• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.484-489
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• 1990

An intracellular inulase ( fJ-fructofuranoside fructohydrolase, EC 3.2.1.26) from Bacillus subtilis has been partially purified and its mode of action and general properties were studied. The enzyme had an apparent molecular weight of 49,000 as estimated by gel filtration and its pI point was 5.2. Substrate concentration studies showed an apparent Km of 10 mM for sucrose and of 18 mM for raffinose. The enzyme was an acid-labile protein with a pH optimum of 6.6. The optimum temperature was 50$^{\circ}$C. The enzyme acts on straight chain oligo- and poly-fructosides of the inulin series via a exo-wise cleavage mechanism, as well as on sucrose.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.510.1-510
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• 1986

Many enzymes require the participation of readily dissociable coenzymes as NAD for thir catalytic activities. The continuous utilization of the enzymes requires the retention and regeneration of the coenzymes. For this purpose, several kinds of macromolecular NAD derivatives have been prepared by covalently attaching NAD to watersoluble polymers. We have prepared poly (ethylene glycol)-bound NAD (PEG-NAD) by coupling N$\^$6/-(2-carboxyethyl)-NAD to one terminal of ${\gamma}$ $\omega$-diaminoly (ethylene glycol) (Mr 3000) with water-soluble carbodiimide. PED-NAD thus obtained has one NAD moiety located at a terminal of the linear, flexible and hydrophilic chain of poly (ethylene glycol). PED-NAD has good coenzyme activity for various dehydrogenases and is applicable in a continuous enzyme reactor. To use these macromolecular NAD derivatives in an enzyme reactor, it si necessary to understand the behavior of the system in which the reactions of dehydrogenases are coupled by the recycling of the NAD derivative. We investigated the kinetic properties of a continuous enzyme reactor containing lactate dehydrogenase, alcohol dehydrogenase and PEG-NAD. The steady-state behavior of the enzyme reactor is explained by a simple kinetic model.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.41 no.5
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• pp.44-49
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• 2009

Old newspaper was deinked using commercial cellulolytic enzymes and a surfactant complex at low alkalinity. The properties of the deinked pulp(DIP) were evaluated and the suspended solids content, cationic demand, turbidity, and chemical oxygen demand(COD) of the process water were measured. The results can summarized as follows, 1. The brightness and yield of the DIP were improved using enzymatic surfactant complex deinking. 2. The amount of foaming during deinking with the enzyme surfactant complex was higher than that with synthetic surfactant deinking. However, it was not sufficient to cause process problem. 3. The pH and turbidity of the white water from deinking with the enzyme surfactant complex were similar to those of the white water from surfactant deinking. 4. The suspended solids content, cationic demand, and COD of the white water from deinking with the enzyme surfactant complex were improved compared to those of the white water from surfactant deinking.

• Textile Coloration and Finishing
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• v.23 no.1
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• pp.1-10
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• 2011

Research information related to application of enzyme as pretreatment and subsequent functional finishing on wool blended textiles for imparting multi-functional properties is still scanty. Yarn-blended wool/cotton fabric was pretreated with both a cellulase (Bactosol-CA) or a protease (Savinase-16.0LEx) in individual, subsequently finished with Synthappret-BAP and ${\beta}$-cyclodextrin based combination to impart anti-shrink, anti-microbial, softening and anti-crease properties. The performance of the finished fabrics depended on type of finishing combinations applied rather than enzyme pretreatment. Savinase pretreatment followed by Synthappret+Ceraperm-MW combination finishing impart both anti-shrink property as well as softening, while Bactosol pretreatment followed by ${\beta}$-cyclodextrin and sanitize combination finishing impart antimicrobial activity as well as anti-shrink finish to the wool/cotton blend fabric.

• The Korean Journal of Mycology
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• v.13 no.2
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• pp.111-114
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• 1985

The production of lac case by the funguson various media was studied. The characteristics of the enzyme were also studied regarding to the optimum pH, stability, Km value, and inactivation. The maximum activity of laccase reached the 40 days of incubation and the barley straw extract appeared to be a strong inducer for laccase. The enzyme showed stability at wide range of pH with optimum pH of 6.6. Temperature stability of the enzyme was high. Laccase was not inactivated by the organic solvents used for the precipitation. The enzyme, how­ever, was completely inactivated by trichloroacetic acid and sodium azide.

