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Purification and characterization of cold-adapted beta-agarase from an Antarctic psychrophilic strain

Li, Jiang; Hu, Qiushi; Li, Yuquan; Xu, Yuan.
Braz. J. Microbiol.; 46(3): 683-690, July-Sept. 2015. tab, ilus
Artigo em Inglês | VETINDEX | ID: vti-14832

Resumo

An extracellular β-agarase was purified from Pseudoalteromonas sp. NJ21, a Psychrophilic agar-degrading bacterium isolated from Antarctic Prydz Bay sediments. The purified agarase (Aga21) revealed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with an apparent molecular weight of 80 kDa. The optimum pH and temperature of the agarase were 8.0 and 30 °C, respectively. However, it maintained as much as 85% of the maximum activities at 10 °C. Significant activation of the agarase was observed in the presence of Mg2+, Mn2+, K+; Ca2+, Na+, Ba2+, Zn2+, Cu2+, Co2+, Fe2+, Sr2+ and EDTA inhibited the enzyme activity. The enzymatic hydrolyzed product of agar was characterized as neoagarobiose. Furthermore, this work is the first evidence of cold-adapted agarase in Antarctic psychrophilic bacteria and these results indicate the potential for the Antarctic agarase as a catalyst in medicine, food and cosmetic industries..(AU)
Biblioteca responsável: BR1.1
Localização: BR68.1