The Analyst

    2014  Volume 139, Issue 19, Page(s) 4790–4793

    Abstract: To construct a self-assembled biosensor with signal amplification, a cellulosome system, comprising type I and type II dockerin-cohesin interactions with different specificities, from the anaerobic Clostridia bacterium was applied. The self-assembled ... ...

    Abstract To construct a self-assembled biosensor with signal amplification, a cellulosome system, comprising type I and type II dockerin-cohesin interactions with different specificities, from the anaerobic Clostridia bacterium was applied. The self-assembled biosensor was highly sensitive and achieved 128.1-fold increase in detection levels compared to the control.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biosensing Techniques ; Blotting, Western ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cellulosomes/chemistry ; Cellulosomes/metabolism ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Clostridium/metabolism ; Electrophoresis, Polyacrylamide Gel ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Plasmids/genetics ; Plasmids/metabolism ; Polymerase Chain Reaction ; Protein Binding ; Cohesins
    Chemical Substances Bacterial Proteins ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2014-08-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 210747-8
    ISSN 1364-5528 ; 0003-2654
    ISSN (online) 1364-5528
    ISSN 0003-2654
    DOI 10.1039/c4an00856a
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    Zs.A 2423: Show issues Location:
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  4. Article: Synergistic effect of the enzyme complexes comprising agarase, carrageenase and neoagarobiose hydrolase on degradation of the red algae

    Kang, Dae Hee / Jeong Eun Hyeon / Sang Kyu Shin / Seung Kyou You / Sung Ok Han / Young-Chul Joo

    Bioresource technology. 2018 Feb., v. 250

    2018  

    Abstract: In the practice of converting red algae biomass into biofuel or valuable biomaterials, the critical step is the decomposition process of the agarose to give fermentable monomeric sugars. In this study, we selected three enzymes such as agarase, ... ...

    Abstract In the practice of converting red algae biomass into biofuel or valuable biomaterials, the critical step is the decomposition process of the agarose to give fermentable monomeric sugars. In this study, we selected three enzymes such as agarase, carrageenase and neoagarobiose hydrolase to inducible the simultaneous hydrolysis of the major substrates such as agar and carrageenan constituting the pretreated red algae, and expressed the chimeric enzymes and formed a complexes through optimization of addition ratio. As a result, hydrolysis by enzyme complexes showed a maximum sugar release of 679 mg L−1 with 67.9% saccharification yield from G. verrucosa natural substrate. The difference in the reducing sugar by the enzyme complexes was 3.6-fold higher than that of the monomer enzyme (cAgaB yield 188.6 mg L−1). The synergistic effect of producing sugars from red algae biomass through these enzyme complexes can be a very important biological tools aimed at bioenergy production.
    Keywords agar ; agarose ; biocompatible materials ; biofuels ; biomass ; carrageenan ; enzymes ; hydrolysis ; reducing sugars ; Rhodophyta ; saccharification ; synergism
    Language English
    Dates of publication 2018-02
    Size p. 666-672.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 1065195-0
    ISSN 1873-2976 ; 0960-8524
    ISSN (online) 1873-2976
    ISSN 0960-8524
    DOI 10.1016/j.biortech.2017.11.098
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  5. Article ; Online: Synergistic effect of the enzyme complexes comprising agarase, carrageenase and neoagarobiose hydrolase on degradation of the red algae.

    Kang, Dae Hee / You, Seung Kyou / Joo, Young-Chul / Shin, Sang Kyu / Hyeon, Jeong Eun / Han, Sung Ok

    Bioresource technology

    2018  Volume 250, Page(s) 666–672

    Abstract: In the practice of converting red algae biomass into biofuel or valuable biomaterials, the critical step is the decomposition process of the agarose to give fermentable monomeric sugars. In this study, we selected three enzymes such as agarase, ... ...

