• Korean Journal of Microbiology
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• v.52 no.3
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• pp.319-326
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• 2016

An antimicrobial bacterium to pathogenic microorganisms, strain $W5-1^T$ was isolated from Korean fermented-food Kimchi. The isolate was Gram-staining-variable, strictly aerobic, rod-shaped, endospore-forming, and motile with peritrichous flagella. It grew at $15-40^{\circ}C$, at pH 6.0-10.0, and in the presence of 0-4% NaCl. Strain $W5-1^T$ could hydrolyze esculin and xylan, and assimilate $\small{D}$-mannose, but not $\small{D}$-mannitol. Strain $W5-1^T$ showed antimicrobial activity against Listeria monocytogens, Pseudomonas aeruginosa, Staphylococcus aureus, and Salmonella typhi. The G+C content of the DNA of strains $W5-1^T$ was 52.6 mol%. The predominant respiratory quinone was menaquinone-7 (MK-7) and the major cellular fatty acids were $C_{16:0}$, antieiso-$C_{15:0}$, $C_{18:0}$, and $C_{12:0}$. The strain contained meso-diaminopimelic acid in cell-wall peptidoglycan. On the basis of 16S rRNA gene sequence and phylogenetic analysis, the strain W5-1 was shown to belong to the family Paenibacillaceae and was most closely related to Paenibacillus pinihumi $S23^T$ (98.4% similarity) and Paenibacillus tarimensis $SA-7-6^T$ (96.4%). The DNA-DNA relatedness between the isolate and Paenibacillus pinihumi $S23^T$ was 8.5%, indicating that strain $W5-1^T$ represented a species in the genus Paenibacillus. On the basis of the evidence from this polyphasic study, it is proposed that strain $W5-1^T$ is considered to represent a novel species of the genus Paenibacillus, for which the name Paenibacillus kimchicus sp. nov. is proposed. The type strain is $W5-1^T$ (=KACC $15046^T$ = $LMG 25970^T$).

• Journal of Life Science
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• v.27 no.7
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• pp.805-811
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• 2017

In the previous paper, we isolated a bacterium that can hydrolyze various organic materials from soybean paste, including cellulose, lipids, starch, and protein. The activity and chemical properties of the crude enzymes produced by the isolate Bacillus subtilis CK-2 were further investigated. Cellulase showed the highest activity at pH 5.0 and $55^{\circ}C$. The stability of cellulase was maintained within the ranges of pH 5.0~10.0 and $20{\sim}50^{\circ}C$. Cellulolytic enzymes were activated by a $Co^{2+}$ ion, demonstrating the highest activity at a 0.45%(w/v) concentration of $Co^{2+}$. The optimal conditions for amylase were pH 5.0 and $50^{\circ}C$. The activity of amylase was stable within the ranges of pH 4.0~5.0 and $20{\sim}50^{\circ}C$. The $Co^{2+}$ ion was also necessary for amylase activity, which was the highest at a 0.2%(w/v) concentration of $Co^{2+}$. The optimal pH and temperature conditions of protease were pH 8.0 and $50^{\circ}C$. The activity of protease was stable within the ranges of pH 7.0~8.5 and $20{\sim}50^{\circ}C$. Protease activity was catalyzed by $Mn^{2+}$, which was the highest at a 0.125%(w/v) concentration of $Mn^{2+}$. The isolate B. subtilis CK-2 demonstrated a high activity of autolysin. Based on these results, we identified and suggested the optimal pH, temperature, and metal ion concentration in the use of the hydrolytic enzymes of B. subtilis CK-2 for industrial purposes.

• Korean Chemical Engineering Research
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• v.50 no.1
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• pp.18-24
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• 2012

Lignocellulose is difficult to hydrolyze due to the presence of lignin and the technology developed for cellulose fermentation to ethanol is not yet economically viable. However, recent advances in the extremely new field of biotechnology for the ethanol production are making it possible to use of Agriculture residual biomass, e.q., Barley straw, because of their several superior aspects as Agriculture residual biomass; low lignin, high contents of carbohydrates. Barley straw consists of 39.78% cellulose (glucose), 22.56% hemicelluloses and 19.27% lignin. Pretreatment of barley straw using NaOH pretreatment solutions concentration with 2%, temperature $85^{\circ}C$ and reaction times 1 hr were investigates. $NH_4OH$ pretreatment condition was solutions concentration with 15%, temperature $60^{\circ}C$, and reaction times 24hr were investigates. Furthermore, enzymatic saccharification using cellulose at $50^{\circ}C$, pH 4.8, 180 rpm for conversion of cellulose contained in barley straw to monomeric sugar. The pretreatment of barley straw using NaOH and $NH_4OH$ can significantly improve enzymatic saccharification of barley straw by extract more lignin and increasing its accessibility to hydrolytic enzymes. The result showed NaOH pretreatment extracted yield of lignin was 24.15%. $NH_4OH$ pretreatment extracted yield of lignin was 29.09%. Shaccharification of barley straw pretreatment by NaOH for 72hr and pH 4.8 result in maximum glucose concentration 15.39g/L (58.40%) and by $NH_4OH$ for 72hr and pH 4.8 result in maximum glucose concentration 16.01g/L (64.78%).

