Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Núñez-Montero, Kattia, Salazar, Rodrigo, Santos, Andrés, Gómez-Espinoza, Olman, Farah, Scandar, Troncoso, Claudia, Hoffmann, Catalina, Melivilu, Damaris, Scott, Felipe, Barrientos Díaz, Leticia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8074230/
https://www.ncbi.nlm.nih.gov/pubmed/33923711
http://dx.doi.org/10.3390/ijms22084144
_version_ 1783684307859013632
author Núñez-Montero, Kattia
Salazar, Rodrigo
Santos, Andrés
Gómez-Espinoza, Olman
Farah, Scandar
Troncoso, Claudia
Hoffmann, Catalina
Melivilu, Damaris
Scott, Felipe
Barrientos Díaz, Leticia
author_facet Núñez-Montero, Kattia
Salazar, Rodrigo
Santos, Andrés
Gómez-Espinoza, Olman
Farah, Scandar
Troncoso, Claudia
Hoffmann, Catalina
Melivilu, Damaris
Scott, Felipe
Barrientos Díaz, Leticia
author_sort Núñez-Montero, Kattia
collection PubMed
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 Online
Article
Text
id pubmed-8074230
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-80742302021-04-27 Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes Núñez-Montero, Kattia Salazar, Rodrigo Santos, Andrés Gómez-Espinoza, Olman Farah, Scandar Troncoso, Claudia Hoffmann, Catalina Melivilu, Damaris Scott, Felipe Barrientos Díaz, Leticia Int J Mol Sci Article 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. MDPI 2021-04-16 /pmc/articles/PMC8074230/ /pubmed/33923711 http://dx.doi.org/10.3390/ijms22084144 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Núñez-Montero, Kattia
Salazar, Rodrigo
Santos, Andrés
Gómez-Espinoza, Olman
Farah, Scandar
Troncoso, Claudia
Hoffmann, Catalina
Melivilu, Damaris
Scott, Felipe
Barrientos Díaz, Leticia
Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes
title 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_short Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes
title_sort antarctic rahnella inusitata: a producer of cold-stable β-galactosidase enzymes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8074230/
https://www.ncbi.nlm.nih.gov/pubmed/33923711
http://dx.doi.org/10.3390/ijms22084144
work_keys_str_mv AT nunezmonterokattia antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT salazarrodrigo antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT santosandres antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT gomezespinozaolman antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT farahscandar antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT troncosoclaudia antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT hoffmanncatalina antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT meliviludamaris antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT scottfelipe antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes
AT barrientosdiazleticia antarcticrahnellainusitataaproducerofcoldstablebgalactosidaseenzymes