    Abstract In the practice of converting red algae biomass into biofuel or valuable biomaterials, the critical step is the decomposition process of the agarose to give fermentable monomeric sugars. In this study, we selected three enzymes such as agarase, carrageenase and neoagarobiose hydrolase to inducible the simultaneous hydrolysis of the major substrates such as agar and carrageenan constituting the pretreated red algae, and expressed the chimeric enzymes and formed a complexes through optimization of addition ratio. As a result, hydrolysis by enzyme complexes showed a maximum sugar release of 679 mg L
    MeSH term(s) Disaccharidases ; Glycoside Hydrolases ; Rhodophyta
    Chemical Substances Disaccharidases (EC 3.2.1.-) ; Glycoside Hydrolases (EC 3.2.1.-) ; neoagarobiose hydrolase (EC 3.2.1.-) ; agarase (EC 3.2.1.81)
    Language English
    Publishing date 2018-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 1065195-0
    ISSN 1873-2976 ; 0960-8524
    ISSN (online) 1873-2976
    ISSN 0960-8524
    DOI 10.1016/j.biortech.2017.11.098
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Efficient enzymatic degradation process for hydrolysis activity of the Carrageenan from red algae in marine biomass.

    Kang, Dae Hee / Hyeon, Jeong Eun / You, Seung Kyou / Kim, Seung Wook / Han, Sung Ok

    Journal of biotechnology

    2014  Volume 192 Pt A, Page(s) 108–113

    Abstract: Carrageenan is a generic name for a family of polysaccharides obtained from certain species of red algae. New methods to produce useful cost-efficiently materials from red algae are needed to convert enzymatic processes into fermentable sugars. In this ... ...

    Abstract Carrageenan is a generic name for a family of polysaccharides obtained from certain species of red algae. New methods to produce useful cost-efficiently materials from red algae are needed to convert enzymatic processes into fermentable sugars. In this study, we constructed chimeric genes cCgkA and cCglA containing the catalytic domain of κ-carrageenase CgkA and λ-carrageenase CglA from Pseudoalteromonas carrageenovora fused with a dockerin domain. Recombinant strains expressing the chimeric carrageenase resulted in a halo formation on the carrageenan plate by alcian blue staining. The recombinant cCgkA and cCglA were assembled with scaffoldin miniCbpA via cohesin and dockerin interaction. Carbohydrate binding module (CBM) in scaffoldin was used as a tag for cellulose affinity purification using cellulose as a support. The hydrolysis process was monitored by the amount of reducing sugar released from carrageenan. Interestingly, these results indicated that miniCbpA, cCgkA and cCglA assembled into a complex and that the dockerin-fused enzymes on the scaffoldin had synergistic activity in the degradation of carrageenan. The observed enhancement of activity by carrageenolytic complex was 3.1-fold-higher compared with the corresponding enzymes alone. Thus, the assemblies of advancement of active enzyme complexes will facilitate the commercial production of useful products from red algae biomass which represents inexpensive and sustainable feed-stocks.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biomass ; Carrageenan/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Glycoside Hydrolases/genetics ; Glycoside Hydrolases/metabolism ; Hydrolysis ; Pseudoalteromonas/enzymology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Rhodophyta ; Cohesins
    Chemical Substances Bacterial Proteins ; Carrier Proteins ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Recombinant Fusion Proteins ; Carrageenan (9000-07-1) ; Glycoside Hydrolases (EC 3.2.1.-)
    Language English
    Publishing date 2014-10-02
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 843647-2
    ISSN 1873-4863 ; 0168-1656 ; 1389-0352
    ISSN (online) 1873-4863
    ISSN 0168-1656 ; 1389-0352
    DOI 10.1016/j.jbiotec.2014.09.019
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    Zs.A 2299: Show issues Location:
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  7. Article: Efficient enzymatic degradation process for hydrolysis activity of the Carrageenan from red algae in marine biomass

    Kang, Dae Hee / Jeong Eun Hyeon / Seung Kyou You / Seung Wook Kim / Sung Ok Han

    Journal of biotechnology. 2014 Dec. 20, v. 192

    2014  

    Abstract: Carrageenan is a generic name for a family of polysaccharides obtained from certain species of red algae. New methods to produce useful cost-efficiently materials from red algae are needed to convert enzymatic processes into fermentable sugars. In this ... ...

