|
KMID : 0545120180280020284
|
|
Journal of Microbiology and Biotechnology
2018 Volume.28 No. 2 p.284 ~ p.292
|
|
|
Biochemical Characterization of a Novel GH86 β-Agarase Producing Neoagarohexaose from Gayadomonas joobiniege G7
|
|
Lee Yeong-Rim
Jung Su-Bin
Chi Won-Jae
Bae Chang-Hwan
Jeong Byeong-Chul
Hong Soon-Kwang
Lee Chang-Ro
|
|
|
Abstract
|
|
|
|
A novel β-agarase, AgaJ5, was identified from an agar-degrading marine bacterium, Gayadomonas joobiniege G7. It belongs to the glycoside hydrolase family 86 and is composed of 805 amino acids with a 30-amino-acid signal peptide. Zymogram analysis showed that purified AgaJ5 has agarase activity. The optimum temperature and pH for AgaJ5 activity were determined to be 30°C and 4.5, respectively. AgaJ5 was an acidic β-agarase that had strong activity at a narrow pH range of 4.5-5.5, and was a cold-adapted enzyme, retaining 40% of enzymatic activity at 10°C. AgaJ5 required monovalent ions such as Na+ and K+ for its maximum activity, but its activity was severely inhibited by several metal ions. The Km and Vmax of AgaJ5 for agarose were 8.9 mg/ml and 188.6 U/mg, respectively. Notably, thin-layer chromatography, mass spectrometry, and agarose-liquefication analyses revealed that AgaJ5 was an endo-type β-agarase producing neoagarohexaose as the final main product of agarose hydrolysis. Therefore, these results suggest that AgaJ5 from G. joobiniege G7 is a novel endotype neoagarohexaose-producing β-agarase having specific biochemical features that may be useful for industrial applications.
|
|
|
KEYWORD
|
|
|
agar, β-agarase, GH86, Gayadomonas joobiniege
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|