• Microbiology and Biotechnology Letters
• /
• v.25 no.5
• /
• pp.468-476
• /
• 1997

Soft-rot bacterial pathogen, Erwinia sp., was isolated from chinese cabbage tissue showing soft-rot symptom. This bacterial strain caused soft-rot to chinese cabbage and potato, and it was identified as Erwinia carotovora subsp. carotovora LY34 (E. c. subsp. carotovora LY34). Erwinia carotovora subsp. carotovora LY34 did not have hemicellulase but extracellular cellulase, pectinase, polygalacturonase, protease activity. The results of the microscopy showed that chinese cabbage tissue and potato tissue were macerated by infection of E. c. subsp. carotovora LY34. In analysis of the cellulases activity of the isolated cellulose-degradation enzymes from E. c. subsp. carotovora LY34 total protein, three cellulase activity bands were detected by non-denaturation gel electrophoresis method and five cellulase activity bands were detected by CMC-SDS-PAGE direct stain method.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.23 no.1
• /
• pp.14-21
• /
• 1999

The Tencel fabrics were treated with bio-softness finish to improve softness. The change of the properties depending on the softner as well as cellulase treatment was investigated. The relative activity of cellulase for tencel was maximum ap pH 4-4.3 cellulase concentration 14-16% (o. w .f) treatment time 4 hour and liquor ratio 100: 1 The treatment of epoxy silicon softner improved in pilling whiteness dye absorption of Tencel fabric.

• 한국생물공학회:학술대회논문집
• /
• 2000.04a
• /
• pp.347-350
• /
• 2000

Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase from Trichoderma reesei Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deinking, maximum brightness and freeness were obtained at 2 unit/g ODP. Deinking by papain-hydrolyzed cellulase showed similar results with one by Novozym 342. It was better in brightness and freeness, but showed lower physical strength and yield, than the conventional deinking by sodium hydroxide. The ratio of endo-1,4-glucanase and exo-1,4-glucanase components in papain hydrolyzed cellulase from T. reesei Rut C-30 was similar to that of commercial enzyme, Novozym 342, implicating a successful application as a deinking enzyme.

• Textile Coloration and Finishing
• /
• v.8 no.3
• /
• pp.59-65
• /
• 1996

Cotton fabrics were treated by low temperature plasma and/or cellulase, and its physical and dyeing properties were investigated. All the pretreatments of the cotton with low temperature plasma of oxygen, nitrogen and argon slowed down the rate of weight loss of cotton in cellulase solution. Plasma pretreatment did not show any strength retention effect on cotton fiber in the subsequent cellulase treatment. Pretreatment of cotton with low temperature oxygen plasma decreased the rate of dyeing in direct dye bath, while cellulase or plasma/cellulase pretreatment increased the rate. Equilibrium dye uptake of cotton was not changed greatly by the pretreatments except the normal untreated cotton showed more or less high uptake. The pretreatment of cellulase with a water-soluble carbodiimide reduced the enzymatic activity, and did not show any strength retention of cotton in enzymatic weight loss.

• The Korean Journal of Food And Nutrition
• /
• v.3 no.1
• /
• pp.57-68
• /
• 1990

In order to obtain the fundamental informations on cellulase of Trichoderma viride QM 9414 for its production and utilization, some physico-chemical properties of the enzyme were reviewed. When T. viride QM 9414 was cultured on wheat bran medium, filter paper-disintegrating and carboxymethyl cellulose-saccharifying activity were increased with the cell growth, and thereafter CMC-saccharifying activity was kept on almost the same leved while filter-paper disintegrating activity was decreased sharply. And B-glucosidase was formed maximally on the late stationary phase of growth. The crude cellulase of cell-free extracts was purified by (NH4)2SO4 fractionation, Sephadex-G 200 column chromatography and DEAE Sephadex A-50 column chromatography. Filter paper-disintegrating, CMC-saccharifying and B-glucosidase activity were purified 10-fold, 47-fold and 38-fold, respectively. The crude enzyme was proved to be a complex of three different enzyme proteins which were showing filter paper-disintegrating, CMC-saccharifying and B-glucosidase activity. The optimal pH of the three enzyme components was alike pH 4.0, and the optimal temperature for CMC-saccharifying, filter paper-disintegrating and B-glucosidase activity were 4$0^{\circ}C$, 45$^{\circ}C$ and 5$0^{\circ}C$ respectively. The Km and Vmax values of CMC saccharifying activity for CMC were 0.485% and 3.10, and the Km and Vmax vallues of B-glucosidase for PNPG were 0.944$\times$10-3M and 0.097, respectively. The Km and Vmax values of filter paper-disintegrating activity for Avicel were determined to be 0.09% and 0.178, respectively. B-Glucosidase activity was competitively inhibited by glucose, and the Ki value for this enzyme was 3.54$\times$10-3M, CMC saccharifying activity was found to be greatly inhibited by cellobiose.

