• Korean Journal of Food Science and Technology
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• v.26 no.5
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• pp.484-489
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• 1994

Solubilization of plant ceil wall(tofu-residue) using enzyme complex obtained by Aspergillus niger CF-34 was attempted. The hydrolysis reaction was done at pH 4.0, $50^{\circ}C$, which were optimum pH and temperature of the enzyme, respectively. At the enzyme dosage of 2.5% (in terms of solid content of tofu-residue) and reaction time of 3 hr, the solubilizing percent of protein and carbohydrate were 62% and 50% respectively. Homogenization prior to enzyme reaction did not have much effect on tofu-residue solubilization. To improve solubility of tofu-residue, additional treatment such as alkali with 0.1% NaOH solution was found to be useful. The results showed that tofu-residue, which mainly consists of cell wall component of cellulose and hemicellulose, was not accessible to enzyme reaction and some prior treatment is required to enhance enzyme hydrolysis.

• The Journal of Natural Sciences
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• v.14 no.2
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• pp.67-82
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• 2004

A thiol-specific antioxidant protein (TSA or TPx) was purified from Halophilic archeabacteria Halococcus agglomeratus, by DEAE-Cellulose, Phnyl, sepharose, Sephadex G-75, Sephacryl S-100, Sephacryl S-200, and Q-Wepharose FF. This protein exhibited the preventeive effect against the inactivation of glutamine synthehase (GS) activity was support by a thiol-reducing equicalent such as dithiothreitol. TPx activity was maximal at NaCl concentration above 500mM. The molecular mass of the protein was determinated to be 22-kDa by SDS-PAGE. The TPx purified from Halococcus agglomeratus seems to be similar to other TPx family, except for the salt requirement for the maximal antioxidant activity.

• Journal of Life Science
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• v.21 no.12
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• pp.1716-1720
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• 2011

A bacterium hydrolysing various organic materials including cellulose, protein, starch and lipid was isolated. The isolate was identified as Bacillus subtilis, and named Bacillus subtilis CK-2 in this paper. This bacterium showed optimal growth at $40\sim45^{\circ}C$, pH 6~9, and 0~3% of NaCl. B. subtilis CK-2 seemed to synthesis highly active autolysin. The hydrolytic enzymes produced by B. subtilis CK-2 were primary enzymes because extracellular enzyme activities varied similarly to the growth curve. The hydrolytic enzymes seemed to be stable at basic pH conditions. From these results, B. subtilis CK-2 was found to bea useful bacterial agent for composting, or for use in feed-production waste in agriculture, fishery, forest materials, livestock farming, and food.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.45 no.6
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• pp.30-35
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• 2013

To conserve wood resources for papermaking, chemical compositions of the hemp (Cannabis sativa L.) bast fiber cultivated in Korea such as holocellulose, ${\alpha}$-cellulose, lignin, alcohol-benzene extractives, hot and cold water extractives, and ash contents were investigated to manufacture the specialty packaging paper effectively. Significantly very low klason lignin content of 3.3% was accomplished by removing of the outer shell of bark. Laboratory soda pulping method which is very useful for the nonwood fiber was adapted, and it was found that there was no significant difference in both kappa number and H-factor between 25% and 30% NaOH charge. Hemp pulp cooked with the laboratory digester in 25% NaOH at $170^{\circ}C$ were mixed together with the wood pulp(NBKP:LBKP=1:1) in order to find the optimum mixture ratio which exhibited acceptable paper strength properties such as tensile index, burst index, and tear strength. When 10% of hemp soda pulps was mixed with 90% of wood pulps comprised of SwBKP and HwBKP (1:1), all physical strength increased significantly. The physical strength decreased as the amount of hemp pulp increased because the cell wall of bast fiber is very thick which causes low conformability and low fiber-fiber bonding. These results showed that paper made of hemp-wood pulp can be used for the specialty packaging paper which requires both the characteristic surface properties and the high physical strength of hemp fiber.

