Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes
There has been a recent increase in the exploration of cold-active β-galactosidases, as it offers new alternatives for the dairy industry, mainly in response to the current needs of lactose-intolerant consumers. Since extremophilic microbial compounds might have unique physical and chemical properti...
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ftdoajarticles:oai:doaj.org/article:c60ea095729e4c3f9acdeae1551c1ca6 2023-05-15T13:45:44+02:00 Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes Kattia Núñez-Montero Rodrigo Salazar Andrés Santos Olman Gómez-Espinoza Scandar Farah Claudia Troncoso Catalina Hoffmann Damaris Melivilu Felipe Scott Leticia Barrientos Díaz 2021-04-01T00:00:00Z https://doi.org/10.3390/ijms22084144 https://doaj.org/article/c60ea095729e4c3f9acdeae1551c1ca6 EN eng MDPI AG https://www.mdpi.com/1422-0067/22/8/4144 https://doaj.org/toc/1661-6596 https://doaj.org/toc/1422-0067 doi:10.3390/ijms22084144 1422-0067 1661-6596 https://doaj.org/article/c60ea095729e4c3f9acdeae1551c1ca6 International Journal of Molecular Sciences, Vol 22, Iss 4144, p 4144 (2021) β-galactosidase Antarctica lactose cold-adapted bacteria extremozymes Biology (General) QH301-705.5 Chemistry QD1-999 article 2021 ftdoajarticles https://doi.org/10.3390/ijms22084144 2022-12-31T06:36:16Z There has been a recent increase in the exploration of cold-active β-galactosidases, as it offers new alternatives for the dairy industry, mainly in response to the current needs of lactose-intolerant consumers. Since extremophilic microbial compounds might have unique physical and chemical properties, this research aimed to study the capacity of Antarctic bacterial strains to produce cold-active β-galactosidases. A screening revealed 81 out of 304 strains with β-galactosidase activity. The strain Se8.10.12 showed the highest enzymatic activity. Morphological, biochemical, and molecular characterization based on whole-genome sequencing confirmed it as the first Rahnella inusitata isolate from the Antarctic, which retained 41–62% of its β-galactosidase activity in the cold (4 °C–15 °C). Three β-galactosidases genes were found in the R. inusitata genome, which belong to the glycoside hydrolase families GH2 (LacZ and EbgA) and GH42 (BglY). Based on molecular docking, some of these enzymes exhibited higher lactose predicted affinity than the commercial control enzyme from Aspergillus oryzae . Hence, this work reports a new Rahnella inusitata strain from the Antarctic continent as a prominent cold-active β-galactosidase producer. Article in Journal/Newspaper Antarc* Antarctic Antarctica Directory of Open Access Journals: DOAJ Articles Antarctic The Antarctic International Journal of Molecular Sciences 22 8 4144 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
β-galactosidase Antarctica lactose cold-adapted bacteria extremozymes Biology (General) QH301-705.5 Chemistry QD1-999 |
spellingShingle |
β-galactosidase Antarctica lactose cold-adapted bacteria extremozymes Biology (General) QH301-705.5 Chemistry QD1-999 Kattia Núñez-Montero Rodrigo Salazar Andrés Santos Olman Gómez-Espinoza Scandar Farah Claudia Troncoso Catalina Hoffmann Damaris Melivilu Felipe Scott Leticia Barrientos Díaz Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
topic_facet |
β-galactosidase Antarctica lactose cold-adapted bacteria extremozymes Biology (General) QH301-705.5 Chemistry QD1-999 |
description |
There has been a recent increase in the exploration of cold-active β-galactosidases, as it offers new alternatives for the dairy industry, mainly in response to the current needs of lactose-intolerant consumers. Since extremophilic microbial compounds might have unique physical and chemical properties, this research aimed to study the capacity of Antarctic bacterial strains to produce cold-active β-galactosidases. A screening revealed 81 out of 304 strains with β-galactosidase activity. The strain Se8.10.12 showed the highest enzymatic activity. Morphological, biochemical, and molecular characterization based on whole-genome sequencing confirmed it as the first Rahnella inusitata isolate from the Antarctic, which retained 41–62% of its β-galactosidase activity in the cold (4 °C–15 °C). Three β-galactosidases genes were found in the R. inusitata genome, which belong to the glycoside hydrolase families GH2 (LacZ and EbgA) and GH42 (BglY). Based on molecular docking, some of these enzymes exhibited higher lactose predicted affinity than the commercial control enzyme from Aspergillus oryzae . Hence, this work reports a new Rahnella inusitata strain from the Antarctic continent as a prominent cold-active β-galactosidase producer. |
format |
Article in Journal/Newspaper |
author |
Kattia Núñez-Montero Rodrigo Salazar Andrés Santos Olman Gómez-Espinoza Scandar Farah Claudia Troncoso Catalina Hoffmann Damaris Melivilu Felipe Scott Leticia Barrientos Díaz |
author_facet |
Kattia Núñez-Montero Rodrigo Salazar Andrés Santos Olman Gómez-Espinoza Scandar Farah Claudia Troncoso Catalina Hoffmann Damaris Melivilu Felipe Scott Leticia Barrientos Díaz |
author_sort |
Kattia Núñez-Montero |
title |
Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
title_short |
Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
title_full |
Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
title_fullStr |
Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
title_full_unstemmed |
Antarctic Rahnella inusitata : A Producer of Cold-Stable β-Galactosidase Enzymes |
title_sort |
antarctic rahnella inusitata : a producer of cold-stable β-galactosidase enzymes |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doi.org/10.3390/ijms22084144 https://doaj.org/article/c60ea095729e4c3f9acdeae1551c1ca6 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_source |
International Journal of Molecular Sciences, Vol 22, Iss 4144, p 4144 (2021) |
op_relation |
https://www.mdpi.com/1422-0067/22/8/4144 https://doaj.org/toc/1661-6596 https://doaj.org/toc/1422-0067 doi:10.3390/ijms22084144 1422-0067 1661-6596 https://doaj.org/article/c60ea095729e4c3f9acdeae1551c1ca6 |
op_doi |
https://doi.org/10.3390/ijms22084144 |
container_title |
International Journal of Molecular Sciences |
container_volume |
22 |
container_issue |
8 |
container_start_page |
4144 |
_version_ |
1766230444059131904 |