Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology
A novel transglutaminase (TGase, EC 2.3.2.13) from antarctic Penicillium chrysogenum was partially purified using ammonium sulfate precipitation and anionic exchange chromatography. The final extract had a specific activity of 7.81 mU/mg, purification fold of 7.16, and a yield of 5.02%. The molecula...
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ftconicet:oai:ri.conicet.gov.ar:11336/131169 2023-10-09T21:46:44+02:00 Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology Glodowsky, Alejandro Pablo Ruberto, Lucas Adolfo Mauro Martorell, María Martha Mac Cormack, Walter Patricio Levin, Gustavo Javier application/pdf http://hdl.handle.net/11336/131169 eng eng Elsevier info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S1878818120311695 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2020.101807 http://hdl.handle.net/11336/131169 Glodowsky, Alejandro Pablo; Ruberto, Lucas Adolfo Mauro; Martorell, María Martha; Mac Cormack, Walter Patricio; Levin, Gustavo Javier; Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology; Elsevier; Biocatalysis and Agricultural Biotechnology; 29; 10-2020; 1-8 1878-8181 CONICET Digital CONICET info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ ANTARCTIC FUNGI COLD-ACTIVE ENZYME FOOD TECHNOLOGY TRANSGLUTAMINASE https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.bcab.2020.101807 2023-09-24T18:51:49Z A novel transglutaminase (TGase, EC 2.3.2.13) from antarctic Penicillium chrysogenum was partially purified using ammonium sulfate precipitation and anionic exchange chromatography. The final extract had a specific activity of 7.81 mU/mg, purification fold of 7.16, and a yield of 5.02%. The molecular weight was estimated to be 67 kDa by bioinformatic analysis and SDS-PAGE. Maximum TGase activity was observed at pH 8.0 and 30 °C, mesophilic conditions (near 40 °C) resulted in total inactivation. A slight improvement in TGase activity was observed in the presence of Ca2+, it increased to 127.78 ± 9.62% at 35 mM but return to normal values at higher concentrations. Additionally, the enzyme activity decreased progressively in the presence of EDTA and STPP suggesting that the enzyme is Ca2+ dependent but this cofactor is being supplied by the fermented substrate. The partially purified TGase was used as an additive to modify the rheology of a cold-set gelatin gel achieving an increase in the gel strength and gumminess of 32.25% and 30.50% respectively. Fil: Glodowsky, Alejandro Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina Fil: Ruberto, Lucas Adolfo Mauro. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Martorell, María Martha. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de ... Article in Journal/Newspaper Antarc* Antarctic Dirección Nacional del Antártico Instituto Antártico Argentino CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Antarctic Argentino Argentina Pablo ENVELOPE(-63.717,-63.717,-64.283,-64.283) Entre Ríos ENVELOPE(-66.333,-66.333,-66.433,-66.433) Biocatalysis and Agricultural Biotechnology 29 101807 |
institution |
Open Polar |
collection |
CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
ANTARCTIC FUNGI COLD-ACTIVE ENZYME FOOD TECHNOLOGY TRANSGLUTAMINASE https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
spellingShingle |
ANTARCTIC FUNGI COLD-ACTIVE ENZYME FOOD TECHNOLOGY TRANSGLUTAMINASE https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 Glodowsky, Alejandro Pablo Ruberto, Lucas Adolfo Mauro Martorell, María Martha Mac Cormack, Walter Patricio Levin, Gustavo Javier Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
topic_facet |
ANTARCTIC FUNGI COLD-ACTIVE ENZYME FOOD TECHNOLOGY TRANSGLUTAMINASE https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
description |
A novel transglutaminase (TGase, EC 2.3.2.13) from antarctic Penicillium chrysogenum was partially purified using ammonium sulfate precipitation and anionic exchange chromatography. The final extract had a specific activity of 7.81 mU/mg, purification fold of 7.16, and a yield of 5.02%. The molecular weight was estimated to be 67 kDa by bioinformatic analysis and SDS-PAGE. Maximum TGase activity was observed at pH 8.0 and 30 °C, mesophilic conditions (near 40 °C) resulted in total inactivation. A slight improvement in TGase activity was observed in the presence of Ca2+, it increased to 127.78 ± 9.62% at 35 mM but return to normal values at higher concentrations. Additionally, the enzyme activity decreased progressively in the presence of EDTA and STPP suggesting that the enzyme is Ca2+ dependent but this cofactor is being supplied by the fermented substrate. The partially purified TGase was used as an additive to modify the rheology of a cold-set gelatin gel achieving an increase in the gel strength and gumminess of 32.25% and 30.50% respectively. Fil: Glodowsky, Alejandro Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina Fil: Ruberto, Lucas Adolfo Mauro. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Martorell, María Martha. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de ... |
format |
Article in Journal/Newspaper |
author |
Glodowsky, Alejandro Pablo Ruberto, Lucas Adolfo Mauro Martorell, María Martha Mac Cormack, Walter Patricio Levin, Gustavo Javier |
author_facet |
Glodowsky, Alejandro Pablo Ruberto, Lucas Adolfo Mauro Martorell, María Martha Mac Cormack, Walter Patricio Levin, Gustavo Javier |
author_sort |
Glodowsky, Alejandro Pablo |
title |
Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
title_short |
Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
title_full |
Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
title_fullStr |
Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
title_full_unstemmed |
Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology |
title_sort |
cold active transglutaminase from antarctic penicillium chrysogenum: partial purification, characterization and potential application in food technology |
publisher |
Elsevier |
url |
http://hdl.handle.net/11336/131169 |
long_lat |
ENVELOPE(-63.717,-63.717,-64.283,-64.283) ENVELOPE(-66.333,-66.333,-66.433,-66.433) |
geographic |
Antarctic Argentino Argentina Pablo Entre Ríos |
geographic_facet |
Antarctic Argentino Argentina Pablo Entre Ríos |
genre |
Antarc* Antarctic Dirección Nacional del Antártico Instituto Antártico Argentino |
genre_facet |
Antarc* Antarctic Dirección Nacional del Antártico Instituto Antártico Argentino |
op_relation |
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S1878818120311695 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2020.101807 http://hdl.handle.net/11336/131169 Glodowsky, Alejandro Pablo; Ruberto, Lucas Adolfo Mauro; Martorell, María Martha; Mac Cormack, Walter Patricio; Levin, Gustavo Javier; Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology; Elsevier; Biocatalysis and Agricultural Biotechnology; 29; 10-2020; 1-8 1878-8181 CONICET Digital CONICET |
op_rights |
info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
op_doi |
https://doi.org/10.1016/j.bcab.2020.101807 |
container_title |
Biocatalysis and Agricultural Biotechnology |
container_volume |
29 |
container_start_page |
101807 |
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1779309249623490560 |