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Alginate-modifying enzymes: biological roles and biotechnological uses.

Frontiers in microbiology

Ertesvåg H.
PMID: 26074905
Front Microbiol. 2015 May 27;6:523. doi: 10.3389/fmicb.2015.00523. eCollection 2015.

Alginate denotes a group of industrially important 1-4-linked biopolymers composed of the C-5-epimers β-D-mannuronic acid (M) and α-L-guluronic acid (G). The polysaccharide is manufactured from brown algae where it constitutes the main structural cell wall polymer. The physical properties...

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Ertesvåg H. Alginate-modifying enzymes: biological roles and biotechnological uses. Front Microbiol. 2015;6:523doi: 10.3389/fmicb.2015.00523.
Ertesvåg, H. (2015). Alginate-modifying enzymes: biological roles and biotechnological uses. Frontiers in microbiology, 6523. https://doi.org/10.3389/fmicb.2015.00523
Ertesvåg, Helga. "Alginate-modifying enzymes: biological roles and biotechnological uses." Frontiers in microbiology vol. 6 (2015): 523. doi: https://doi.org/10.3389/fmicb.2015.00523
Ertesvåg H. Alginate-modifying enzymes: biological roles and biotechnological uses. Front Microbiol. 2015 May 27;6:523. doi: 10.3389/fmicb.2015.00523. eCollection 2015. PMID: 26074905; PMCID: PMC4444821.
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Mechanistic basis for understanding the dual activities of the bifunctional .

Applied and environmental microbiology

Gaardløs M, Heggeset TMB, Tøndervik A, Tezé D, Svensson B, Ertesvåg H, Sletta H, Aachmann FL.
PMID: 34878812
Appl Environ Microbiol. 2021 Dec 08;AEM0183621. doi: 10.1128/AEM.01836-21. Epub 2021 Dec 08.

The structure and functional properties of alginates are dictated by the monomer composition and molecular weight distribution. Mannuronan C-5 epimerases determine the monomer composition by catalysing the epimerization of β-d-mannuronic acid residues (M) into α-l-guluronic acid residues (G). The...

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Gaardløs M, Heggeset TMB, Tøndervik A, et al. Mechanistic basis for understanding the dual activities of the bifunctional . Appl Environ Microbiol. 2021;AEM0183621doi: 10.1128/AEM.01836-21.
Gaardløs, M., Heggeset, T. M. B., Tøndervik, A., Tezé, D., Svensson, B., Ertesvåg, H., Sletta, H., & Aachmann, F. L. (2021). Mechanistic basis for understanding the dual activities of the bifunctional . Applied and environmental microbiology, AEM0183621. https://doi.org/10.1128/AEM.01836-21
Gaardløs, Margrethe, et al. "Mechanistic basis for understanding the dual activities of the bifunctional ." Applied and environmental microbiology vol. (2021): AEM0183621. doi: https://doi.org/10.1128/AEM.01836-21
Gaardløs M, Heggeset TMB, Tøndervik A, Tezé D, Svensson B, Ertesvåg H, Sletta H, Aachmann FL. Mechanistic basis for understanding the dual activities of the bifunctional . Appl Environ Microbiol. 2021 Dec 08;AEM0183621. doi: 10.1128/AEM.01836-21. Epub 2021 Dec 08. PMID: 34878812.
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Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4.

Glycobiology

Gaardløs M, Samsonov SA, Sletmoen M, Hjørnevik M, Sætrom GI, Tøndervik A, Aachmann FL.
PMID: 33822050
Glycobiology. 2021 Apr 01; doi: 10.1093/glycob/cwab025. Epub 2021 Apr 01.

Mannuronan C-5 epimerases catalyse the epimerization of monomer residues in the polysaccharide alginate, changing the physical properties of the biopolymer. The enzymes are utilized to tailor alginate to numerous biological functions by alginate-producing organisms. The underlying molecular mechanisms that...

