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  • Title: Characterization of a Novel Neoagarobiose-Producing GH42 β-Agarase, AgaJ10, from Gayadomonas joobiniege G7.
    Author: Choi U, Jung S, Hong SK, Lee CR.
    Journal: Appl Biochem Biotechnol; 2019 Sep; 189(1):1-12. PubMed ID: 30854607.
    Abstract:
    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.
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