• Journal of Life Science
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• v.25 no.6
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• pp.680-685
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• 2015

Previously, cellulase and xylanase producing microorganism, Bacillus subtilis NC1, was isolated from soil. Based on the 16S rRNA gene sequence and API 50 CHL test the strain was identified as Bacillus subtilis, and named as B. subtilis NC1. We cloned and sequenced the genes for cellulase and xylanase. Plus, the deduced amino acid sequences from the genes of cellulase and xylanase were determined and were also identified as glycosyl hydrolases family (GH) 5 and 30, respectively. In this study to optimize the medium parameters for cellulase production by B. subtilis NC1 the RSM (response surface methodology) based on CCD (central composite design) model was performed. Three factors, tryptone, yeast extract, and NaCl, for N or C source were investigated. The cellulase activity was measured with a carboxylmethyl cellulose (CMC) plate and the 3,5-dinitrosalicylic acid (DNS) methods. The coefficient of determination (R²) for the model was 0.960, and the probability value (p=0.0001) of the regression model was highly significant. Based on the RSM, the optimum conditions for cellulase production by B. subtilis NC1 were predicted to be tryptone of 2.5%, yeast extract of 0.5%, and NaCl of 1.0%. Through the model verification, cellulase activity of Bacillus subtilis NC1 increased from 0.5 to 0.62 U/ml (24%) compared to the original medium.

• Journal of Nutrition and Health
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• v.19 no.6
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• pp.363-373
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• 1986

This study was devised to elucidate whether soused shrimp exhibits a digestive action on boiled pork meats. and the mechanism by which sousing with a high concentration of sodium chloride preserves nutrients in foods for a prolonged pe\ulcornerriod. Protease was isolated from soused shrimp using a combination of ammonium sulfate fractionation. DEAE - cellulose ion exchange chromatography and gel filtra\ulcornertion. The isolated protease had specific activity of 1.560 units. 210 purification fo\ulcornerld with an yield of 38%. Its optimum pH and temperature were 8.0 and $43^{\circ}C$ respectively. The molecular weight of the enzyme was 35.000. The Km value of the enzyme for casein was 1.6 x $10^{-6}$ M The e=yme required the presence of cu\ulcornerpric ion to exhibit its full activity. Eighty eight percent of the enzyme activity was in\ulcornerhibited by 3.5M NaCI showing a reversibly linear decrease of the enzyme activity as NaCI concentration increased. The nature of the inhibition by NaCl was rever\ulcornersible and noncompetitive. The protease activity in soused shrimp was well preser\ulcornerved with the elapse of time at least in part due to NaCI induced suppression of autodigestion. The enzyme was denatured by acid easily. i.e. 1% of the original activity remained after staying at pH 2 for 10 minutes. which is within the norm\ulcorneral range of pH of the human stomach. Soused shrimp was observed to be one of those containing the highest protease activity compared with the other soused foo\ulcornerds such as soused oyster. squid. clam. and Pollack intestine with respect to spec\ulcornerific activities of dialized 1:4 whole homogenates(w/v) in 5 mM sodium phospha\ulcornerte - 2.4 mM j3 - mercaptoethanol buffer. pH 8.0. Casein and boiled meats including pork, beef, and chicken appeared to be the good substrates for the protease. Casein was the best. Therefore. the ingestion of boiled meats including pork together with soused sh\ulcornerrimp would help digestion of boiled pork in human not only by increasing appe\ulcornertite also by the direct proteolytic digestion of boiled meats by soused shrimp to\ulcorner some extent. And a high concentration of sodium chloride inhibited the protease activity reversibly in a remarkable degree, which ensued in a significant retardat\ulcornerion of autodigestion of protein in foods by proteases, and hereby contributed to the preservation of foods for an extended period.