• Journal of Life Science
• /
• v.18 no.3
• /
• pp.323-328
• /
• 2008

In this study we evaluated the method to develop red ginseng oil containing high content of phytochemicals by enzymes treatment. To select the optimum extraction process of red ginseng with oils, the antioxidant activities of red ginseng using various enzymes were measured. Red ginseng after 0.5% cellulase treatment for 1 hr at $50^{\circ}C$ had higher antioxidant activity than the other conditions. We found that red ginseng/soybean oil extracted for 15 days at $40^{\circ}C$ after 0.5% cellulase treatment increased DPPH radical scavenger activity and decreased the TBA and POV values. However, red ginseng/olive oil had little functional activities compare to the red ginseng/soybean 0il. We also analyzed vitamin A and E by HPLC and found that vitamin E was increased by 0.5% cellulase treatment in the oil. This is the first report that red ginseng oil extracted by enzyme treatment has various beneficial effects.

• Journal of the Korean Wood Science and Technology
• /
• v.17 no.3
• /
• pp.52-60
• /
• 1989

This study was carried out to know the possibility of simultaneous utilization of laccase from white-rot fungus with cellulase on enzymatic hydrolysis of cellulosic substrate from autohydrolyzed oak wood. Laccases from 3 white-rot fungi, Pleurotus ostreatus. Ganoderma lucidum, and Phanerochaete chrysosporium, were isolated, purified and measured their activities. The highest activity was shown in Pleurotus ostreatus and the lowest in Phanerochaete chrysosporium. Laccase from Pleurotus ostreatus has optimum pH of 5.94, Km value of 3.209 mM and appeared to be stable at relatively wide pH range, 4.7-8.72. Temperature stability showed that 60% activity was preserved after 40 minutes at $50^{\circ}C$. Laccase from Ganoderma lucidum reached to the maximum activity during 15-20 day incubation. This enzyme has optimum pH of 6.45, Km value of 6.71 mM and pH range of 5.0-9.0 for stabilization. 95% activity was preserved at $30^{\circ}C$ and 58% activity at $50^{\circ}C$. Concerned to the enzymatic hydrolysis of cellulosic substrate with both enzymes, cellulase and laccase, simultaneously, mixed culture filtrates and mycellium extracts were shown higher hydrolysis rates than those of Trichoderma viride. There were no significant differences in the extent of hydrolysis among various mixed culture filtrates and mycellium extracts.

• Journal of Animal Science and Technology
• /
• v.52 no.1
• /
• pp.65-70
• /
• 2010

A bacterium producing acidic cellulase was isolated from pig feces. The isolate, ATC6 strain, was found to be Gram-positive, non-motile, catalase-positive, and spore-forming stain. Under an electron microscope, the cells were observed to be rod-shaped. The isolate was identified as Bacillus amyloliquefaciens ATC6 on the basis of morphological and biochemical properties as well as 16S rRNA gene sequences. Optimum pH and temperature for the cellulase activity of the culture supernatant of B. amyloliquefaciens ATC6 were found to be pH 4.5 and $55^{\circ}C$, respectively. More than 80% of its maximum activity was maintained at pH 4.0. The cellulase activity was maintained at temperatures ranging from 35 to $55^{\circ}C$ after 2 h incubation at pH 4.5, whereas it's activity decreased rapidly at $65^{\circ}C$.

• Journal of the Korean Society of Tobacco Science
• /
• v.7 no.1
• /
• pp.75-84
• /
• 1985

A strain of Trichoderm sp. J-30 which strongly products cellulase to reduce the content of cellulose in the stem of leaf tobacco was isolated from leaf tobaco. The Trichoderma sp. J-30 was identified as Trochoderma voride. The cellulase from this strain was purified with the physico-chemical methods and treated in the culled stem of leaf tobacco. The results obtained were summarized as follows. 1. Optimal pH of the enzyme was at pH 5.0. 2. The enzyme shooed a higher activity at $40^{\circ}C$ and its thermal stability began to decrease at $60^{\circ}C$. 3. The enzyme activity was promoted by the metal ions such as $Ca^{2+}, Mg^{2+}, Pb^{2+}and\;Zn^{2+}.$ 4. When the culled stem of leaf tobacco was applied with the 3% of the enzyme solution at $40^{\circ}C$ for 3 days. 15 to 17% of cellulose contents decreased, 12 to 13% of total sugar increased and the filling power was increased by 10-13% in the sample.

• Korean Journal of Microbiology
• /
• v.35 no.4
• /
• pp.277-282
• /
• 1999

A bacterium producing the extracellular cellulase was isolated from cattle feces and screened as cellulase activity was excellent upon congo red straining method and activity measurements. Isolate was identified as Bacillus subtilis CH-10 on the basis of morphological and biochemical properties as well as cellular fatty acids composition. The enzyme which the isolate secretes had the optimum initial pH and temperature for its induction was 7.5 and 50${\circ}C$, respectively. The maximum CMCase activity in crude enzyme solution was observed at pH 7.5 and 75${\circ}C$ and was stable for pH 7.5 to 9.0 to maintain 70% activity. When the isolate was cultured in CMC media at 37${\circ}C$ for 24 hrs, CMCase and FPase activity was 1.13 U/㎖and 0.16U/㎖, respectively whereas Avicelase and ${\beta}$-glucosidase activity was not detected. When crude supernatant was used for zymogram, three major bands, cel 1, cel 2 and cel 3, were detected approximately 39, 41 and 57 KDa, respectively on CMC-SDS-PAGE.