• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.4
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• pp.648-652
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• 2002

Removing shup from oyster by aeration method and coating with edible coating materials were investigated to improve oyster quality for the retort processing. Aeration rate and pore size of nozzle were critical factors to remove shup by aeration method. Optimum aeration rate and nozzle size were 45 L/min and 0.4 mm, respectively, when aeration was peformed two times and each operation maintained for 1 minute. Sodium alginate (SA) was used for oyster as the basal coating material. However, SA affected mouth-feel when it was applied at high concentrations. Sub-coating materials including skim milk, waxy corn starch, Purity CSC, white corn starch and carboxymethylcellulose (CMC) in decreasing order showed a positive effect on improving coatability and mouth-feel. Therefore, it is suggested that 1.5% SA and 0.9% skim milk should be the optimum composition of coating materials for oyster. Browning and syneresis of the porridge containing the coated oyster were considerably inhibited as compared with the sample without the coated oyster.

• Korean Journal of Food Science and Technology
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• v.33 no.6
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• pp.664-668
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• 2001

The physical and chemical stabilities of carthamin of red pigment from safflower petals were investigated at various conditions of pHs, temperatures, inorganic ions, sugars, light and polysaccharides. The half-life values at pH 3.0, 5.0, 9.0 and 11.0 were 5.3, 5.0, 11.0 and 45.0 h, respectively, at $25^{\circ}C$. Therefore, carthamin is unstable at acidic condition. Carthamin was red, orange and yellow at acidic, neutral and alkaline solutions, respectively. At pH 3.0, carthamin was thermally unstable and the half lives were 3.62, 9.05 and 48.2min at $90^{\circ}C$, $70^{\circ}C$ and $50^{\circ}C$, respectively. Among various inorganic ions, $Al^{3+}$ stabilized carthamin at acidic condition. At pH 5.0, carboxymethylcellulose prolonged the half-lives of carthamin at $25{\sim}90^{\circ}C$. Carthamin was very sensitive to light (20,000 lux) and the half-life was 2.32 min at pH 3.0.

• Journal of Life Science
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• v.27 no.9
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• pp.1003-1010
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• 2017

An open reading frame coding for mannanase predicted from the partial genomic sequence of Paenibacillus woosongensis was cloned into Escherichia coli by polymerase chain reaction amplification, and completely sequenced. This mannanase gene, designated man26AT, consisted of 3,162 nucleotides encoding a polypeptide of 1,053 amino acid residues. Based on the deduced amino acid sequence, Man26AT was identified as a modular enzyme, which included a catalytic domain belonging to the glycosyl hydrolase family 26 and two carbohydrate-binding modules, CBM27 and CBM11. The amino acid sequence of Man26AT was homologous to that of several putative mannanases, with identity of 81% for P. ihumii and identity of less than 57% for other strains of Paenibacillus. A cell-free extract of recombinant E. coli carrying the man26AT gene showed maximal mannanase activity at $55^{\circ}C$ and pH 5.5. The enzyme retained above 80% of maximal activity after preincubation for 1 h at $50^{\circ}C$. Man26AT was comparably active on locust bean gum (LBG), galactomanan, and kojac glucomannan, whereas it did not exhibit activity on carboxymethylcellulose, xylan, or para-nitrophenyl-${\beta}$-mannopyranoside. The common end products liberated from mannooligosaccharides, including mannotriose, mannotetraose, mannopentaose, and mannohexaose, or LBG by Man26AT were mannose, mannobiose, and mannotriose. Mannooligosacchrides larger than mannotriose were found in enzymatic hydrolyzates of LBG and guar gum, respectively. However, Man26AT was unable to hydrolyze mannobiose. Man26AT was intracellularly degraded into at least three active proteins with different molecular masses by zymogram.

• The Korean Journal of Mycology
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• v.42 no.4
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• pp.312-321
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• 2014

Tricholoma bakamatsutake is one of the edible ectomycorrhizal mushrooms as an allied species of Tricholoma matsutake. This is the first report on physical characteristics of T. bakamatsutake strains collected from Quercus mongolica forests in Korea. The pure cultures of these strains were isolated from the tissues of fruit bodies and the culture characteristics were investigated under different conditions (media, temperatures, nitrogen sources). Most strains showed the highest mycelial growth on potato dextrose agar (PDA) at 20 or $25^{\circ}C$. Two strains of T. bakamatsutake preferred the ammonium-form rather than the nitrate-form as an inorganic nitrogen source. T. bakamatsutake showed significantly slower mycelial growth when compared with T. matsutake from a Korean forest, although the optimum culture conditions for the two allied species were similar. We also tested the ability to form mycorrhizae as well as cellulase activity of T. bakamatsutake. All strains showed cellulase activity on a carboxymethylcellulose (CMC) agar plate. The mycorrhizae on axenic Pinus densiflora seedlings were formed by two strains of T. bakamatsutake after 3 or 8 months of inoculation. P. densiflora seedlings inoculated with T. bakamatsutake had a much higher biomass than un-inoculated seedlings.

• Horticultural Science & Technology
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• v.16 no.2
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• pp.222-225
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• 1998

The objective of this study was to observe the effects of potassium-carboxymethyl cellulose (K-CMC), which is a natural polymer derivative, and polyacrylamide (PAM), which is a commercial synthetic polymer, on soil physicochemical properties and yields of the cabbage. To increase water absorbing capacity (WAC), hydrophilic carboxymethyl group was introduced to cellulose chain and it was confirmed by FT-IR. WAC was tested by tea-bag method in distilled water and 3% NaCl solution. PAM is slightly more absorptive than K-CMC in distilled water, but in NaCl solution, K-CMC is more absorptive than PAM. Soil particle sizes above $1_{mm}$ were immediately increased from 9.6 to approximately 16.6% by the application of K-CMC and PAM, respectively. Infiltration rates of soil were approximately twice as great as those of the control when conditioned with the K-CMC and PAM treatment. K content of soil treated with K-CMC was significantly higher than those of PAM and control, but the other components of soil chemical properties were not different. The early growth and vegetative production of cabbage in the K-CMC and PAM treatments were significantly higher than the control. The contents of vitamin C were increased with the treatment of K-CMC. It was proposed that K-CMC treatment influence K component of the soil and vitamin C content of the cabbage, therefore, it improved the yields as well as crop quality.