• Journal of Life Science
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• v.10 no.1
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• pp.1-5
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• 2000

Pectinase was isolated from culture medium of Bacillus sp. BS-214 and purified 105-fold with 3.4% yield by ammonium sulfate precipitation, gel filteration using Sephadex G-75 and DEAE-cellulose followed by gel filteration through Sephadex G-100. The molecular weight of the purified enzyme was estimated to be about 43 kDa on SDS-PAGE and by gel filtration, indicating that the enzyme is a monomer. the optium pH and temperature of the enzyme were 9.0 and 55$^{\circ}C$, respectively. the enzyme was stable at 60$^{\circ}C$ for 30min and in a pH range from 7.5 to 10.5 for 12 h ant 4$^{\circ}C$. The enzyme activity was highly enhanced by Ca2+, and also K+, Li+ and Na+showed a positive effect, while stongly inhibited by Zn2+ and Hg2+.

• Textile Coloration and Finishing
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• v.23 no.3
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• pp.201-209
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• 2011

With a new method of applying chitosan and alginate onto cellulose, multi-coated cotton fabrics with chitosan and alginate were prepared and characterized. To coat cotton with chitosan, raw cotton was dipped in chitosan solution, mangled of 1kgf/$cm^2$, neutralized in 2 wt% NaOH soluton, washed, and dried at $60^{\circ}C$ oven. The chitosan-coated fiber was dipped in sodium alginate solution, 1kgf/$cm^2$ mangled, neutralized in 2 wt% $CaCl_2$ solution, washed, and dried at $60^{\circ}C$ oven, resulting in CCAC(coated cotton with chitosan and calcium alginate skin) fiber characteristics. Excellent absorbancy of distilled water and saline solution was observed by the absorption test on cotton fabric treated with CCAC(0.5 wt% calcium alginate) and 0.5 wt% calcium alginate respectively. The SEM photograph confirmed the uniform coating on the cotton fabric surface.

• Food Science of Animal Resources
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• v.18 no.1
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• pp.35-41
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• 1998

The objective of this study was to examine the changes of physical properties by additions of different kinds of stabilizers milk proteins concentration, when stored at 4$^{\circ}C$ or 20$^{\circ}C$ for yoghurt. the results were summarized as follows: 1. Addition of 2% carboxyl methyl cellulose and carrageenan, gelation 0.4%, pectin and starch 0.6%, and carrageenan & pectin 0.8% in the manufacture of yoghurt increased the viscosity, water-holding capacity and protein hydration of yoghurt. 2. Addition of 3% skim milk powder, Ca-caseinate or Na-caseinate 0.6% increased the viscosity, water-holding capacity and protein hydration of yoghurt. 3. Twenty five percent of evaporation of milk promoted to build up the optimal structure of the micelles of yoghurt and improved viscosity, water-holding capacity and protein hydration of yoghurt. 4. Addition of stabilizers to yoghurt showed an increase of viscosity, water-holding capacity and protein hydration when compared with non-addition of stabilizers to yoghurt at 4$^{\circ}C$, 20$^{\circ}C$ storage for 12hrs, 96hrs followed by the decrease of it.

• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.432-438
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• 1995

The intracellular alginase from Vibrio sp. AL-145 was purified by ion chromatography on DEAE-Cellulose column, Q-Sepharose column, and gel filtration on Sephadex G-100 column. The optimum pH and temperature for the activity of the purified intracellular enzyme were 8.0 and 37$\circ$C, respectively. The enzyme was stable at the pH range of 7.5-8.5, and at 30$\circ$C for 30 min. The molecular weight of the intracellular enzyme was estimated to be about 23, 000 daltons by SDS-polyacrylamide gel electrophoresis. NaCl was required for enzyme activity and the optimum concentration was 0.5 M. The activity of intracellular enzyme was inhibited by Co$^{2+}$, Hg$^{2+}$, Zn$^{2+}$, 0-phenanthroline, $\rho$-CMB, EDTA and iodoacetate, and stimulated by Ca$^{2+}$, L-cysteine and 2-mercaptoethanol. This enzyme was an alginase specifically degrading alginic acid.