• Textile Coloration and Finishing
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• v.13 no.3
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• pp.155-164
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• 2001

Textile wet-processing industry usually five rise to environmental pollution problems caused by using chemical substance. The objective of this study is to apply enzymes for wool and reduce the environmental problems. Three commercial protein degradation enzymes and a cellulose degradation enzyme as a reference were treated to prevent the shrinkage of wool fabric on laundering. Shrink resistant effects used change with the kinds of enzyme, the amount of enzyme, assistant chemicals, and the pre-treatment condition of wool fabric. When pre-treated with corona before enzyme treatment under ultrasonic condition, the weight loss was increased and strength was decreased and elongation was increased. Both corona pre-treatment and the addition of $Na_2SO_4$ also decreased shrinkage of wool fabrics on laundering. The existence of assistant chemicals increased alkali solubility of wool fabrics.

• Journal of Microbiology
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• v.34 no.3
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• pp.270-273
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• 1996

Micrococcus luteus purine nucleoside phosphorylase (PNP) has been purified and characterized. The physical and kinetic properties have been described previously. Chemical modification of the enzyme was attempted to gain insight on the active site. The enzyme was inactivated in a time-dependent manner by the arginine- specific modifying reagent phenylglyoxal. There was a linear relationship between the observed rate of inactivation and the phenylglyoxal concentration. At 30 $^{\circ}C$ the bimolecular rate constant for the modification was 0.015 $min^{-1}mM^{-1}$ in 50 mM $NaHCO_3$ buffer, pH 7.5. The plot of logk versus log phenylglyoxal concentration was a strainght line with a slope value of 0.9, indicating that modification of one arginine residue was needed to inactivate the enzyme. Preincubation with saturated solutions of substrates protected the enzyme from inhibition of phenylglyoxal, indicating that reactions with phenylglyoxal were directed at arginyl residues essential for the catalytic functioning of the enzyme.

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.312-318
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• 1987

The apparent Michaelis constant Km of extracellular adenine deaminase from Streptomyces sp. J-350P was 5.8$\times$10$^{-5}$M. The activation energy or the enzyme was calculated from Arrhenius plots for adenine and the value was 3.13 Kcal/mole. The purine analogues, 6-chloropurine, 2,6-diaminopurine, 6-bromopurine, 4-aminopyrazolo[3,4-d] pyrimidine, 6-iodopurine, and 8-bromoadenine were substrates for the enzyme. 6-Dimethylaminopurine was a competitive inhibitor of the enzyme. The enzyme was inhibited by 0.1mM of Fe$^{3+}$, Ag+, and Hg$^{2+}$ and 1 mM of $\alpha$, $\alpha$＇-dipyridyl, Penta-chiorophenol, and p-chloromercuribenzoate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.638-639
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• 2000

Quinone reductase was purified to electrophoretic homogeneity from bovine liver by using ammonium sulfate fractionation, ion-exchange chromatography, and gel filtration chromatography. The enzyme utilized either NADH or NADPH as the electron donor. The optimum pH of the enzyme was pH 8.5, and the activity of the enzyme was greatly inhibited by $Cu^{2+}$ and $Hg^{2+}$ ions, dicumarol and cibacron blue 3GA. The enzyme catalyzed the reduction of several quinones and other artificial electron acceptors. Furthermore, the enzyme catalyzed NAD(P)H-dependent reduction of azobenzene or 4-nitroso-N,N-dimethylaniline. The apparent $K_m$ for 1,4-benzoquinone, azobenzene, and 4-nitroso-N,N-dimethylaniline was 1.64mM, 0.524mM and 0.225mM, respectively. The reduction of azobenzene or 4-nitroso-N,N-dimethylaniline by quinone reductase was strongly inhibited by dicumarol or cibacron blue 3GA, potent inhibitors of quinone reductase.