• KSBB Journal
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• v.6 no.2
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• pp.167-174
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• 1991

Enzymatic cellulose hydrolysis depends on the several factors such as the structural features (CrI, particle size and surface area, etc.), the nature of cellulase enzyme system, the inhibitory effects of products, and enzyme deactivation. At the presence of products on the initial hydro- lysis rate of cellulose, cellobiose has more severe inhibitory effect than glucose. Othewise, the inhibition effect of products for adsorbed enzyme is related to the glucose and cellobiose conentration hyperbolically. Enzyme deactivation of FPA and ${\beta}-glucosidase$ were expressed by exponential decay profile.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.508-508
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• 1986

이온성 계면활성제 존재하에서 유기용매에 물을 첨가하면 물이 계면활성제에 약해 둘러싸이면서 유기용매에 용해되어 의사 이상계가 형성된다. 이러한 계를 역미셀 또는 W/O microemulsion이라고 하며 계면활성제로 둘러 쌓인 물분자 집하체를 water pool이라고 한다. 그런데, 10여년 전 water pool에 bipolymer를 용해시킬 수 있다는 사실이 밟혀짐에 따라 이러한 체계를 생체막을 단순화시킨 모형막으로서 막을 통해 일어나는 여러 가지 현상의 규명에 이용하거나 물에 불용성인 기질의 효소 촉매반응의 반응계로 이용하는 연구가 꾸준히 이루어져 있다. 본 강연은 역미셀계에 리파제를 용해시켜 유지의 가수분해를 유도함으로써 지방산을 생산하는 방법에 관한 연구이다. 역미셀계에서 리파제의 특성은 에멀전계와 비교했을 때 큰 차이가 없었으며 물과 계면활성제의 몰 비율(R값)은 효소의 초기반응 속도에 커다란 영향을 끼치는 인자로 나타났다. 올리브유 농도가 5%(v/v), AOT농도가 0.1M, 초기 물 농도가 1.0M의 조건에서 유지의 회분식 가수분해 실험을 행한 결과 이 기질은 거의 완전히 가수분해되었으며, 이 반응계에서 R값과 초기 물 농도는 반응의 평형에 커다란 영향을 끼치는 것으로 나타났는데 초기 물 농도가 증가할수록 평형 가수분해율은 증가하였단 이러한 결과를 반응속도론 측면에서 분석한 결과 역미셀계에서 리파제 반응은 에멀전계에서와는 달리 2차 반응을 따르는 것으로 나타났다. 물 농도가 평형 가수 분해율과 속도 변수에 끼치는 영향을 수학적으로 표시하기 위하여 2차 가역적 반응 속도론에 근거하여 가수분해율, 평형상수, 속도상수 둥을 나타내는 식을 유도하였고 이를 바탕으로 여러 가지 실험 조건 하에서 리파제 반응의 반응 시간에 따른 가수분해율을 예측한 결과는 실제 실험 결과와 잘 일치하였다(편차는 5%). 또한 속도상수와 R값과의 관계식 및 유도한 방정식을 이용하여 추정한 초기속도와 평형 가수분해율을 최대화하는 R값은 각각 10.4 와 11.4 였다.

• Textile Coloration and Finishing
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• v.10 no.4
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• pp.24-29
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• 1998

11종류의 cellulose에 고착된 vinylsulfone(VS)계 반응성 염료(F-type)의 알칼리 가수분해 거동과 염료와 섬유의 결합 안정성을 cellophane film을 이용한 film권층법에 의하여 조사하였다. F-type은 알칼리욕에서 분해되어 VS type을 생성하고 VS type은 가수분해에 의해 hydroxyethylsulfone(Hy)을 생성하거나 cellulose와 재결합하여 F-type을 생성하였다. F-type은 알칼리 처리에 의해 cellulose의 수산기의 위치에 기인하는 bimodal 가수분해 거동(fast and slow hydrolysis)을 나타내었다. Orange 7과 Yellow 17는 cellulose와의 반응성이 높고 F-type의 초기 분해속도가 빠르며 일반적으로 fast 가수분해속도가 slow 가수분해 속도보다 약 5배정도 큼을 알 수 있었다. 또한 조사된 대부분의 염료의 경우 slow 가수분해 속도는 거의 유사함을 알 수 있었다.

• Journal of the Korean Society of Clothing and Textiles
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• v.23 no.1
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• pp.111-119
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• 1999

가수분해된 네 개의 반응성 염료를 이용하여 견, 양모 나일론 섬유를 염색할 때 영향을 미치는 여러 인자들에 대하여 연구하였다 염의 투입을 가수분해 전과 후로 달리하였을 때 염색된 직물의 K/S 값에 미치는 영향은 염료와 직물의 종류에 따라 각기 달랐으며 염의 영향은 염료의 분자 크기가 클 때 더 크게 나타났다. 이는 염 노동의 증가시 염욕 안에서의염료 용해도가 염료 분자가 클 때 더많은 영향을 받기 때문인 것으로 생각된다. 욕비 증가시에는 염색된 직물의 K/S값은 초기에 감소를 보이다가 높은 욕비에서 K/S값이 증가되었는데 이는 염의 농도의 감소로 인한 영향으로 사료된다. 가수분해된 반응성 염료로 염색된 직물의 수세 견뢰도는 염료의 분자 크기에 의해 영향을 받았으며 직물의 마찰 땀 견괴도는 Gray scale에서 3보다 높았다 본 연구의 결과는 면섬유 염색에 사용한 가수분해된 반응성 염료를 이용하여 견, 양모, 또는 나일론섬유의 염색에 재 사용할 수 있는 가능성을 제시하여 준다.

