• Journal of Life Science
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• v.22 no.12
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• pp.1724-1728
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• 2012

A marine bacterial strain that degraded fucoidan from Ecklonia cava was isolated from seawater. The crude fucoidanase of this strain efficiently degraded fucoidan at pH 8 and $50^{\circ}C$. The crude enzyme hydrolyzed 7.1% (w/w) fucoidan within 24 hrs from an 1% (w/v) fucoidan solution and produced oligosaccharides by endo-type hydrolysis as the reaction products. The results of 16S rRNA gene sequence analysis and biochemical tests permitted a tentative identification of strain SB 1493 as a Pseudoalteromonas species.

• Fisheries and Aquatic Sciences
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• v.6 no.1
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• pp.1-6
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• 2003

A chitinolytic enzyme-producing bacterium was isolated from sea water on the coast of Busan. The bacterium was identified as Aeromonas sp. based on its morphological, cultural and biochemical characteristics and designated Aeromonas sp. J-5003. The strain produced two chitinoloytic enzymes: chitinase and chitobiase. The optimum culture conditions of the strain for production of chitinoloytic enzymes were investigated. For the production of chitinase, the major components of medium were colloidal chitin $0.5\%$, glucose $0.2\%$, yeast extract $0.25\%$ and peptone $0.25\%$ while for the production of chitobiase, they were colloidal chitin $0.5\%$, galactose and tryptone $0.2\%$. The optimum cultural temperature and initial pH for the production of chitinase and chitobiase were $30^{\circ}C$ and pH 7.0, respectively.

• Korean Journal of Microbiology
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• v.38 no.4
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• pp.224-224
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• 2002

Chitin-degrading marine bacterial strain 98CJ11027 was isolated from bryozoa from the coastal area of Cheju Island, Korea, and identified as a member of the genus Vibrio. The molecular mass of the main extracellular chitinase (chitinase I), purified from strain 98CJ11027, was estimated to be 98 kDa. The optimal condition for chitinase I activity is pH 6.0 and 45℃. The activity was inhibited by $Fe^+2$ and$Cu^+2$. Chitinase I displayed the hydrolysis type of chitobiosidase and catalyzed reversed hydrolysis leading to the synthesis of tetraacetylchitotetraose.

• KSBB Journal
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• v.14 no.5
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• pp.572-577
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• 1999

A marine bacterium with highly effective agar degrading activity was ioslated from the southern sea of Korea (Chonnam, YoChon) and identified as Cytophaga sp. and named as Cytophaga sp. AYK301. This strain produced an extracellular agarase which had a high activity with agar. The optimum culture conditions for the production of agarase have been determined. For the increase of agarase productivity, 0.2% agar, 0.3% beef extract, and 0.05% NH$_4$NO$_3$ were used as carbon, organic and inorganic nitrogen source, respectively. The optimal initial pH, NaCl, culture time and temperature for the agar degrading activity were 7.5, 7.0%, 36 hr and $25^{\circ}C$, respectively. In the optimal conditions, the agarase production was increased up to more than 4.0 folds as compared to that by the basal medium.

• Journal of Life Science
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• v.17 no.1 s.81
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• pp.70-75
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• 2007

A novel agar-degrading bacterium SL-5 was isolated from seashore of Homigot at Kyung-Buk province, and cultured in marine broth 2216 media. The bacterium SL-5 was identified as Thalassomonas genus by 16S rDNA sequencing with 96% identity. Growth rate was faster at $27^{\circ}C$ than at $37^{\circ}C$ and agarase was produced as growth-related. The optimum pH of the enzyme activity was 7.0 and the optimum temperature for the reaction was $40^{\circ}C$. Although the enzyme had no thermostability, the enzyme activity was remained over 80% at $60^{\circ}C$. The enzyme hydrolyzed neoagarohexaose to yield neoagarobiose as the main product, indicating that the enzyme is $\beta-agarase$. Thus, the enzyme would be useful for the industrial production of neoagarobiose.

• Journal of Microbiology and Biotechnology
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• v.23 no.7
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• pp.913-922
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• 2013

An agar-degrading bacterium was isolated from red seaweed (Gelidium amansii) on a natural seawater agar plate, and identified as Saccharophagus sp. AG21. The ${\beta}$-agarase gene from Saccharophagus sp. AG21 (agy1) was screened by long and accurate (LA)-PCR. The predicted sequence has a 1,908 bp open reading frame encoding 636 amino acids (aa), and includes a glycosyl hydrolase family 16 (GH16) ${\beta}$-agarase module and two carbohydrate binding modules of family 6 (CBM6). The deduced aa sequence showed 93.7% and 84.9% similarity to ${\beta}$-agarase of Saccharophagus degradans and Microbulbifer agarilyticus, respectively. The mature agy1 was cloned and overexpressed as a His-tagged recombinant ${\beta}$-agarase (rAgy1) in Escherichia coli, and had a predicted molecular mass of 69 kDa and an isoelectric point of 4.5. rAgy1 showed optimum activity at $55^{\circ}C$ and pH 7.6, and had a specific activity of 85 U/mg. The rAgy1 activity was enhanced by $FeSO_4$ (40%), KCl (34%), and NaCl (34%), compared with the control. The newly identified rAgy1 is a ${\beta}$-agarase, which acts to degrade agarose to neoagarotetraose (NA4) and neoagarohexaose (NA6) and may be useful for applications in the cosmetics, food, bioethanol, and reagent industries.

