RESUMO

An extracellular ß-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 Mg(2+), Mn(2+), K(+); Ca(2+), Na(+), Ba(2+), Zn(2+), Cu(2+), Co(2+), Fe(2+), Sr(2+) 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.

Assuntos

Adaptação Fisiológica/fisiologia , Ágar/metabolismo , Glicosídeo Hidrolases/metabolismo , Pseudoalteromonas/enzimologia , Adaptação Fisiológica/genética , Regiões Antárticas , Proteínas de Bactérias/metabolismo , Temperatura Baixa , Dissacarídeos/biossíntese , Sedimentos Geológicos/microbiologia , Glicosídeo Hidrolases/isolamento & purificação , Hidrólise , RNA Ribossômico 16S/genética

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.

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Assuntos

Adaptação Fisiológica/fisiologia , Ágar/metabolismo , Glicosídeo Hidrolases/metabolismo , Pseudoalteromonas/enzimologia , Regiões Antárticas , Adaptação Fisiológica/genética , Proteínas de Bactérias/metabolismo , Temperatura Baixa , Dissacarídeos/biossíntese , Sedimentos Geológicos/microbiologia , Glicosídeo Hidrolases/isolamento & purificação , Hidrólise , /genética

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)

Assuntos

Adaptação Fisiológica/fisiologia , Ágar/metabolismo , /metabolismo , Pseudoalteromonas/enzimologia , Adaptação Fisiológica/genética , Regiões Antárticas , Proteínas de Bactérias/metabolismo , Temperatura Baixa , Dissacarídeos/biossíntese , Sedimentos Geológicos/microbiologia , Glicosídeo Hidrolases/isolamento & purificação , Hidrólise , /genética