• Journal of the Korean Chemical Society
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• v.32 no.6
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• pp.520-527
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• 1988

The crystal structures of $Co^{2+}\;and\;Ag^+\;exchanged\;zeolite\; A,\; Ag_6Co_3$-A(a = 12.131(5)$\AA$) and $Ag_3Co_{4.5}$-A(a = 12.145(1)$\AA$), have been determined by single crystal X-ray diffraction techniques. Both structures were solved and refined in the cubic space group Pm3m at 21(1)$^{\circ}C$. Full-matrix leastsquares refinement converged to the final error indices of R1 = 0.045 and R2 = 0.041 for $Ag_3Co_{4.5}-A,\; and\; R1 = 0.066\; and\; R2 = 0.076\; for\; Ag_6Co_3$-A using the 258 and 189 reflections, respectively, for which I > 3$\sigma$(I). Both structures indicate that CO(Ⅱ)ions are coordinated by three framework oxygens; the Co(II) to O(3) distances are 2.118(4)$\AA$ for $Ag_3Co_{4.5}$-A and 2.106(1)$\AA$ for $Ag_6Co_3-A$, respectively. In each structure, the angle substended at Co(II), O(3)-Co(II)-O(3) is ca 120°, close to the idealized trigonalplanar value. $Co^{2+}$ ions prefer to 6-ring sites and $Ag^+$ ions prefer to 8-ring site when total number of cations is more than 8. The crystals of hydrated and dehydrated $Ag_{12-2x}Co_x-A (x > 4.5)$ had no crystalline diffraction pattern, indicating the apparent exchange limit of $Co^{2+}\; into\; Ag_{12}-A\; is\; 4.5 Co^{2+}$ ions per unit cell. $Co^{2+}$ ions hydrolyze $H_2O$ molecules and $H_3O^+$ concentraction is accumulating. These $H_3O^+$ ions destroy the zeolite structures.

• Journal of Life Science
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• v.25 no.2
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• pp.237-242
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• 2015

The use of calcite-forming bacteria (CFB) in crack remediation and durability improvements in construction materials creates a permanent and environmentally-friendly material. Therefore, research into this type of application is stimulating interdisciplinary studies between microbiology and architectural engineering. However, the mechanisms giving rise to these materials are dependent on calcite precipitation by the metabolism of the CFB, which raises concerns about possible hazards to cement-based construction due to microbial metabolic acid production. The aim of this study was to determine target microorganisms that possibly can have bio-corrosive effects on cement mortar and to assess multi-functional CFBs for their safe application to cement structures. The chalky test was first used to evaluate the $CaCO_3$ solubilization feature of construction sites by fungi, yeast, bacterial strains. Not all bacterial strains are able to solubilize $CaCO_3$, but C. sphaerospermum KNUC253 or P. prolifica KNUC263 showed $CaCO_3$ solubilization activity. Therefore, these two strains were identified as target microorganisms that require control in cement structures. The registered patented strains Bacillus aryabhatti KNUC205, Arthrobacter nicotianae KNUC2100, B. thuringiensis KNUC2103 and Stenotrophomonas maltophilia KNUC2106, reported as multifunctional CFB (fungal growth inhibition, crack remediation, and water permeability reduction of cement surfaces) and isolated from Dokdo or construction site were unable to solubilize $CaCO_3$. Notably, B. aryabhatti KNUC205 and A. nicotianae KNUC2100 could not hydrolyze cellulose or protein, which can be the major constituent macromolecules of internal materials for buildings. These results show that several reported multi-functional CFB can be applied to cement structures or diverse building environments without corrosive or bio-deteriorative risks.

