• Fashion & Textile Research Journal
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• v.8 no.2
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• pp.239-244
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• 2006

For studies of fibrinolytic enzyme strain K-54 was isolated from the Korean traditional food chungkook-jang. Isolated strains K-54 was identified as Bacillus subtilis. The molecular weight of fibrinolytic enzyme from B. subtilis K-54 was 27 kDa. Optimum temperature for fibrinolytic enzyme of B. subtilis K-54 was $50-70^{\circ}C$ and optimum pH for producing the enzyme of this strain was ranging from 8 to 12. Also, it was found out enzyme activity was completely inhibited by 1mM PMSF. The result indicated this enzyme was thermo-stable alkaline serine protease with strong fibrinolytic activity. The wool and silk were treated with protease of B. subtilis K-54. As a result, the property of dyeing of wool fabrics was increased. By the increasing of treatment time became smoothened. But the change of mechanical properties were not changed.

• The Research Journal of the Costume Culture
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• v.12 no.5
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• pp.737-742
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• 2004

The purpose of this study is restoration for tearing strength of the durable press (DP) finished 100% cotton fabric by enzymatic treatment. Dimethylol Dihydroxy Ethylene Urea (DMDHEU) was used as a DP finish chemical. Enzymes (cellulase, pectinase, protease, lipolase) were selected based on their specific reaction activities. Ideal application of the enzymes for this work was to remove cross-links created by DMDHEU on the surface of the fibers to offer migration property between microstructures of cellulose, yet cross-links that exist inside of the fibers are still remained to impart effect of wrinkle resistance. Physical characteristics (tearing strength, wrinkle recovery, FT-IR) of enzyme treated samples were measured and compared. It was found out that, in case of enzyme treatment, most of enzymes didn't have a great effect on tearing strength, but, in case of Protease, tearing strength increased at DMDHEU 2% treatment. As a result of an experiment on wrinkle recovery of the textiles treated with enzyme making density of DMDHEU different whenever respective experiment was made, it was discovered that density of DMDHEU increased as wrinkle recovery increased and, in the relation to enzyme treatment especially in Lipase enzyme treatment, the lesser density of DMDHEU, the more wrinkle recovery increased.

• Mycobiology
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• v.36 no.1
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• pp.74-76
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• 2008

To obtain basic information on the biochemical property of basidiospores of shiitake mushroom (Lentinula edodes), the ability of producing extracellular enzyme was assessed using a chromogenic plate-based assay. For the aim, amylase, avicelase, $\beta$-glucosidase, CM-cellulase, pectinase, proteinase, and xylanase were tested against monokaryotic strains generated from forty basidiospores of two different parental dikaryotic strains of shiitake mushroom, Sanjo-101Ho and Sanjo-108Ho. These two parental strains showed different degree of extracellular enzyme activity. No identical patterns of the degree of enzyme activity were observed between monokaryotic strains and parental strains of the two shiitake cultivars. The degree of extracellular enzyme activity also varied among monokaryotic strains of the two shiitake cultivars. Our results showed that dikaryotic parental strains of shiitake mushroom produce monokaryotic basidiospores having very diverse biochemical properties.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.3
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• pp.406-413
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• 2010

To enhance the yield and bioactivity of hot-water extract from herbal medicine, Astragalus membranaceus was hydrolyzed with carbohydrases, such as ClariSEB and Fungamyl. After hot-water extracts were prepared from each hydrolysate (HW-C/F), physicochemical property, antioxidant activity and sensory property were evaluated. The solid content ($^{\circ}Brix$) of HW-C/F was higher than hot-water extract from A. membranaceus no treated enzyme (control). Although pH of HW-C/F was lower than that of the control, the acidity was higher. Lightness of Hunter's color values was increased in HW-C/F whereas redness and yellowness were decreased. The contents of reducing sugar, flavonoid and polyphenol of HW-C/F were higher than the control but the content of ascorbic acid was not different from control. The inhibitory activity of HW-C/F against lipid peroxidation was slightly higher than control, but DPPH radical scavenging, ABTS reducing, metal chelating activities were significantly increased by HW-C/F. The sensory evaluation also revealed that the sensory panelists preferred HW-C/F to that of control. Therefore, hydrolysis by carbohydrases for preparation of hot-water extract from A. membranaceus is one of the good methods to improve antioxidative activity and sensory property of hot-water extract.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.37 no.3
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• pp.17-22
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• 2005

The cleaning efficiency of papermaking felt which is contaminated with fiber fines and various micro-materials was investigated and compared between the application of enzyme and commercial detergent. It was found that the cleaning efficiency by the treatment of acidic-based detergent was more efficient than that of alkaline-based one in the conventional commercial detergent. it was also observed that the treatment design of first acidic-based detergent treatment to second alkaline-based detergent procedure was better in the cleaning efficiency, compared to alkaline based-to-acidic based one. The cleaning property of felt with enzyme was resulted in good cleaning efficiency, without any addition of surfactant. Especially, the enzyme treatment under alkaline condition (pH 10) showed a better cleaning result than that under acidic condition(pH 5). The addition of nonionic surfactant to the enzyme increased the cleaning efficiency of felt and decreased the cationic demand of wastewater. These results showed more favour than the application of conventional commercial detergent.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.6
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• pp.1143-1147
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• 1998

Enzymatic characterization of peroxidase(E.C. 1.11.1.7) from soybean sprouts was investigated. The optimum pH of the purified peroxidase was 7.0 and relatively stable at pH 6.0~7.0. And the optimum temperature was 50oC. The enzyme was most active with guaiacol as a substrate, followed by (＋)catechin, pyrogallol and p phenylenediamine. The Km values for guaiacol and H2O2 were 4.2mM and 2.5mM, respectively. L Ascorbic acid and 2 mercaptoethanol greatly inhibited the enzyme activity, while Cu2+, Co2+ and Ni2+ activated the enzyme.

