• Applied Biological Chemistry
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• v.38 no.1
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• pp.20-25
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• 1995

This experiment was attempted to improve ethanol productivity by immobilization of Kluyveromyces marxianus FO43 using Jerusalem artichoke powder. Sucrose medium was used to determine optimum conditions for cell immobilization. The optimum conditions were alginate concentration of 2%, bead size of 2 mm, a particle input ratio of 30 : 100, cultivation period of 24 hours, and substrate concentration of 10%(w/v). The immobilized cells produced the high concentrations of ethanol at pH $4.5{\sim}6.5$ and $30{\sim}45^{\circ}C$, broader ranges of pH and temperatures than those of free cells. Under optimum conditions the immobilized cells showed ethanol concentration of 46.4 g/L and productivity of 1.93 g/L.h. The microphotograph using a two phase contrast microscope showed that immobilized cells cultivated under the optimum conditions were densely populated toward the surface area of beads.

• Microbiology and Biotechnology Letters
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• v.20 no.4
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• pp.459-469
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• 1992

The immobilization characteristics of Zymomonas mobilis for ethanol production were examined. Four different strains of Zymomonas mobilis have been used for ethanol production. Among those, Zymomonas mobilis KCTC 1534 has been selected as the best strain for the highest ethanol productivity from glucose and sucrose. The optimum temperature and pH of the selected strain for ethanol production were $37^{\circ}C$ and 5.0 respectively for both free and immobilized cells. When the cells were immobilized by the gel entrapment method, the immobilized cells could produce ethanol at a little higher temperature than free cells. Calcium alginate was selected as the best gel for immobilizing cells. The immobilized cells could maintain the viability of 80% in 10 weeks storage at $4^{\circ}C$ in the medium with 2% calcium chloride. 20-25 hours of preincubation in 10% glucose solution was required for the activation of immobilized cells entrapped within calcium alginate gel.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.279-285
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• 1992

Cytidine deaminase (EC 3.5.4.5) from Aspergillus fumigatus IFO 5840, which was the first cytidine deaminase to be found in a mold, was fractionated with ammonium sulfate (35-60%). When the enzyme solution in 0.25M of Tris-HCI buffer (pH 7.2) was preincubated at $37^{\circ}C$ for 25min, the enzyme activity was reached to maximum state. The optimum pH and temperature for the enzyme activity were found to be 6.8 to 7.2 and near $37^{\circ}C$, respectively. The enzyme was stable in a pH 7.2 to 9.0, and was generally stable at 4$0^{\circ}C$, but after treating at 6$0^{\circ}C$ for 20min at the optimal pH, 17% of the enzyme activity was inactivated, and disappeared completely by treating at 1$0^{\circ}C$ for 25min. Activation energy (Ea) of fungal cytidine deaminase was calculated as 14.190 Kcal /mol by the Arrhenius plot, and temperate coeffient ($Q_{10}$ ) of the enzyme was calculated as 2.163.

• Korean Journal of Food Science and Technology
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• v.34 no.1
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• pp.65-72
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• 2002

This study was to determine the optimum conditions of malt extracting temperature, extracting time of malt in water, ratio of malt to water, and rice volume of malt extract water on saccharification in producing sikhe (sweet rice drink) using central composite design of response surface methodology. Glucose and maltose were analyzed by a biosensor having dual cathode system. The optimum temperatures of malt extracting for glucose and maltose were 60 and $55^{\circ}C$. The saccharification power for the two sugars was highest when malt powder soaked for 6.5 and 5.75 hour, respectively. And ratios of malt to water for optimum saccharification were 1 : 6.3 to 1 : 8.8, respectively. The optimum volumes of malt extracting to rice for the two sugars were 0.48% and 0.6%, respectively. The application of response surface methodology to sikhe processing showed a good correlation with high significance.

• Korean journal of food and cookery science
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• v.13 no.5
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• pp.623-626
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• 1997

The purpose of this study was to investigate the properties of proteolytic enzymes extracted from mulberry (Morus alba L.). The protease activity of the enzymes from mulberry was 2,358 unit/g. The enzymes showed strong activities toward hemoglobin and collagen. The optimum temperature and pH of the enzymes were 50$^{\circ}C$ and 6.0, respectively. The enzymes were stable at the temperature range of 30$^{\circ}C$ to 60$^{\circ}C$ and the pH from 5.0 to 7.0 for 1 hr at 37$^{\circ}C$ of incubation and also retained whole activity after incubation for 1 hr at 60$^{\circ}C$.