• Journal of Life Science
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• v.26 no.4
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• pp.453-459
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• 2016

Agarases are classified into α-agarase and β-agarase that produce agarooligosaccharides and neoagarooligosaccharides, respectively. Neoagarooligosaccharides have whitening effect of skin, delay of starch degradation, and inhibition of bacterial growth etc. Hence, the object of this study was to isolate a novel agarase producing marine bacterium and characterization of its β-agarase. A novel agar-degrading bacterium was isolated from seashore of Namhae at Gyeongnamprovine, Korea and purely cultured with Marine agar 2216 media. The isolated bacterium was identified as Simiduia sp. SH-4 after 16S rRNA gene sequencing. The enzymatic sample was obtained from culture media of Simiduia sp. SH-4. Enzymatic activity was highly increased from 20(30% relative activity) to 30℃ (100%) and decreased from 30 to 40℃(75%) and so more. Relative activity was 100% at pH 6 while those were about 91% and 59% at pH 5.0 and 7.0, respectively, meaning the enzyme possesses narrow optimal pH range. Hence, the enzyme exhibited the maximal activity with 120.4 units/l at pH 6.0 and 30℃ in 20 mM Tris-HCl buffer. Thin layer chromatography (TLC) analysis showed that Simiduia sp. SH-4 produces β-agarase, which hydrolyze agarose to produce biofunctional neoagarooligosaccharides such as neoagarotetraose and neoagarobiose. Hence, broad applications would be possible using Simiduia sp. SH-4 and its enzyme in the food industry, cosmetics and medical fields.

• Microbiology and Biotechnology Letters
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• v.39 no.3
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• pp.218-223
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• 2011

To obtain eicosapentaenoic acid (EPA)-producing bacteria, some 600 strains of bacteria were isolated from Antarctic sediment and marine organisms during the summer expedition of 1999-2000 and 7 EPA-producing bacteria were obtained through screening with TLC and GC. A strain designated as L93 showed the highest EPA production, which was gram-negative, rod-shaped bacterium. L93 strain was identified as Shewanella sp., from the sequence analysis of 16S rDNA. Optimal conditions temperature and pH for the growth and EPA production were about $4^{\circ}C$ and pH 7. In addition, its production was optimized by 50%(w/v) sea salt. We establish the optimal production system to produce about 320 mg per liter by using this optimal EPA production conditions. EPA-methyl ester was purified from cultured L93 strain to a purity of higher than 97% and typical purification yield is greater than 72% of the input amount via urea complexation and HPLC.

• Journal of Microbiology and Biotechnology
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• v.29 no.2
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• pp.235-243
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• 2019

A special eosinophilic agarase exo-type ${\beta}$-agarase gene, AgaDL6, was cloned from a marine agar-degrading bacterium, Flammeovirga sp. HQM9. The gene comprised 1,383-bp nucleotides encoding a putative agarase AgaDL6 of 461 amino acids with a calculated molecular mass of 52.8 kDa. Sequence analysis revealed a ${\beta}$-agarase domain that belongs to the glycoside hydrolase family (GH) 16 and a carbohydrate-binding module (CBM_4_9) unique to agarases. AgaDL6 was heterologously expressed in Escherichia coli BL21 (DE3). Enzyme activity analysis of the purified protein showed that the optimal temperature and pH of AgaDL6 were $50^{\circ}C$ and 3.0, respectively. AgaDL6 showed thermal stability by retaining more than 98% of activity after incubation for 2 h at $50^{\circ}C$, a feature quite different from other agarases. AgaDL6 also exhibited outstanding acid stability, retaining 100% of activity after incubation for 24 h at pH 2.0 to 5.0, a property distinct from other agarases. This is the first agarase characterized to have such high acid stability. In addition, we observed no obvious stimulation or inhibition of AgaDL6 in the presence of various metal ions and denaturants. AgaDL6 is an exo-type ${\beta}$-1,4 agarase that cleaved agarose into neoagarotetraose and neoagarohexaose as the final products. These characteristics make AgaDL6 a potentially valuable enzyme in the cosmetic, food, and pharmaceutical industries.

• Microbiology and Biotechnology Letters
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• v.34 no.1
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• pp.1-6
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• 2006

Harmful algal blooms (HABs or red tides), caused by uncontrolled proliferation of marine phytoplankton, impose a severe environmental problem and occasionally threaten even public health. We sequenced the genome of an EPS-producing marine bacterium Hahella chejuensis that produces a red pigment with the lytic activity against red-tide dinoflagellates at parts per billion level. H. chejuensis is the first sequenced species among algicidal bacteria as well as in the order Oceanospirillales. Sequence analysis indicated a distant relationship to the Pseudomonas group. Its 7.2-megabase genome encodes basic metabolic functions and a large number of proteins involved in regulation or transport. One of the prominent features of the H. chejuensis genome is a multitude of genes of functional equivalence or of possible foreign origin. A significant proportion (${\sim}23%$) of the genome appears to be of foreign origin, i.e. genomic islands, which encode genes for biosynthesis of exopolysaccharides, toxins, polyketides or non-ribosomal peptides, iron utilization, motility, type III protein secretion and pigment production. Molecular structure of the algicidal pigment was determined to be prodigiosin by LC-ESI-MS/MS and NMR analyses. The genomics-based research on H. chejuensis opens a new possibility for controlling algal blooms by exploiting biotic interactions in the natural environment and provides a model in marine bioprospecting through genome research.