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Gaardløs M, Samsonov SA, Sletmoen M, et al. Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4. Glycobiology. 2021;doi: 10.1093/glycob/cwab025.
Gaardløs, M., Samsonov, S. A., Sletmoen, M., Hjørnevik, M., Sætrom, G. I., Tøndervik, A., & Aachmann, F. L. (2021). Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4. Glycobiology, . https://doi.org/10.1093/glycob/cwab025
Gaardløs, Margrethe, et al. "Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4." Glycobiology vol. (2021). doi: https://doi.org/10.1093/glycob/cwab025
Gaardløs M, Samsonov SA, Sletmoen M, Hjørnevik M, Sætrom GI, Tøndervik A, Aachmann FL. Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4. Glycobiology. 2021 Apr 01; doi: 10.1093/glycob/cwab025. Epub 2021 Apr 01. PMID: 33822050.
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Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2.

Enzyme and microbial technology

Ramstadab MV, Markussen S, Ellingsen TE, Skjåk-Braek G, Levine DW.
PMID: 11118599
Enzyme Microb Technol. 2001 Jan 02;28(1):57-69. doi: 10.1016/s0141-0229(00)00273-8.

The mannuronan C-5-epimerase AlgE2 is one of a family of Ca(2+)-dependent epimerases secreted by Azotobacter vinelandii. These enzymes catalyze the conversion of beta-D-mannuronic acid residues (M) to alpha-L-guluronic acid residues (G) in alginate. AlgE2 had a pH optimum between...

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Ramstadab MV, Markussen S, Ellingsen TE, et al. Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2. Enzyme Microb Technol. 2001;28(1):57-69doi: 10.1016/s0141-0229(00)00273-8.
Ramstadab, M. V., Markussen, S., Ellingsen, T. E., Skjåk-Braek, G., & Levine, D. W. (2001). Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2. Enzyme and microbial technology, 28(1), 57-69. https://doi.org/10.1016/s0141-0229(00)00273-8
Ramstadab, et al. "Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2." Enzyme and microbial technology vol. 28,1 (2001): 57-69. doi: https://doi.org/10.1016/s0141-0229(00)00273-8
Ramstadab MV, Markussen S, Ellingsen TE, Skjåk-Braek G, Levine DW. Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2. Enzyme Microb Technol. 2001 Jan 02;28(1):57-69. doi: 10.1016/s0141-0229(00)00273-8. PMID: 11118599.
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A structural basis for the amphiphilic character of alginates - Implications for membrane fouling.

Carbohydrate polymers

Stewart MB, Myat DT, Kuiper M, Manning RJ, Gray SR, Orbell JD.
PMID: 28325313
Carbohydr Polym. 2017 May 15;164:162-169. doi: 10.1016/j.carbpol.2017.01.072. Epub 2017 Jan 22.

Ostensibly hydrophilic alginates are known to foul hydrophobic membranes, under various conditions. Here, controlled experiments have been conducted at high and low pH on the fouling of a polypropylene membrane by alginate and the results suggest that the observed...

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Stewart MB, Myat DT, Kuiper M, et al. A structural basis for the amphiphilic character of alginates - Implications for membrane fouling. Carbohydr Polym. 2017;164:162-169doi: 10.1016/j.carbpol.2017.01.072.
Stewart, M. B., Myat, D. T., Kuiper, M., Manning, R. J., Gray, S. R., & Orbell, J. D. (2017). A structural basis for the amphiphilic character of alginates - Implications for membrane fouling. Carbohydrate polymers, 164162-169. https://doi.org/10.1016/j.carbpol.2017.01.072
Stewart, Matthew B, et al. "A structural basis for the amphiphilic character of alginates - Implications for membrane fouling." Carbohydrate polymers vol. 164 (2017): 162-169. doi: https://doi.org/10.1016/j.carbpol.2017.01.072
Stewart MB, Myat DT, Kuiper M, Manning RJ, Gray SR, Orbell JD. A structural basis for the amphiphilic character of alginates - Implications for membrane fouling. Carbohydr Polym. 2017 May 15;164:162-169. doi: 10.1016/j.carbpol.2017.01.072. Epub 2017 Jan 22. PMID: 28325313.
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Showing 1 to 5 of 5 entries