    Abstract Carrageenan is a generic name for a family of polysaccharides obtained from certain species of red algae. New methods to produce useful cost-efficiently materials from red algae are needed to convert enzymatic processes into fermentable sugars. In this study, we constructed chimeric genes cCgkA and cCglA containing the catalytic domain of κ-carrageenase CgkA and λ-carrageenase CglA from Pseudoalteromonas carrageenovora fused with a dockerin domain. Recombinant strains expressing the chimeric carrageenase resulted in a halo formation on the carrageenan plate by alcian blue staining. The recombinant cCgkA and cCglA were assembled with scaffoldin miniCbpA via cohesin and dockerin interaction. Carbohydrate binding module (CBM) in scaffoldin was used as a tag for cellulose affinity purification using cellulose as a support. The hydrolysis process was monitored by the amount of reducing sugar released from carrageenan. Interestingly, these results indicated that miniCbpA, cCgkA and cCglA assembled into a complex and that the dockerin-fused enzymes on the scaffoldin had synergistic activity in the degradation of carrageenan. The observed enhancement of activity by carrageenolytic complex was 3.1-fold-higher compared with the corresponding enzymes alone. Thus, the assemblies of advancement of active enzyme complexes will facilitate the commercial production of useful products from red algae biomass which represents inexpensive and sustainable feed-stocks.
    Keywords active sites ; biomass ; carbohydrate binding ; carrageenan ; cellulose ; chimerism ; enzymes ; genes ; hydrolysis ; Pseudoalteromonas carrageenovora ; reducing sugars ; Rhodophyta ; staining ; synergism
    Language English
    Dates of publication 2014-1220
    Size p. 108-113.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 843647-2
    ISSN 1873-4863 ; 0168-1656 ; 1389-0352
    ISSN (online) 1873-4863
    ISSN 0168-1656 ; 1389-0352
    DOI 10.1016/j.jbiotec.2014.09.019
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  8. Article ; Online: GntR-type transcriptional regulator PckR negatively regulates the expression of phosphoenolpyruvate carboxykinase in Corynebacterium glutamicum.

    Hyeon, Jeong Eun / Kang, Dae Hee / Kim, Young In / You, Seung Kyou / Han, Sung Ok

    Journal of bacteriology

    2012  Volume 194, Issue 9, Page(s) 2181–2188

    Abstract: The pck (cg3169) gene of Corynebacterium glutamicum encodes a phosphoenolpyruvate carboxykinase (PEPCK). Here, a candidate transcriptional regulator that binds to the promoter region of pck was detected using a DNA affinity purification approach. An ... ...

    Abstract The pck (cg3169) gene of Corynebacterium glutamicum encodes a phosphoenolpyruvate carboxykinase (PEPCK). Here, a candidate transcriptional regulator that binds to the promoter region of pck was detected using a DNA affinity purification approach. An isolated protein was identified to be PckR (Cg0196), a GntR family transcriptional regulator which consists of 253 amino acids with a mass of 27 kDa as measured by peptide mass fingerprinting. The results of electrophoretic mobility shift assays verified that PckR specifically binds to the pck promoter. The putative regulator binding region extended from position -44 to -27 (an 18-bp sequence) relative to the transcriptional start point of the pck gene. We measured the expression of pck in a pckR deletion mutant by using quantitative real-time reverse transcription-PCR. The expression level of pck in the pckR mutant was 7.6 times higher than that in wild-type cells grown in glucose. Comparative DNA microarray hybridizations and bioinformatic searches revealed the gene composition of the transcriptional regulon of C. glutamicum. Based on these results, PckR seemed to play an important role in the regulation of PEPCK in C. glutamicum grown in glucose. In particular, these assays revealed that PckR acts as a repressor of pck expression during glucose metabolism.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Corynebacterium glutamicum/classification ; Corynebacterium glutamicum/enzymology ; Corynebacterium glutamicum/genetics ; DNA, Bacterial/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Escherichia coli ; Gene Deletion ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial/physiology ; Genome, Bacterial ; Oligonucleotide Array Sequence Analysis ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics ; Phosphoenolpyruvate Carboxykinase (GTP)/metabolism ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription Initiation Site
    Chemical Substances Bacterial Proteins ; DNA, Bacterial ; DNA-Binding Proteins ; Transcription Factors ; Phosphoenolpyruvate Carboxykinase (GTP) (EC 4.1.1.32)
    Language English
    Publishing date 2012-02-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.06562-11
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    Ud II Zs.50: Show issues Location:
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  9. Article: GntR-Type Transcriptional Regulator PckR Negatively Regulates the Expression of Phosphoenolpyruvate Carboxykinase in Corynebacterium glutamicum

    Hyeon, Jeong Eun / Kang, Dae Hee / Kim, Young In / You, Seung Kyou / Han, Sung Ok

    Journal of bacteriology. 2012 May 1, v. 194, no. 9

    2012  

    Abstract: The pck (cg3169) gene of Corynebacterium glutamicum encodes a phosphoenolpyruvate carboxykinase (PEPCK). Here, a candidate transcriptional regulator that binds to the promoter region of pck was detected using a DNA affinity purification approach. An ... ...

