Agarolytic bacterium Persicobacter sp. CCB‐QB2 exhibited a diauxic growth involving galactose utilization pathway

  title={Agarolytic bacterium Persicobacter sp. CCB‐QB2 exhibited a diauxic growth involving galactose utilization pathway},
  author={Go Furusawa and Nyok-Sean Lau and Appalasamy Suganthi and A. A. Amirul},
The agarolytic bacterium Persicobacter sp. CCB‐QB2 was isolated from seaweed (genus Ulva) collected from a coastal area of Malaysia. Here, we report a high‐quality draft genome sequence for QB2. The Rapid Annotation using Subsystem Technology (RAST) annotation server identified four β‐agarases (PdAgaA, PdAgaB, PdAgaC, and PdAgaD) as well as galK, galE, and phosphoglucomutase, which are related to the Leloir pathway. Interestingly, QB2 exhibited a diauxic growth in the presence of two kinds of… 
Biochemical Characterization of Thermostable and Detergent-Tolerant β-Agarase, PdAgaC, from Persicobacter sp. CCB-QB2
Although the major hydrolytic product was neoagarobiose (NA2), monomeric sugar was also detected by thin-layer chromatographic analysis, indicating the agarase may play an important role in the diauxic growth.
Agarase Production by Marine Pseudoalteromonas sp. MHS: Optimization, and Purification
Biomass of the red alga Pterocladia capillacea proved to be a suitable substrate for agarase production using Pseudoalteromonas sp.
Crystal structure of a neoagarobiose-producing GH16 family β-agarase from Persicobacter sp. CCB-QB2
The crystal structure of PdAgaC’s catalytic domain, which has one of the highest Vmax value at 2.9 × 103 U/mg, was determined in order to understand its unique mechanism.
Enhanced anti-oxidant activity of neoagarooligosaccharides produced by β-agarase derived from Aquimarina agarilytica NI125
Results obtained suggest the potential application of the produced neoagarooligosaccharides anti-oxidants as promising additives in food and feed products.
Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2
AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains — a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32)
Biphasic cellular adaptations and ecological implications of Alteromonas macleodii degrading a mixture of algal polysaccharides
Distinct temporal changes in exometabolome composition, including the alginate/pectin-specific secretion of pyrroloquinoline quinone, suggest that substrate-dependent adaptations influence chemical interactions within the community, and contribute to the understanding of bacteria–algae interactions and the remineralization of chemically diverse polysaccharide pools, a key step in marine carbon cycling.
Mono-specific algal diets shape microbial networking in the gut of the sea urchin Tripneustes gratilla elatensis
The dense and well-connected microbial network in the gut of Ulva-fed sea urchin Tripneustes gratilla elatensis, together with animal's rapid growth, may suggest that this alga was most nutritious among the experimental diets.
Climate Change Effects and Marine Renewable Energy Important Topics Targeted by the Journal of Marine Science
  • E. Rusu
  • Environmental Science
    Journal of Marine Science
  • 2022


Production and Characterization of a Novel Thermostable Extracellular Agarase from Pseudoalteromonas hodoensis Newly Isolated from the West Sea of South Korea
Thin-layer chromatography analysis, mass spectrometry, and enzyme assay revealed that AgaA7 is both an exo- and endo-type β-agarase that degrades agarose into neoagarotetraose, neoagarohexaose, and neoagarooctaose (minor).
Genomic and Proteomic Analyses of the Agarolytic System Expressed by Saccharophagus degradans 2-40
The agarolytic system of S. degradans 2-40 is predicted to be composed of a secreted endo-acting GH16-dependent depolymerase, a surface-associated GH50-dependent depot, an exo- acting GH86-dependent agarase, and an α-neoagarobiose hydrolase to release galactose from agarose.
Gene cloning, expression and characterization of a neoagarotetraose-producing β-agarase from the marine bacterium Agarivorans sp. HZ105
The agarase rHZ2 degraded agarose and neoagarooligosaccharides with degrees of polymerization above four, to yield neoagarotetraose as the dominant product, which was different from β-agarase agaB of Vibrio sp.
Identification of a Marine AgarolyticPseudoalteromonas Isolate and Characterization of Its Extracellular Agarase
The phenotypic and agarolytic features of an unidentified marine bacteria that was isolated from the southern Pacific coast was investigated and this strain was identified as Pseudoalteromonas antarcticastrain N-1, gram negative, obligately aerobic, and polarly flagellated.
Purification and characterization of the alpha-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B.
The phenotypic features of strain GJ1B, an unidentified marine bacterium that degrades agar, were investigated and its agarolytic system was characterized using 13C-NMR spectroscopy to analyse the agarose degradation products.
Overexpression and Characterization of a Novel Thermostable β-Agarase YM01-3, from Marine Bacterium Catenovulum agarivorans YM01T
The present study highlights a thermostable agarase with great potential application value in industrial production, YM01-3, which was cloned and expressed in Escherichia coli and was stable below 50 °C and retained 13% activity after incubation at 80 °C for 1 h, characteristics much different from other agarases.
Purification and Characterisation of a Novel Agarase Secreted by a Marine Bacterium, Pseudoalteromonas sp. Strain CKT1.
A marine bacterium which grows on agar as its sole carbon and energy source shows an agar liquefying ability, which is found to be an endo-type agarase which hydrolyses agar and agarose to yield galactose, neoagarobiose and a trace amount of neoagarohexaose.
[Isolation, identification and agarose degradation of a polysaccharide-degrading marine bacterium Persicobacter sp. JZB09].
OBJECTIVE To isolate and identify a versatile carbohydrate-degrading bacterium from marine environments, and characterize the extracellular agarase activity. METHODS The I2 staining method was