• Proceedings of the Korean Society for Agricultural Machinery Conference
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• 2003.02a
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• pp.209-214
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• 2003

바이오 센서는 생물학적 인식 반응(Biological recognition reaction)이나 생물 촉매 공정(Bio-catalytic process)을 측정 가능한 전기적 신호로 변환시켜주는 적절한 변환기(Transducer)와 같은 생물학적 인식요소로 이루어진 감지 장치를 의미한다. 1962년 효소를 이용한 Glucose 전극봉의 개발이후 이 분야에 대한 수많은 연구와 기기의 개발이 진행되어왔다. 분석도구로써 바이오 센서는 효소, 항체, 수용체, 세포, 조직 등과 같은 생물학적 인식 요소들에 광범위하게 적용 가능하다는 장점이 있는 반면, 위에 열거한 생물학적 인식 요소들의 불안정성으로 인해 신뢰성이 유지되지 못하는 단점을 동시에 지니고 있다. (중략)

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.571-574
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• 2000

Hydrolase is a group of the most widely used enzymes in industrial biological processes. Generally, their activities are easily changed with pH. With this characteristics, research for the optimal pH of hydrolases is required to obtain the optimization of process conditions. We selected xylanase, lysozyme, glucoamylase and barnase as model enzymes. To predict optimum pH of hydrolases, the calculation program based on Tanford-Kirkwood(TK) model was used. Results show that charge difference of catalytic residues is an important parameter deciding optimum pH and when charge difference of catalytic residues is maximum, optimum pH of the hydrolase establishes.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.412-415
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• 2004

본 연구는 감마선 조사를 이용한 알레르기 저감화 식품을 개발하기 위한 실용화 방법의 안전성을 검토하기 위해 실시되었다. 감마선 조사 후 가열 처리된 OVA는 전기영동상에서pepsin에 의해서 상당히 감소하는 것을 확인할 수 있었다. IgG 항체를 통해 살펴본 소화성은 intact OVA보다 증가하여 가수분해되기 쉬운 형태임을 알 수 있었다. 또한 효소처리 전의 IgE-binding ability는 현저히 감소하였고 최종 효소분해까지 일정하게 낮은 농도가 유지되어 가상 소화모델 시스템 내에서의 안전성을 확인할 수 있었다. 이상의 결과에서 감마선 및 가열 처리를 단독으로 시행하는 공정보다는 감마선과 가열을 병용하는 방법이 알레르기 저감 식품을 개발에 더욱 효과적일 것으로 사료된다.

• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.402-407
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• 1987

Glucose oxidase from Aspergillus niger KUF-04 was purified homogeneously by the procedure of seven steps including crystallization. The ball-like crystalline enzyme was obtained from the 23-fold purified enzyme solution. The glucose oxidase was found to be composed of two identical subunits and the molecular weight of the enzyme and its subunit were estimated to be about 210, 000 and 110, 000 by HPLC and SDS-acrylamide gel electrophoresis, respectively.

• Korean Journal of Food Science and Technology
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• v.16 no.1
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• pp.113-119
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• 1984

Initial moisture content and weight of the rice bran and treatment time were identified as important variables for the inactivation of lipase and peroxidase present in rice bran. Multiple regression analysis was used to obtain a prediction equation to measure the effects of moisture content and weight of the sample and microwave treatment time on the residual lipase activity and loss in weight. It was found that the microwave treatment did not affect acid value and extractability of the rice bran oil.

• Journal of the Korean Society of Clothing and Textiles
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• v.25 no.10
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• pp.1738-1744
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• 2001

본연구의 목적은 반응성 염료를 이용한 텐셀섬유의 피브릴화 조절 효과를 표면 형태, 감량율, 역학적 성질 및 태의 변화의 측면에서 고찰하는데 있다. 반응성 염료에 의한 가교는 섬유의 비결정 영역의 구조를 변화시켜 피브릴화를 억제하였으며 또한 효소의 작용에 영향을 주어 감량율을 감소시켰다. 반응성 염료에 의한 가교는 역학적 성질 중 특히 전단강성, 압축에너지, 압축레질리언스를 증가시켰다. 염색후 효소처리한 시료는 다른 시료보다 numeri와 fukurami 값이 높아 더 나은 종합태를 보였다. 공정순서에 따라 약간씩 차이가 있는 촉감을 나타냈다.

