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- Title
Overexpression and characterization of a novel GH16 β-agarase (Aga1) from Cellulophaga omnivescoria W5C.
- Authors
Ramos, Kristine Rose M.; Valdehuesa, Kris Niño G.; Bañares, Angelo B.; Nisola, Grace M.; Lee, Won-Keun; Chung, Wook-Jin
- Abstract
Objective: To identify and characterize a new β-agarase from Cellulophaga omnivescoria W5C capable of producing biologically-active neoagarooligosaccharides from agar. Results: The β-agarase, Aga1, has signal peptides on both N- and C-terminals, which are involved in the type IX secretion system. It shares 75% protein sequence identity with AgaD from Zobellia galactanivorans and has a molecular weight of 54 kDa. Biochemical characterization reveals optimum agarolytic activities at pH 7–8 and temperature 30–45 °C. Aga1 retains at least 33% activity at temperatures lower than the sol–gel transition state of agarose. Metal ions are generally not essential, but calcium and potassium enhance its activity whereas iron and zinc are inhibitory. Finally, hydrolysis of agarose with Aga1 yields neoagarotetraose, neoagarohexaose, and neoagarooctaose. Conclusions: Aga1 displays unique traits such as moderate psychrophilicity, stability, and synergy with other agarases, which makes it an excellent candidate for biosynthetic production of neoagarooligosaccharides from agar.
- Subjects
SIGNAL peptides; MOLECULAR weights; AMINO acid sequence; LOW temperatures; METAL ions
- Publication
Biotechnology Letters, 2020, Vol 42, Issue 11, p2231
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-020-02933-x