• Microbiology and Biotechnology Letters
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• v.28 no.1
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• pp.59-61
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• 2000

The various extracellular enzymes produced by lactic acid bacteria isolated from kimchi were assayed to improve the shelf-life of kimchi. Peroxidase was not detected in all tested lactic acid bacteria and small amount of ascorbic acid oxidase was detected in Pediococcus pentosaceus and Lactobacillus brevis. In case of $\alpha$-amylase, 27.8 and 20.9 unit/mg were shown in Pediococcus acidilactici and Pediococcus pentosaceus, respectively but $\beta$-amylase and protease activities were very low. The enzyme related to textural property of kimchi, pectinesterase showed low activity but polygalacturonase activity was 0.28 unit/mg in Lactobacillus homohiochii and 0.27 unit/mg in Lactobacillus plantarum.

• Journal of Life Science
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• v.12 no.6
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• pp.682-687
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• 2002

We analyzed improvement on the enzyme activity of CPase Taq by addition of various metal ions. The enzyme activity was increased more then four times by 1 mM cobalt ion and almost three times by 1 mM calcium ion. However, the active center metal zinc ion did not affect the enzyme activity. In order to investigate whether the active center metal affects the enzyme activity, zinc ion which is occupied the active center of the enzyme was replaced by cobalt ion which activates the enzyme activity very effectively. Since the cobalt ion in the active center of the cobalt-substituted CPase Taq did not affect the enzyme activity, it could act as the natal metal ion in the active center of the enzyme.

• Journal of the Korea Fashion and Costume Design Association
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• v.10 no.3
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• pp.173-180
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• 2008

Cotton, wool, cotton/wool blended (80:20) and tencel fabrics were treated with low temperature oxygen plasma, enzymes (cellulase or protease), or oxygen plasma-enzyme and they were examined for dyeing and handling properties for environment friendly finishing. The appropriate conditions for cellulase treatment were enzyme concentration of 3g/l, pH of 5, and $60^{\circ}C$ for one hour, and for protease treatment were enzyme concentration of 4g/l, pH of 8, and $60^{\circ}C$ for one hour. The equilibrium uptake of a direct dye on cotton changed with plasma treatment and plasma-cellulase treatment, and the rate of dyeing slightly decreased. When wool was dyed with acid dye, the equilibrium dye uptake did not change with plasma, protease treatment nor plasma-protease treatment, however, the rate of dyeing had increased with plasma-protease treatment. From these results, it is assumed that plasma attacks the surface of the fiber, and enzyme mainly affects the inner part of the fiber. Plasma treatment did not affect mechanical properties related to the handling of fabrics. The handling test showed increased extension at maxmum load(EM), tensile energy(WT) with decreased tensile resilience (RT), and the fabrics became softer but resilience decreased slightly with enzyme treatment. The bending recidity(B), hysteresis of bending moment(2HB), and hysteresis of shear force at five degrees(2HG5) decreased, however, shear stiffness(G) increased. I knew the plasma pre-treatment made fabrics softer with lower koshi(stiffness). The handling of plasma pre-treated fabrics was better than that of enzyme-treated fabrics. When we pre-treated fabrics, the handling test showed decreased coefficient of friction(MIU), geometrical roughness(SMD), while the surface of fabrics became smoother and numeri increased. Even though compression resilience(RC) increased, fukurami(bulky property) and compressive elasticity, decreased due to the linearity of compression-thickness curve(LC) and compression energy(WC).

• Journal of the Korean Chemical Society
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• v.24 no.1
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• pp.25-33
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• 1980

Pyrocatechase as a phenolytic dioxygenase was extracted from the benzoate-induced cells of a soil bacterium, a member of Pseudomonadaceae, and purified partially by DEAE-cellulose ion-exchange chromatography and Sephadex G-75 gel filtration. Final preparation of the enzyme yielding 200 fold purification over the crude extracts showed a specific activity of about 40 ${\mu}moles$ per minute per mg protein based on catechol as the substrate. The enzyme showed a very limited substrate specificity towards catechol for its catalytic activity. Based on the inhibition study with the substrate analogues, it was assumed that ortho dihydroxy groups on the aromatic ring may participate in the enzyme-substrate binding. The $K_m$ value for catechol was obtained as $1.9{\times}10^{-6}M$, and the optimum activity of the enzyme was obtained at the pH range of 7∼10 and $35^{\circ}C$. With SH-group blocking agents the enzyme was inhibited seriously. The activity of enzyme was also inhibited by the addition of some heavy metals, $Ag^+$ and $Cu^{2+}$, but was not affected by EDTA. General property of the enzyme was characterized and the possible nature of the enzyme active center was also discussed.