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Biochemical Characterization of Thermostable and Detergent-Tolerant β-Agarase, PdAgaC, from Persicobacter sp. CCB-QB2

Hafizah, Nur Fazli, Teh, Aik-Hong, Furusawa, Go
Applied biochemistry and biotechnology 2019 v.187 no.3 pp. 770-781
Flammeovirga, Persicobacter, active sites, agarose, bacteria, beta-agarase, copper, detergents, developmental stages, genome, glycosides, iron, nickel, octoxynol, second growth, sugars, thermal stability, thin layer chromatography, tryptones
Persicobacter sp. CCB-QB2 belonging to the family Flammeovirga is an agarolytic bacterium and exhibits a diauxic growth in the presence of tryptone and agarose. A glycoside hydrolase (GH) 16 β-agarase, PdAgaC, was identified in the genome of the bacterium and was highly expressed during the second growth phase, indicating the agarase may play an important role in the diauxic growth. In this study, the catalytic domain of PdAgaC (PdAgaCgh) was cloned and characterized. PdAgaCgh showed thermostability at 50 °C and tolerance towards several detergents. In addition, the activity of PdAgaCgh after incubation with 0.1% of SDS and Triton X-100 increased approximately 1.2-fold. On the other hand, PdAgaCgh was sensitive to Fe²⁺, Ni²⁺, and Cu²⁺. The Kₘ and Vₘₐₓ of PdAgaCgh were 5.15 mg/ml and 2.9 × 10³ U/mg, respectively. Interestingly, although the major hydrolytic product was neoagarobiose (NA2), monomeric sugar was also detected by thin-layer chromatographic analysis.