Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

• Published in: Polar Research
• Main Authors: Mauro Tropeano, Silvia Coria, Adrián Turjanski, Daniel Cicero, Andrés Bercovich, Walter Mac Cormack, Susana Vázquez
• Format: Article in Journal/Newspaper
• Language: English
• Published: Norwegian Polar Institute 2012
• Subjects: Microbial enzymes; Antarctic bacteria; marine bacteria; cold enzymes; psychrophiles; Environmental sciences; GE1-350; Oceanography; GC1-1581; Antarctic; Potter Cove; South Shetland Islands; Antarc*; Antarctica; Polar Research
• Online Access: https://doi.org/10.3402/polar.v31i0.18507; https://doaj.org/article/f1f3a91be7df40048855db1143dcaaab

Affiliations of the dominant culturable bacteria isolated from Potter Cove, South Shetland Islands, Antarctica, were investigated together with their production of cold-active hydrolytic enzymes. A total of 189 aerobic heterotrophic bacterial isolates were obtained at 4°C and sorted into 63 phylotypes based on their amplified ribosomal DNA restriction analysis profiles. The sequencing of the 16S rRNA genes of representatives from each phylotype showed that the isolates belong to the phyla Proteobacteria (classes Alpha- and Gamma-proteobacteria), Bacteroidetes (class Flavobacteria), Actinobacteria (class Actinobacteria) and Firmicutes (class Bacilli). The predominant culturable group in the site studied belongs to the class Gammaproteobacteria, with 65 isolates affiliated to the genus Pseudoalteromonas and 58 to Psychrobacter. Among the 189 isolates screened, producers of amylases (9.5%), pectinases (22.8%), cellulases (14.8%), CM-cellulases (25.4%), xylanases (20.1%) and proteases (44.4%) were detected. More than 25% of the isolates produced at least one extracellular enzyme, with some of them producing up to six of the tested extracellular enzymatic activities. These results suggest that a high culturable bacterial diversity is present in Potter Cove and that this place represents a promising source of biomolecules.