• Korean Journal of Food Science and Technology
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• v.29 no.1
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• pp.26-31
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• 1997

Bee venom (Apis mellifera) phospholipase $A_2$ solubilized in reversed micelles containing small amount of water stabilized by surfactant could catalyze the hydrolysis of dipalmitoyl phosphatidylcholine (DPPC). A sensitive and simple high performance liquid chromatographic (HPLC) methodology of phospholipase $A_2$ assay for the hydrolysis of DPPC was developed. Kinetic analysis of the phospholipase $A_2$-catalyzed reaction was found to be possible in reversed micelles. Among the surfactants and organic solvents tested, aerosol-OT and isooctane were most effective for the hydrolysis of DPPC in reversed micelles. Optimal temperature, optimal pH, $K_{m,app.},\;V_{max.,app.}$ and activation energy were determined to be $35{\sim}40^{\circ}C$, 7.0, 8.73 mM, 2.83 units/㎎ protein and 12.31 kcal/mole, respectively. The hydrolysis activity was dependent on water content and maximum activity was obtained at R value (=[water]/[aerosol-OT]) of 10.0.

• KSBB Journal
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• v.10 no.5
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• pp.540-546
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• 1995

Dry corn gluten meal of 70% protein content was enzymatically hydrolyzed by alkaline protease in a pH-state reactor. Such process variables as temperature, pH, and enzyme-to-substrate ratio were varied, and at each condition degree of hydrolysis was monitored and calculated. The ultimate degree of hydrolysis, which ranged between 25 and 28% based on gluten protein mass, was not significantly affected by the process variables. However, $50^{\circ}C$ and pH 9-10 appeared optimum. Kinetic analysis indicated enzyme deactivation was negligible during the hydrolysis, and the experimental data were near perfectly fitted to the model kinetic equation which was modified after neglecting enzyme deactivation term. The enzyme reaction was 1$100\times$ scaled up and basically the same hydrolysis performance was resulted. Amino acid analysis showed the hydrolyzate was relatively rich in glutamine/glutamic acid, leucine, and alanine at 19.6, 16.1, and 12.3 mole %, respectively.

• Journal of the Korean Chemical Society
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• v.53 no.2
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• pp.213-217
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• 2009

• KSBB Journal
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• v.15 no.6
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• pp.630-634
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• 2000

Chiral epoxides are useful chiral synthons in organic synthesis, and various biological methods have been investigated for their production. In this work, the enantioselective resolution of racemic styrene oxide was investigated using Aspergillus niger sp. for the production of optically pure (S)-styrene oxide. The enantioselectivity and initial hydrolysis rates of the racemic substrate were highly dependent of the pH, temperature, and the volume ratio of cosolvent. Experimental sets of pH, temperature, and the volume ratio of cosolvent were investigated using a central composite experimental design, and reaction conditions were optimized by response surface analysis. The optimal conditions of pH, temperature, and the volume ratio of cosolvent were determined to be 7.78, $28.32^{\circ}C$, and 2.4%(v/v), respectively, and optically pure (S)-styrene oxide (>99% ee) was obtained at 35% yield using this microbial enantioselective hydrolysis reaction.

• Journal of the Korean Chemical Society
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• v.38 no.5
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• pp.366-371
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• 1994

The kinetics of the hydrolysis of 5,6-dihydro-1,4-thiazine derivatives was investigated by ultraviolet spectrophotometry in $H_2O$ at 25$^{\circ}C$. A rate equation which can be applied over a wide pH range was obtained. The substituent effects on the hydrolysis of 5,6-dihydro-1,4-thiazine derivatives were studied and the rate of hydrolysis was shown to be accelerated by electron donating groups. Final product of the hydrolysis was 2-(N-acetylaminoethylthio)-acetoacetanilide enol from Judging from the results of the rate equation, general base effect, activation parameters and final products, the hydrolysis of 5,6-dihydro-1,4-thiazine derivatives seemed to be initiated by the neutral $H_2O$ molecule which does not dissociate at pH below 10.0, but proceeded by the hydroxide ion at pH above 11.0, and those two reactions occurred competively at pH 10.0∼11.0 range. On the basis of these findings a plausible mechanism for the hydrolysis of 5,6-dihydro-1,4-thiazine derivative was proposed.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.303-307
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• 2001

Operation conditions to maximize the hydrolysis of beef tallow was investigated by using the response surface method. In the response surface analysis, reaction temperature, pressure, and ratio of fat to water was considered as independent variables. The concentrations of triglycerides. diglycerides, monoglycerides and free fatty acids were considered as dependent. variables. The optimum conditions for the hydrolysis was as follows' the reaction temperature was $271^{\circ}C$, pressure 86 bar and ratio of fat to water was 106.08g / 133.93 g. The maximum concentration of free fatty acids was 96.49 % at these optimum conditions.