TY - JOUR
T1 - Antarctic rahnella inusitata
T2 - A producer of cold-stable β-galactosidase enzymes
AU - Núñez-Montero, Kattia
AU - Salazar, Rodrigo
AU - Santos, Andrés
AU - Gómez-Espinoza, Olman
AU - Farah, Scandar
AU - Troncoso, Claudia
AU - Hoffmann, Catalina
AU - Melivilu, Damaris
AU - Scott, Felipe Ignacio
AU - Díaz, Leticia Barrientos
N1 - Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/4/16
Y1 - 2021/4/16
N2 - 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 pro-duce 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.
AB - 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 pro-duce 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.
KW - Antarctica
KW - Cold-adapted bacteria
KW - Extremozymes
KW - Galactosidase
KW - Lactose
UR - http://www.scopus.com/inward/record.url?scp=85104302322&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/e5db7f7f-9eb1-3f53-9e67-1f8c45a0178a/
U2 - 10.3390/ijms22084144
DO - 10.3390/ijms22084144
M3 - Article
C2 - 33923711
AN - SCOPUS:85104302322
SN - 1661-6596
VL - 22
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 8
M1 - 4144
ER -