• Microbiology and Biotechnology Letters
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• v.11 no.1
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• pp.23-32
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• 1983

In the present study, two kinds of D-xylanases (1, 4-$\beta$-D-xylan xylanohydrolase (EC 3.2.1.8) were purified and characterized from crude extract of Aspergillus niger KG79. Xylanase I was most active at pH 5.0, whereas xylanse II at pH 4.0 Both enzymes demonstrated their maximum activity at 45$^{\circ}C$. They were relatively stable between pH 4.0 and 6.0 at 3$0^{\circ}C$ for 6 hours. Molecular weight of xylanse I and II were 12, 500 and 11, 500, respectively. Michaelis-Menten constants of xylanse I and II were 0.28% and 0.26% of xylan, respectively. Both enzymes could degrade commercial D-xylan to xylose, xylobiose, and xylotriose to the degree of about 10% of total reducing power. Xylanse I could, however, liberate arabinose from barley straw xylan in addition to xylose and xylooligasaccharides more rapidly than xylanase II. The degree of hydrolysis was about 25%. The reconstituted D-xylanase system with purified xylanases and $\beta$-xylosidase degraded commercial xylan and barley straw xylan to the degree of 28% and 54% respectively. The limit of hydrolysis by the enzymes was suggested to be resulted from the physical structure of the substrate.

• The Korean Journal of Mycology
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• v.17 no.2
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• pp.57-65
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• 1989

The effect of various cellulosic and hemicellulosic substrates on the induction of cellulase and xylanase complexes in Aapergillus nidulans was investigated. The most efficient substrates for the induction of cellulase and xylanase complexes were carboxymethylcellulose for endoglucanase, cellobiose for ${\beta}-glucosidase$, and xylan for endoxylanase and ${\beta}-xylosidase$, respectively. However, the mixtures of these substrates, especially CMC-xylan and CMC-xylan-laminarin mixture, were much more effective not only for the enhancement of the biosynthesis of all the cellulase and xylanase complexes but also for the balanced production of these enzyme components than individual substrate. The polyacrylamide gel electrophoresis followed by activity staining showed the variation in the patterns and relative intensity of ${\beta}-glucosidase$, endoglucanase and endoxylanase components in individual enzyme preparations from A. nidulans cultures grown on different substrates. These results suggest that the biosynthesis is of cellulase and xylanase systems in A. nidulans is regulated in coordination at the level of induction.

• Membrane Journal
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• v.12 no.1
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• pp.21-27
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• 2002

The formation of soluble microbial products(SMP) and molecular weight distribution on loading rate were observed in batch-type culture medium, which phenol was fed as a substrate. The molecular weight destribution was obtained by using 30K, 100K dalton and $0.45{\mu}$ membrane filters. When the phenol concentrationas a substrate was 120, 230 and 440 mg/L , the specific substrate utilization rate(q) showed 0.639, 1.281 and 1.744 mgTOC/mgMLSS/day, respectively. The endogenous biomass decay rate constant($K_d$) at each substrate concentration was 0.00536, 0.0661 and 0.0749($day^1$), respectively. The $SMP_e$ product rate constant($k_{SMP}_ e$) showed 0.006, 0.0058 and 0.0057($day^1$), respectively. The initial influent substrate during the course of time degraded and produced $SMP_s$. The $SMP_s$ was converted to the $SMP_{nd}$ and endogenous phase converted to the $SMP_e$ ingredients. The molecula weight distribution on loading rate was converted to a higher MW during the course of time.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.3
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• pp.458-465
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• 2011

Response surface methodology (RSM) was applied to optimize substrate conditions of ribose and hydrolyzed wheat gluten solution for Maillard reaction. Independent variables were NaCl concentration of hydrolyzed wheat gluten ($X_1$), concentration of ribose ($X_2$) and concentration of hydrolyzed wheat gluten ($X_3$), while the dependent variables of the central composite design (CCD) were browning index (absorbance 420 nm), DPPH radical scavenging activity (DF) and sensory preference (score). Optimum substrate conditions at $140^{\circ}C$, 30 min reaction were 3% NaCl concentration of hydrolyzed wheat gluten, 6.2% concentration of ribose and 13.27% concentration of hydrolyzed wheat gluten. The coefficients of determination ($R^2$) were 0.975, 0.960 and 0.854, the model fit was very significant (p<0.001). DPPH radical scavenging activities and sensory preferences were predicted as 700 (DF) and 8.42 (score), respectively. The model solution increased more browning and DPPH radical scavenging activities with increasing ribose and hydrolyzed wheat gluten concentration. Especially hydrolyzed wheat gluten concentration was the most influential factor, while NaCl concentration of hydrolyzed wheat gluten hardly affected the responses. Sensory preference was increased with rising wheat gluten concentration and decreasing NaCl concentration of hydrolyzed wheat gluten.

• Journal of the Korean GEO-environmental Society
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• v.15 no.5
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• pp.39-46
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• 2014

The objectives of this study were to determine biodegradation and characteristics of BTEX and MTBE under aerovic-anaerobic conditions and evaluate the potential of natural attenuation method in denitrifying condition.. In the single-substrate experiments, all of the BTEX compounds were degraded under all the conditions. but, lower degradation of benzene and p-xylene were observed under aerobic condition due to the lack of oxygen initially supplied. In the mixed-substrate experiments, BTEX degradation was delayed compared to that in the single-substrate experiments due to a competition of the substrates. Biodegradation of MTBE was observed only under denitrifying conditions and we expected that MTBE mineralized to $CO_2$ without the accumulation of TBA. We also conducted to determine the effect of initial nitrate concentration on BTEX and MTBE degradation. At low nitrate concentration (<50 mg/L), BTEX degradations were limited by the lack of electron acceptor and BTEX degradation was inhibited at high nitrate concentration (>200 mg/L). The results in this study indicated that biotransformation could be applied to the gasoline-contaminated region under aerovic-anaerobic.

