트레할로스 및 효소제 첨가가 백설기 품질에 미치는 영향

오문헌(Moon-Hun Oh),신형찬(Hyung-Chan Shin),박종대(Jong-Dae Park),이현유(Hyun-Yu Lee),김근성(Keun-Sung Kim),금준석(Jun-Seok Kum) 한국식품영양과학회 2010 한국식품영양과학회지 Vol.39 No.7

본 연구에서는 백설기의 품질변화를 최소화할 수 있는 방안으로 효소제(BS-300 0.3%)와 트레할로스(trehalose 3%, 6%)를 첨가한 6가지의 백설기를 제조하여 품질변화를 관찰 하였다. 쌀가루의 RVA호화특성을 조사한 결과, 효소제와 트레할로스를 첨가한 쌀가루는 가공의 안정도가 높아지고, 노화도가 감소되는 것으로 나타났다. DSC를 이용하여 백설기의 노화정도를 비교한 결과, 효소제와 트레할로스를 첨가한 시료에서 노화억제 효과가 나타났고 효소제와 트레할로스 6%를 함께 첨가한 시료에서 가장 큰 효과가 나타났다. 제조한 백설기의 저장기간에 따른 품질변화는 효소제와 트레할로스의 병행처리가 보수성을 향상시키며 색도 및 경도 변화를 억제하는 것으로 나타났다. 따라서 백설기의 품질개선에 가장 효과적인 배합비는 효소제 0.3%와 트레할로스 6%가 함께 첨가된 백설기로 나타났다. This study investigated changes of quality during storage period with 6 types of Backsulgie manufactured by adding enzyme (BS-300 0.3%) and trehalose (3%, 6%) to minimize the changes of quality and tried to determine their optimal combination ratio. When Rapid Visco Analyzer (RVA) gelatinization properties of rice powder were examined, adding both of enzyme and trehalose to the powder increased stability of process and reduced retrogradation. In comparison of the degree of retrogradation of Backsulgie by using Differential Scanning Calorimetry (DSC), the sample with enzymes and trehalose suppressed retrogradation. Moreover, the retrogradation effect became larger by using both of enzyme and trehalose and it was the largest in the sample with 0.3% enzyme and 6% trehalose. Enzyme and trehalose added to Backsulgie were found to improve water retention, to minimize changes of texture and color during storage of Backsulgie. Therefore, optimal combination ratio of Backsulgie is 0.3% enzyme with 6% trehalose added Backsulgie.

서양 허브식물의 화학성분

오문헌(Moon-Hun Oh),황혜정(Hea-Jeung Whang) 한국식품과학회 2003 한국식품과학회지 Vol.35 No.1

쌀된장 분말을 첨가한 돈가스 소스의 품질특성

윤향식 ( Hyang Sik Yoon ),주선종 ( Seon Jong Joo ),김기식 ( Ki Sik Kim ),김숙종 ( Sook Jeong Kim ),김성수 ( Sung Soo Kim ),오문헌 ( Moon Hun Oh ) 한국식품저장유통학회 ( 구 한국농산물저장유통학회 ) 2006 한국식품저장유통학회지 Vol.13 No.4

한국산 허브를 이용한 혼합 침출차 가공특성

주선종 ( Seon Jong Joo ),최금주 ( Keum Joo Choi ),김기식 ( Ki Sik Kim ),박성규 ( Sung Gue Park ),김태수 ( Tea Su Kim ),오문헌 ( Moon Hun Oh ),이상수 ( Sang Su Lee ),고재원 ( Jae Won Ko ) 한국식품저장유통학회 ( 구 한국농산물저장유통학회 ) 2002 한국식품저장유통학회지 Vol.9 No.4

쌀된장분말을 첨가한 쿠키의 품질특성

윤향식 ( Hyang Sik Yoon ),주선종 ( Seon Jong Joo ),김기식 ( Ki Sik Kim ),김숙종 ( Sook Jeong Kim ),김성수 ( Sung Soo Kim ),오문헌 ( Moon Hun Oh ) 한국식품저장유통학회 ( 구 한국농산물저장유통학회 ) 2005 한국식품저장유통학회지 Vol.12 No.5