    Abstract The pck (cg3169) gene of Corynebacterium glutamicum encodes a phosphoenolpyruvate carboxykinase (PEPCK). Here, a candidate transcriptional regulator that binds to the promoter region of pck was detected using a DNA affinity purification approach. An isolated protein was identified to be PckR (Cg0196), a GntR family transcriptional regulator which consists of 253 amino acids with a mass of 27 kDa as measured by peptide mass fingerprinting. The results of electrophoretic mobility shift assays verified that PckR specifically binds to the pck promoter. The putative regulator binding region extended from position –44 to –27 (an 18-bp sequence) relative to the transcriptional start point of the pck gene. We measured the expression of pck in a pckR deletion mutant by using quantitative real-time reverse transcription-PCR. The expression level of pck in the pckR mutant was 7.6 times higher than that in wild-type cells grown in glucose. Comparative DNA microarray hybridizations and bioinformatic searches revealed the gene composition of the transcriptional regulon of C. glutamicum. Based on these results, PckR seemed to play an important role in the regulation of PEPCK in C. glutamicum grown in glucose. In particular, these assays revealed that PckR acts as a repressor of pck expression during glucose metabolism.
    Keywords Corynebacterium glutamicum ; DNA ; DNA microarrays ; amino acids ; bioinformatics ; gel electrophoresis ; glucose ; metabolism ; microarray technology ; mutants ; promoter regions ; regulon ; reverse transcriptase polymerase chain reaction ; transcription (genetics) ; transcription factors
    Language English
    Dates of publication 2012-0501
    Size p. 2181-2188.
    Publishing place American Society for Microbiology
    Document type Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.06562-11
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  10. Article ; Online: Enhancing Fatty Acid Production of Saccharomyces cerevisiae as an Animal Feed Supplement.

    You, Seung Kyou / Joo, Young-Chul / Kang, Dae Hee / Shin, Sang Kyu / Hyeon, Jeong Eun / Woo, Han Min / Um, Youngsoon / Park, Chulhwan / Han, Sung Ok

    Journal of agricultural and food chemistry

    2017  Volume 65, Issue 50, Page(s) 11029–11035

    Abstract: Saccharomyces cerevisiae is used for edible purposes, such as human food or as an animal feed supplement. Fatty acids are also beneficial as feed supplements, but S. cerevisiae produces small amounts of fatty acids. In this study, we enhanced fatty acid ... ...

    Abstract Saccharomyces cerevisiae is used for edible purposes, such as human food or as an animal feed supplement. Fatty acids are also beneficial as feed supplements, but S. cerevisiae produces small amounts of fatty acids. In this study, we enhanced fatty acid production of S. cerevisiae by overexpressing acetyl-CoA carboxylase, thioesterase, and malic enzyme associated with fatty acid metabolism. The enhanced strain pAMT showed 2.4-fold higher fatty acids than the wild-type strain. To further increase the fatty acids, various nitrogen sources were analyzed and calcium nitrate was selected as an optimal nitrogen source for fatty acid production. By concentration optimization, 672 mg/L of fatty acids was produced, which was 4.7-fold higher than wild-type strain. These results complement the low level fatty acid production and make it possible to obtain the benefits of fatty acids as an animal feed supplement while, simultaneously, maintaining the advantages of S. cerevisiae.
    MeSH term(s) Acetyl-CoA Carboxylase/genetics ; Acetyl-CoA Carboxylase/metabolism ; Animal Feed/analysis ; Animals ; Cattle/growth & development ; Cattle/metabolism ; Dietary Supplements/analysis ; Fatty Acids/biosynthesis ; Metabolic Engineering ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Fatty Acids ; Saccharomyces cerevisiae Proteins ; Acetyl-CoA Carboxylase (EC 6.4.1.2)
    Language English
    Publishing date 2017-12-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 241619-0
    ISSN 1520-5118 ; 0021-8561
    ISSN (online) 1520-5118
    ISSN 0021-8561
    DOI 10.1021/acs.jafc.7b04485
    Database MEDical Literature Analysis and Retrieval System OnLINE

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