• KSBB Journal
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• v.16 no.4
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• pp.321-326
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• 2001

The change of molecular weight inside and outside a capsule produced using coencapsulating technology was investigated. Chitosan and chitosanase were enveloped in this membrane and product released was a loaded the medium by the principle of size exclusion. The leakage of substrate corresponding to the agitation speed was controlled by adjusting the alginate and CaCO$_3$ concentrations. The optimal condition of alginate concentration and agitation speed were 0.5% and 40rpm, respectively. Membrane thickness and capsules diameter were 10 $\mu$m and approx. 3.0 - 1.5 mm, respectively. Molecular weight difference by concentration and alginate viscosity were of little significance. In accordance with the molecular weight distribution versus enzyme concentration relationship, low concentration of enzyme produced high molecular weight oligosaccharides. At a 1.5 mm capsule size the product diffusion rate to outer surface highest. The molecular weight distribution of the released oligosaccharides was ranged from 1000 to 6000 Da. More than 80% of the initial activity of encapsulated enzyme retained after 8hrs of reaction.

• KSBB Journal
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• v.22 no.1
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• pp.43-47
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• 2007

The effect of surfactant on the hydrolysis of used newspaper was investigated. The most suitable surfactant for the pretreatment stage was found to be NP-series surfactants among 9 kinds of non ionic surfactants. Process parameters such as surfactant concentration, mixing speed, pretreatment temperature and time were tested to optimize for maximum digestibility and 0.5%, 100rpm, 30$^{\circ}C$, and 1 h were found to be optimum, respectively. In order to maximize digestibility, substrate was pretreated with NP-20 and then the pretreated substrate was hydrolyzed by adding TW-80. The effect of surfactant on the hydrolysis of previously surfactant-pretreated newspaper was marginal. Therefore, the digestibility with the addition order of enzyme and surfactant was investigated by using surfactant only in hydrolysis stage. The results show that digestibility was more lowered as the surfactant addition after adding enzyme to substrate was more delayed.

• Journal of the Korea Organic Resources Recycling Association
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• v.2 no.2
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• pp.31-37
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• 1994

For a microbiological study of composting process, screening and assay method for biopolymer degrading enzymes and microorganisms were developed and for the study of the possibility of composting in anaerobic state, distribution of sulfate reducing bacteria which plays a final role in anaerobic degradation was investigated. Substrates used for the development of assay methods for biopolymer degradation are ${\beta}-glucan$, xylan, dextran, CMC(carboxy methly cellulose), casein, and collagen. These substrates were made insoluble by a cross-linking agent and linked with dye to make chromogenic substrates. ${\beta}-glucan$ and xylan substrates could substitute congo-red method for screening of polymer degrading microorganisms without damaging the colonies. Sulfate reducing bacteria contained in the sample sludge showed preference to lactic acid, propionic acid, butyric acid and formic acid and could use acetic acid and valeric acid.

• Applied Biological Chemistry
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• v.38 no.3
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• pp.248-253
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• 1995

Optimum conditions for the enzymatic hydrolysis of isolated sesame meal protein were investigated. Optimum conditions by papain were $60^{\circ}C$, pH 6.0, 3% enzyme concentration to substrate and 1.5% substrate concentration, respectively. The optimum operating conditions using pepsin were $55^{\circ}C$, pH 9.0, 3% enzyme concentration to substrate and 1% substrate concentration. The optimum operating conditions using trypsin were $60^{\circ}C$, pH 9.0, 1% enzyme concentration to substrate and 1% substrate concentration.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.29 no.4
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• pp.64-72
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• 1997

백색부후균에 의한 리그닌의 분해양상을 검토하기 위해 리그닌 분해능이 우수하고 laccase활성이 높은 LKY-7 및 C. versicolor-13 균주와 manganese peroxidase 활성은 비교적 높으나 laccase활성이 전혀 나타나지 않는 LSK-27 균주로 lignosulfonate를 처리하였다. LKY-7 과 C. versicolor-13 균주에서는 lignosulfonate의 중합화 현상이 관찰되었으며 중합화는 laccase 활성 과 비례하는 것으로 나타났다. LSK-27 균주에서는 lignosulfonate의 고분자 영역이 분해되면서 탈중합화가 일어났으며 리그닌 분해 효소로는 manganese peroxidase만 검출되었다. 보조기질로 glucose를 첨가한 결과, LKY-7 균주에서는 laccase 활정이 각소하면서 중합화 현상이 어느 정도 감소하였으나 C. versicolor-13 균주는 laccase 활성의 증가와 함께 중합화도 촉진되는 것으로 나타났다. 또한 LSK-27 균주에서도 glucose 첨가에 의해 manganese peroxidase 활성이 증가되면서 lignosulfonate의 중합화가 관찰되었다. lignosulfonate 중합화에는 laccase 뿐만 아니라 manganese peroxidase도 관여하며 보조기질로서 탄소원의 종류도 영향을 미칠것으로 검토되었다.