Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil

Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus(99%), with query coverage o...

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Bibliographic Details
Published in:Anais da Academia Brasileira de Ciências
Main Authors: Anderson F. Santos, Fabiano Pires, Hugo E. Jesus, André L.S. Santos, Raquel Peixoto, Alexandre S. Rosado, Claudia M. D'Avila-Levy, Marta H. Branquinha
Format: Article in Journal/Newspaper
Language:English
Published: Academia Brasileira de Ciências 2015
Subjects:
Q
Online Access:https://doi.org/10.1590/0001-3765201520130519
https://doaj.org/article/0c2a0bb3695f425e858ac36c03bf4ed6
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Summary:Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus(99%), with query coverage of 99% and 98%, respectively.The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticusalso showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes.