Purified proteases of two Antarctic bacteria: from screening to characterization
Abstract Proteases are widely used in industrial processes, and the discovery of new, more kinetically efficient proteases can have a positive impact on industry. Enzymes from Antarctic microorganisms exhibit cold-adaptive properties, making them useful in biotechnology. The cold and harsh environme...
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Online Access: | http://dx.doi.org/10.1017/s0954102021000468 https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0954102021000468 |
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crcambridgeupr:10.1017/s0954102021000468 2024-03-03T08:38:02+00:00 Purified proteases of two Antarctic bacteria: from screening to characterization Peralta-Figueroa, Christian Martínez-Oyanedel, José Bunster, Marta González-Rocha, Gerardo Instituto Antártico Chileno INACH INNOVA Bio Bio 2021 http://dx.doi.org/10.1017/s0954102021000468 https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0954102021000468 en eng Cambridge University Press (CUP) https://www.cambridge.org/core/terms Antarctic Science volume 33, issue 6, page 633-644 ISSN 0954-1020 1365-2079 Geology Ecology, Evolution, Behavior and Systematics Oceanography journal-article 2021 crcambridgeupr https://doi.org/10.1017/s0954102021000468 2024-02-08T08:31:58Z Abstract Proteases are widely used in industrial processes, and the discovery of new, more kinetically efficient proteases can have a positive impact on industry. Enzymes from Antarctic microorganisms exhibit cold-adaptive properties, making them useful in biotechnology. The cold and harsh environment of Antarctica makes it a valuable source for new biotechnologically related enzymes. In this study, we characterized two cold-adapted proteases purified from Pseudoalteromonas issachenkonii P14M1-4 and Flavobacterium frigidimaris ANT34-7, isolated from King George Island, Antarctica, and compared these with proteases from the non-cold-adapted bacteria Bacillus licheniformis and Geobacillus stearothermophilus . The best temperature growing conditions were used for protease purification and characterization. The protease from P. issachenkonii P14M1-4 was identified as a 40–43 kDa metal-dependent subtilisin-like serine protease and the protease from F. frigidimaris ANT34-7 was identified as a 28 kDa metalloprotease. The enzymes showed an optimum temperature of between 35°C and 40°C and an optimum pH in the neutral to alkaline range. Their activation energies, catalytic constants and growth capacities at different temperatures categorize them as cold-adapted enzymes. We conclude that the characteristics exhibited by these proteases make them useful for biotechnological purposes requiring high activity at low temperatures. Moreover, to the best of our knowledge, this is the first characterization of a cold-adapted protease from F. frigidimaris . Article in Journal/Newspaper Antarc* Antarctic Antarctic Science Antarctica King George Island Cambridge University Press Antarctic King George Island Antarctic Science 1 12 |
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Open Polar |
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Cambridge University Press |
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crcambridgeupr |
language |
English |
topic |
Geology Ecology, Evolution, Behavior and Systematics Oceanography |
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Geology Ecology, Evolution, Behavior and Systematics Oceanography Peralta-Figueroa, Christian Martínez-Oyanedel, José Bunster, Marta González-Rocha, Gerardo Purified proteases of two Antarctic bacteria: from screening to characterization |
topic_facet |
Geology Ecology, Evolution, Behavior and Systematics Oceanography |
description |
Abstract Proteases are widely used in industrial processes, and the discovery of new, more kinetically efficient proteases can have a positive impact on industry. Enzymes from Antarctic microorganisms exhibit cold-adaptive properties, making them useful in biotechnology. The cold and harsh environment of Antarctica makes it a valuable source for new biotechnologically related enzymes. In this study, we characterized two cold-adapted proteases purified from Pseudoalteromonas issachenkonii P14M1-4 and Flavobacterium frigidimaris ANT34-7, isolated from King George Island, Antarctica, and compared these with proteases from the non-cold-adapted bacteria Bacillus licheniformis and Geobacillus stearothermophilus . The best temperature growing conditions were used for protease purification and characterization. The protease from P. issachenkonii P14M1-4 was identified as a 40–43 kDa metal-dependent subtilisin-like serine protease and the protease from F. frigidimaris ANT34-7 was identified as a 28 kDa metalloprotease. The enzymes showed an optimum temperature of between 35°C and 40°C and an optimum pH in the neutral to alkaline range. Their activation energies, catalytic constants and growth capacities at different temperatures categorize them as cold-adapted enzymes. We conclude that the characteristics exhibited by these proteases make them useful for biotechnological purposes requiring high activity at low temperatures. Moreover, to the best of our knowledge, this is the first characterization of a cold-adapted protease from F. frigidimaris . |
author2 |
Instituto Antártico Chileno INACH INNOVA Bio Bio |
format |
Article in Journal/Newspaper |
author |
Peralta-Figueroa, Christian Martínez-Oyanedel, José Bunster, Marta González-Rocha, Gerardo |
author_facet |
Peralta-Figueroa, Christian Martínez-Oyanedel, José Bunster, Marta González-Rocha, Gerardo |
author_sort |
Peralta-Figueroa, Christian |
title |
Purified proteases of two Antarctic bacteria: from screening to characterization |
title_short |
Purified proteases of two Antarctic bacteria: from screening to characterization |
title_full |
Purified proteases of two Antarctic bacteria: from screening to characterization |
title_fullStr |
Purified proteases of two Antarctic bacteria: from screening to characterization |
title_full_unstemmed |
Purified proteases of two Antarctic bacteria: from screening to characterization |
title_sort |
purified proteases of two antarctic bacteria: from screening to characterization |
publisher |
Cambridge University Press (CUP) |
publishDate |
2021 |
url |
http://dx.doi.org/10.1017/s0954102021000468 https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0954102021000468 |
geographic |
Antarctic King George Island |
geographic_facet |
Antarctic King George Island |
genre |
Antarc* Antarctic Antarctic Science Antarctica King George Island |
genre_facet |
Antarc* Antarctic Antarctic Science Antarctica King George Island |
op_source |
Antarctic Science volume 33, issue 6, page 633-644 ISSN 0954-1020 1365-2079 |
op_rights |
https://www.cambridge.org/core/terms |
op_doi |
https://doi.org/10.1017/s0954102021000468 |
container_title |
Antarctic Science |
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1 |
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12 |
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1792503833209864192 |