• Applied Chemistry for Engineering
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• v.10 no.8
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• pp.1200-1209
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• 1999

Prediction model was composed by optimal parameter estimation from best fitting on reactant temperature profile, inlet and outlet temperature of coolant and yield of dual fixed-bed catalytic reactor(FBCR) which was measured in the industrial field. In order to design the FBCR which could obtain maximum conversion and yield, we investigated the effect of catalyst bed length and reactor radius changes. An uniform activity FBCR showed the best performance at z = 2.8 m of total catalysst bed length in case of reactor radius r = 0.01241 m and z =2.80 m(upper layer: 1.88 m, lower layer: 0.92 m) under reactor radius r = 0.01254 m for a dual activities FCBR. In case of reactor radius changes, the axial temperature profile and maximum radial temperature was rapidly risen for radius increase. The reactor radius decrease showed the opposite result.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.3
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• pp.348-355
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• 1989

This experiment was conducted to investigate the characteristics of alkaline protease from Aspergillus fumigatus which was isolated from soil as a superior strain for the production of the alkaline protease. The optimum temperature for enzyme activity was $50^{\circ}C$ and optimum pH was 9.0. The enzyme was stable at pH 8.0 to 10.0 and thermal inactivation was shown $30^{\circ}C$. The activity of the enzyme was increased by the addition of $Mn^{++},\;Cu^{++},\;Ba^{++},\;Mg^{++},\;$wheras it was inhibitied by $K^+,\;Fe^{+++},\;Ag^+,\;Pb^{++},\;Na^+,\;Ca^{++},\;Hg^+,\;Zn^{++}$. EDTA. 2, 4-DNP, ${\varepsilon}-amino$ caproic acid did not show inhibitory effect on the proteolytic activity of alkaline protease but P-chloromercuribenzoic acid inhibited the enzyme activity, indicating that reactive sulfhydryl group is required for the enzymatic activity. The reaction of this enzyme followed typical Michael-Menten Kinetics with the Km value of $8.33{\times}10^{-4}mole/{\ell}$ with the Vmax of $47.62{\mu}g/min$. This enzyme had stronger proteolytic activity than trypsin on substrate such as casin and hemoglibin.

• Microbiology and Biotechnology Letters
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• v.30 no.1
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• pp.33-38
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• 2002

Purification and characterization of enzyme property of a cell-wall lytic enzyme against Lactobacillus plantarum were carried out. Final specific activity of purified enzyme was 5.8 units/mg and purity of the enzyme was increased 8.3 fold compared with the enzyme activity in culture broth. The molecular weight of purified enzyme was estimated to be 60,000 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis. Optimal pH and temperature for the activity of this enzyme were 3.0 and 4$0^{\circ}C$, respectively. The cell-wall lytic enzyme activity was maintained at 3$0^{\circ}C$ when treating the enzyme for 30 mins, whereas the activity was decreased to 80% of the maximum level at 4$0^{\circ}C$ The enzyme activity exhibited good stability at the range of pH 4~7.

• KSBB Journal
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• v.15 no.1
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• pp.9-13
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• 2000

In order to determine the characteristics of $\beta$-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures trom 55 to $70^{\circ}C$ and its optimum temperature was $65^{\circ}C$. The $\beta$-glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of $\beta$-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at $55^{\circ}C$ for 60 min, more than 90% of the enzyme activity was still sustained. Iron($Fe^{++}$) stimulated enzyme activity, whereas mercury($Hg^{++}$) and copper($Cu^{++}$) inhibited. Compared to salicin as a substrate, the relative activity for cellobiose was observed to be 48.6%. The apparent $K_m$ and $V_{max}$ of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1976.10a
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• pp.190.4-190
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• 1976

Naringinase 생산 균주로 분리 선정된 Asp. niger S-1은 동시에 Hesperidinase도 강력히 생산함이 확인 되었으며 이 균의 효소학적 특성을 요약하여 1. 최적 반응 온도는 $60^{\circ}C이며$ $80^{\circ}C에서$ 30분 열처리 하여도 65%을 활성을 가지며 pH 5.0부위에서 최적반응과 안정성을 보였으며 Mg(이온)은 반응을 활성화 하였다. 2. Aceton을 60% 처리하여 조효소를 11배 정제하였으며 35%가 회수되었고 유안 0.4-0.6 포화로 48배 정제되었으며 13%가 회수되었다.