• CELLMED
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• v.4 no.1
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• pp.7.1-7.8
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• 2014

Metabolic effects of ten daily doses of standardized extract of Andrographis paniculata leaves (AP) rich in andrographolide were evaluated in a rat model of type-2 diabetes and in diet induced obese rats. AP was administered per-orally as suspension in 0.3% carboxymethylcellulose at doses of 50, 100 and 200 mg/kg/day for 10 consecutive days. Blood glucose, insulin and lipid profile of rats were measured by using enzyme kits. In addition, effects of such treatments on anti-oxidant enzymes activity and histopathological changes in various organs of diabetic rats were assessed. AP treatments reversed body weight losses and increased plasma insulin level in diabetic rats. The anti-oxidant enzymes activity became normal and histopathological changes observed in pancreas, liver, kidney and spleen of diabetic animals were less severe in extract treated groups. On the other hand, hyperinsulinemia and increased body weight gains observed in high fat or fructose fed rats were less severe in the extract treated groups. These observations revealed therapeutic potentials of the extract for treatments of diabesity associated metabolic disorders, and suggest that the effects of the extract on insulin homeostasis depend on the metabolic status of animals. Activation of cytoprotective mechanisms could be involved in its mode of action.

• Korean Journal of Microbiology
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• v.31 no.2
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• pp.157-165
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• 1993

A 1, 4-.betha.-D-xylanase, designated as xylanase II, was purified from the culture filtrate of Trichoderma koningii ATCC 251131 by column chromatography on Sephadex G-75, SP-Sephadex C-50, DEAE-Sephadex A-50 and Sephadex G-50 with an overall yield of 6.97%. It has a molecular weight of 21.000 and an isoelectric point of 9.4. The enzyme activity is optimal at pH 5.0 and at a temperature of 50.deg.C. Xylanase II is stable up to 50.deg.C, while 40 and 90% of its activity are lost after the incubation for 30 and 60 min at 60.deg.C. The enzyme degrades xylan with relatively high activity, as well as carboxymethylcellulose and Avicel. Its $K_{m}$ values for oat-spelt xylan, larchwood xylan and Avicel are 7.48, 1.98 and 13.33 mg/ml, respectively. The hydrolysis products of oat-spelt xylan by xylanase II are xylose, xylobiose, xylotriose and arabinoxylotriose, while the reaction products of larchwood xylan are xylose, xylobiose, xylotriose and small amount of higher oligomers. The action paterns of the enzyme demonstrate that xylanase II is endo-enzyme.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1295-1302
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• 2004

A gene encoding the mannanase of Bacillus subtilis WL-7, which had been isolated from Korean soybean paste, was cloned into Escherichia coli, and the gene product was purified from the culture filtrate of the recombinant E. coli. This mannanase gene, designated manA, consisted of 1,086 nucleotides, encoding a polypeptide of 362 amino acid residues. The deduced amino acid sequence was highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum at 6.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum, konjak, guar gum, and lichenan, while it did not exhibit activity towards yeast mannan, laminarin, carboxymethylcellulose, $\beta$­glucan, xylan, and para-nitrophenyl-$\beta$-mannopyranoside.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1514-1519
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• 2009

A gene encoding the xylanase of Bacillus subtilis AMX-4 isolated from soil was cloned into Escherichia coli and the gene product was purified from the cell-free extract of the recombinant strain. The gene, designated xylA, consisted of 639 nucleotides encoding a polypeptide of 213 residues. The deduced amino acid sequence was highly homologous to those of xylanases belonging to glycosyl hydrolase family 11. The molecular mass of the purified xylanase was 23 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum of 6.0-7.0 and a temperature optimum of $50-55^{\circ}C$. Xylanase activity was significantly inhibited by 5 mM $Cu^{2+}$ and 5 mM $Mn^{2+}$, and noticeably enhanced by 5 mM $Fe^{2+}$. The enzyme was active on xylans including arabinoxylan, birchwood xylan, and oat spelt xylan, but it did not exhibit activity toward carboxymethylcellulose or p-nitrophenyl-$\beta$-xylopyranoside. The predominant products resulting from xylan and xylooligosaccharide hydrolysis were xylobiose and xylotriose. The enzyme could hydrolyze xylooligosaccharides larger than xylotriose.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2006.11a
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• pp.353-354
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• 2006

This work describes the effect of binders, such as carboxymethylcellulose (CMC), CMC+Polytetrafluoroethylene (PTFE) and PTFE, on the electrochemical and mechanical properties of activated carbon-electrode for electric double layer capacitor. The cell capacitors using the electrode bound with binary binder composed of CMC and PTFE, especially m composition CMC ; PTFE = 60 : 40 wt %, has exhibited the better rate capability and the lower internal resistance than those of the cell capacitor with CMC. On the other hand, the sheet type electrode kneaded with PTFE was bonded with conductive adhesive on Al foil. This cell capacitor using the electrode with PTFE exhibited the best mechanical properties and rate capability compared to the CMC and CMC+PTFE one These behaviors could be explained by the well-developed network structure of PTFE fibrils during the kneading process.