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Characterization of α-agarase from Alteromonas sp. SH-1
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  • Journal title : KSBB Journal
  • Volume 31, Issue 2,  2016, pp.113-119
  • Publisher : Korean Society for Biotechnology and Bioengineering
  • DOI : 10.7841/ksbbj.2016.31.2.113
 Title & Authors
Characterization of α-agarase from Alteromonas sp. SH-1
Lee, Sol-Ji; Shin, Da-Young; Kim, Jae-Deog; Lee, Dong-Geun; Lee, Sang-Hyeon;
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 Abstract
A novel agar-degrading marine bacterium, SH-1 strain, was isolated from seashore of Namhae at Gyeongnam province, Korea. The SH-1 strain exhibited 98% similarity with Alteromonas species based on 16S rDNA sequencing and named as Alteromonas sp. SH-1. Alteromonas sp. SH-1 showed agarase activity of 348.3 U/L (1.67 U/mg protein). The molecular masses of the enzymes were predicted as about 85 kDa and 110 kDa by SDS-PAGE and zymogram. The enzymatic activity was optimal at and the relative agarase activity was decreased as temperature increase from and thus about 90% and 70% activities were shown at and , respectively. The optimum pH was 6.0 for agarase activity in 20 mM Tris-HCl buffer and activities were less than 70% and 85% activity at pH 5.0 and pH 7.0, respectively, compared with that at pH 6. Agarase activity has remained over 90% at after 1.5 hour exposure at this temperature. However, its activity was less than 60% at after 0.5 h exposure at this temperature. The enzymes produced agarooligosaccharides such as agaropentaose and agarotriose from agarose, indicating that the agarases are -agarases. Thus, Alteromonas sp. SH-1 and its agarases would be useful for the industrial production of agarooligosaccharides which are known as having anticancer and antioxidation activities.
 Keywords
-Agarase;agaropentaose;agarooligosaccharide;Alteromonas sp. SH-1;marine derived bacterium;
 Language
Korean
 Cited by
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