• Korean Journal of Food Science and Technology
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• v.53 no.6
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• pp.688-694
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• 2021

Turanose is a potential candidate for use as a functional sweetener because of its gentle taste, low calorie, and non-cariogenicity. The aim of this study was to replace sucrose with turanose to produce health-beneficial maesil-cheong. Quality effects of turanose on maesil-cheong were evaluated by determining the contents of free sugars, organic acids, amygdalin, and antioxidant activity. The pH and Brix values of sucrose- and turanose-based maesil-cheong remained at the same level between 2.83 and 3.00 and 54.6-58.6°Bx, respectively, after 90-day storage. Among oxalic, malic, and citric acids, citric acid content was the highest in both maesil-cheong samples. Turanose did not significantly hydrolyze in maesil-cheong, whereas sucrose was completely hydrolyzed to glucose and fructose. Thus, turanose is suitable for the development of acidic maesil-cheong to improve its health promoting effect. Turanose showed product qualities similar to sucrose-based maesil-cheong. Turanose can be used as a functional sweetener or bulking agent in processed foods.

• Journal of Life Science
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• v.31 no.3
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• pp.356-365
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• 2021

Recently, we sequenced the entire genome of a freshwater agar-degrading bacterium Cellvibrio sp. KY-GH-1 (KCTC13629BP) to explore genetic information encoding agarases that hydrolyze agarose into monomers 3,6-anhydro-L-galactose (L-AHG) and D-galactose. The KY-GH-1 strain appeared to possess nine β-agarase genes and two α-neoagarobiose hydrolase (α-NABH) genes in a 77-kb agarase gene cluster. Based on these genetic information, the KY-GH-1 strain-caused agarose degradation into L-AHG and D-galactose was predicted to be initiated by both endolytic GH16 and GH86 β-agarases to generate NAOS (NA4/NA6/NA8), and further processed by exolytic GH50 β-agarases to generate NA2, and then terminated by GH117 α-NABHs which degrade NA2 into L-AHG and D-galactose. More recently, by employing E. coli expression system with pET-30a vector we obtained three recombinant His-tagged GH50 family β-agarases (GH50A, GH50B, and GH50C) derived from Cellvibrio sp. KY-GH-1 to compare their enzymatic properties. GH50A β-agarase turned out to have the highest exolytic β-agarase activity among the three GH50 isozymes, catalyzing efficient NA2 production from the substrate (agarose, NAOS or AOS). Additionally, we determined that GH117A α-NABH, but not GH117B α-NABH, could potently degrade NA2 into L-AHG and D-galactose. Sequentially, we examined the enzymatic characteristics of GH50A β-agarase and GH117A α-NABH, and assessed their efficiency for NA2 production from agarose and for production of L-AHG and D-galactose from NA2, respectively. In this review, we describe the benefits of recombinant GH50A β-agarase and GH117A α-NABH originated from Cellvibrio sp. KY-GH-1, which may be useful for the enzymatic hydrolysis of agarose for mass production of L-AHG and D-galactose.

• Journal of Life Science
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• v.33 no.4
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• pp.357-362
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• 2023

This report looks at an agar-degrading marine bacterium and characterization of its agarase. Agar-degrading marine bacterium JS-1 was isolated with Marine agar 2216 media from seawater from the seashore of Sojuk-do, Changwon in Gyeongnam Province, Korea. The agar-degrading bacterium was named as Agarivorans sp. JS-1 by phylogenetic analysis based on 16S rRNA gene sequencing. The extracellular agarase was prepared from the culture media of Agarivorans sp. JS-1 and used for characterization. Relative activities at 20℃, 30℃, 35℃, 40℃, 45℃, 50℃, 55℃, and 60℃ were 70%, 74%, 78%, 83%, 87%, 100%, 74%, and 66%, respectively. Relative activities at pH 5, 6, 7, and 8 were 91%, 100%, 90%, and 89%, respectively. Its extracellular agarase showed maximum activity (207 units/l) at pH 6.0 and 50℃ in 20 mM Tris-HCl buffer. The residual activity after heat treatment at 20℃, 30℃, and 50℃ for 30 minutes was 90%, 70%, and 50% or more, respectively. After a 2-hour heat treatment at 20℃, 30℃, 35℃, 40℃, and 45℃, the residual activity was 80%, 68%, 65%, 63%, and 57%, respectively. At 50℃ and above, after heat treatment for 30 minutes, the residual activity was below 60%. Thin layer chromatography analysis suggested that Agarivorans sp. JS-1 produces extracellular β-agarases as they hydrolyze agarose to produce neoagarooligosaccharides such as neoagarohexaose (20.6%), neoagarotetraose (58.5%), and neoagarobiose (20.9%). Agarivorans sp. JS-1 and its thermotolerant β-agarase would be useful in the production of neoagarooligosaccharides, showing functional activity such as inhibition of bacterial growth and delay of starch degradation.