Characterization of a Novel Neoagarobiose-Producing GH42 β-Agarase, AgaJ10, from Gayadomonas joobiniege G7

  • Umji Choi
  • Subin Jung
  • Soon-Kwang Hong
  • Chang-Ro LeeEmail author


Gayadomonas joobiniege G7 is an agar-degrading bacterium, which produces various agarases that have been biochemically characterized recently. In this study, we biochemically characterized a new β-agarase AgaJ10 belonging to the glycoside hydrolase (GH) 42 family from G. joobiniege G7. AgaJ10 is composed of 762 amino acids (89 kDa) and has the highest similarity (63% identity) to a putative β-agarase from the agar-degrading bacterium Catenovulum sp. DS-2, which was obtained from the intestines of a Haliotis diversicolor. The optimal pH and temperature for AgaJ10 activity were determined to be 5.0 and 30 °C, respectively. AgaJ10 exhibited a cold tolerance, retaining more than 40% of its enzymatic activity at 5 °C. The Km and Vmax of AgaJ10 for agarose were 61.5 mg/mL and 294.1 U/mg, respectively. Notably, the activity of AgaJ10 was significantly enhanced by Mn2+ but was strongly inhibited by some metal ions, including Fe2+, Ni2+, and Cu2+. Agarose-liquefaction, mass spectrometry, and thin-layer chromatography analyses showed that AgaJ10 is an exo-type β-agarase that hydrolyzes agarose only into neoagarobiose. Therefore, this study is the first report of a GH42 β-agarase that catalyzes a neoagarobiose-producing exo-type reaction.


Agar β-agarase GH42 Gayadomonas joobiniege 


Funding information

This work was supported by the 2016 Research Fund of Myongji University.

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no competing interests.

Ethics Approval

This article does not contain any studies with human participants performed by any of the authors.


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Authors and Affiliations

  1. 1.Department of Biological SciencesMyongji UniversityYonginRepublic of Korea

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