• Proceedings of the KIEE Conference
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• 2002.11a
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• pp.248-250
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• 2002

본 논문은 당뇨병의 지표물질인 glucose의 농도를 극미량의 시료를 사용하여 정량 할 수 있는 방법을 개발하기 위하여 효소 고정화 전극을 제작하였다. 전극은 실리콘 웨이퍼상에 마이크로 크기의 전극을 반도체 공정을 이용하여 제작하였고, 전기 화학적 방법으로 마이크로 전극에 전도성 고분자 Polypyrrole(PPy) 및 glucose oxidase(GOx)를 고정화한 고감도의 전기화학 전극을 개발하였다. 도전성 고분자의 전기 화학적 중합은 순환 전압 전류법으로 하였으며, 용액의 액성에 따른 효소의 표면 전하를 이용하여, 도전성 고분자를 코팅한 전극에 일정한 전압을 인가하고 GOx를 도우핑 하였다. 제작된 전극은 시간대 전류법으로 glucose의 농도에 따른 감도 측정결과 마이크로 리터의 시료에 $5{\mu}A$/decade를 얻었다. 전극의 표면분석은 Scanning electron microscopy(SEM), Energy dispersive X-ray spectroscopy(EDX)를 이용하였다.

• KSBB Journal
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• v.6 no.3
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• pp.309-319
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• 1991

A continuous stirred tank membrane reactor(CSTMR ) was developed and optimized for the production of cod skin gelatin hydrolyzates using endo-protease Alcalase. A experimental design methodology was used to optimize the four performance variables: enzyme concentration, substrate concentration, permeate flux and reactor volume. All four variables studied had an effect on substrate conversion, with enzyme and substrate concentrations being predominant. Conversion increased with the increase in enzyme concentration, with the decrease in substrate concentration, at high volumes and low flux. A strong interaction was observed between enzyme and substrate concentrations and smaller interactions between enzyme and flux and substrate and flux. The optimum operating conditions for the CSTMR process for an initial substrate concentration for 10% were $50^{\circ}C$, pH 8, flux 7.3ml/min, residence time 82 min, and Alcalase to substrate ratio 0.02(w/w). A gradual decay in reactor activity during 8 hrs was 2.1% conversion/hr. Enzyme leakage through the 10, 000 MWCO membrane was 16% at $50^{\circ}C$ and 12% at $35^{\circ}C$, 6hrs. However, there was no apparent correlation between enayme leakage and substrate conversion. The Km value for the CSTMR was 20 times higher than the batch reactor. The productivity(expressed as mg product/mg enzyme) of the CSTMR was more than six fold higher than the batch at $50^{\circ}C$. The hydrolyzate was non-bitter.

• Korean Journal of Food Science and Technology
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• v.12 no.1
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• pp.45-52
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• 1980

The nylon (poly 6, 10) microcapsules containing ${\beta}-galactosidase$ were obtained by the interfacial polymerization of 1, 6-diaminohexane and sebacoyl chloride with ${\beta}-galactosidase$ from Escherichia coli. They were generally spherical and had a mean diameter of $80{\mu}$ with 45 % of the activity recovery. In particular, there was no transport hamper of lactose through the membrane of microcapsules. The characteristics of the microencapsulated enzyme were similar to those of soluble enzyme optimal pHs, $7.0{\sim}7.2$ for the soluble and $7.3{\sim}7.5$ for the microencapsulated ; optimal temperatures, $50^{\circ}C$ for both ; apparent $K_m,\;3.33{\times}10^{-4}(on ONPG),$ $2.86{\times}10^{-3}$ M(on lactose) for the soluble and $5.28{\times}10^{-4}$ (on ONPG), $4.25{\times}10^{-3}$ M (on lactose) for the microencapsulated ; activation energies, 8.94 for the soluble and 9.78 Kcal/mole for the microencapsulated enzyme. Using this microencapsulated ${\beta}-galactosidase$, hydrolyses of lactose and milk lactose were carried out and 80 % of 5 % lactose solution and 70 % of lactose in skim milk were hydrolyzed in 40 hr at $27^{\circ}C$. The reusability and operational stability showed that the remaining activity was 50 % of the original activity after 5 runs and 120 hr of total operating time at $27^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.50 no.2
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• pp.132-137
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• 2018

Enzymatic treatments of maize flour (MF) were investigated using commercial carbohydrases (Ultraflo L and Pentopan 500 BG) to enhance the phenolic acid content and antioxidant property. The total phenolic acid content of the MF was 3.76 mg/100 g, whereas those of the Pentopan 500 BG and Ultraflo L treated MF were 6.85 and 39.55 mg/100 g, respectively. Particularly, ferulic acid content of Pentopan 500 BG-treated MF was 20.0 times higher than that of untreated MF (1.7 vs. 33.9 mg/100 g). Pentopan 500 BG appeared to be more effective than Ultraflo L in increasing the free phenolic acid content. Antioxidant activities of enzyme treated MF were significantly higher than untreated MF. In particular, the Pentopan 500 BG-treated MF (16.0 mmol TE/100 g) was approximately 1.5 times higher than untreated MF (12.6 mmol TE/100 g). Enzymatic hydrolysis of cell wall polysaccharides in MF could be used as an effective procedure for not only increasing phenolic content but also antioxidant activities.