콩 β-Conglycinin의 대장균 발현과 정제

오문헌,노영희 한국식품영양학회 1999 韓國食品營養學會誌 Vol.12 No.2

콩 단백질은 글리시닌과 β-콘글리시닌을 주요 성분으로 하며, 콩 β-콘글리시닌이 나타내는 알레르기 원인과 콜레스테롤 저하 작용을 밝히고저 유전자 공학적인 방법을 시도하였다. 즉 β-콘글리시닌의 α-subunit를 유전자 클로닝하고 대장균에서의 발현시스템을 구축하였다. 발현벡터는 pET21d이며 플라스미드를 구축하여 E. coli BL21(DE3)에 형질전환시켰고 발현된 단백질은 균체전체 단백질의 15%이며 90%이상이 가용화 상태로 축적되었다. 축적된 발현 단백질은 천연의 β-콘글리시닌과 동일한 트리머로 확인되었다. 발현 단백질은 20∼40% 황산암모늄 분별침전과 Q-Sepharose 이온교환크로마토그래피, Butyltoyopearl 소수성 컬럼크로마토그래피로 정제하였다. 이것은 콩단백질의 기능특성을 규명하는데 필요한 대장균 대량 발현계를 확립하고 발현 단백질의 정제방법을 확립한 결과이다. Soybean protein consists of two major components β-conglycinin and glycinin, which together constitute 70% of the total seed storage protein at maturity. β-Conglycinin is a trimeric glycoprotein and formed by the assembly of various combinations of three subunits, α,α´and β, which have molecular weights of 69,000, 72,000 and 42,000, respectively. Recently, β-conglycinin was identified as powerful LDL lipoprotein receptor activation, hypercholesterolemia and major allergenic proteins. To investigate these reasons, we constructed an expression system of cDNA encoding α-subunit of β-conglycinin in Escherichia coli and purified the expressed protein. The pro-β-conglycinin sythesized in Escherichia coli BL 21 (DE3) comprised approximately 15% of the total bacterial proteins and the expressed protein are formed soluble and trimer such as native protein in Escherichia coli cells. The highly expressed protein was purified to homogeneity by salt precipitation with 20∼40% ammonium sulfate, ion-exchange chromatography with Q-sepharose and hydrophobic column chromatography with Butyltoyopearl.

한국산 자초 적색소의 분리 및 확인

이제헌,오문헌,이희봉 한국식품영양학회 2000 韓國食品營養學會誌 Vol.13 No.4

한국산 자초 적색소의 추출조건과 적색소를 확인한 결과 자초에서 색소성분의 추출은 지용성 용제가 물에 비해서 추출력이 좋으며 특히 95% 에탄올이 적색소 추출에 효과적이었다. 적색소 성분의 추출은 침출 시간에 관계없이 비교적 고른 추출력을 보였으며 40℃이하에서 20분 정도 추출하면 적색소가 충분히 추출되었다. 한국산 자초뿌리의 적색소 성분을 분리하여, IR, NMR. GC/MS로 확인한 결과 대부분이 acetylshikonin으로 동정되었다. Conditions of isolation for the red color pigments from the Korean Lithospermum erythrorhizon were investigated and identification of the red pigment was analysed. Non-polar solvents were more effective than water. Especially, 95% ethanol was observed as optimum solvent for the pigments extraction. About 20 minutes at 40℃ with 95% ethanol was enough for the extraction of the red pigments. The major pigment was analysed as acetylshikonin by TLC, IR, NMR and GC/MS.

Sweep Co-Distillation법에 의한 산화방지제의 추출법

김재관,황혜정,오문헌,도영숙,윤미혜 한국식품영양학회 1999 韓國食品營養學會誌 Vol.12 No.4

식용유지 중의 산화방지제를 효율적으로 분석하기 위하여 일반적인 용매추출법과 SCD법으로 전처리하여 HPLC법으로 비교 분석하였다. SCD법의 최적조건은 florisil의 활성도와 UNITREX의 온도와 추출시간에 따른 회수율로 분석하였다. 식용유지에 산화방지제를 농도별로 가하여 용매추출법과 SCD법의 회수율을 비교한 결과 용매추출법은 80.4∼102.1%, SCD법은 89.8∼106.4%로 나타났다. Florisil의 활성화에 따르면 2% 수분 첨가시 TBHQ, BHA, BHT는 89.8∼106.4%로 회수율이 가장 높았고, PG는 5% 수분 첨가시 53.9±7.3%의 회수율을 보였다. 회수율은 UNITREX의 210℃에서 20분간 추출하였을 때 가장 높았다. This study was conducted to evaluate the extraction methods for the determination of antioxidants in soybean oil. Recovery rates of various antioxidants in soybean oil showed similar rates as 80.4∼102.1% by solvent/solvent extraction method and 89.8∼106.4% by sweep co-distillation method except 46.6∼61.2% of PG at corresponding spiked concentractions. The maximum recovery rates of antioxidants were obtained when extraction time and extraction temperature used in UNITREX were 20min and 210℃ respectively. In the recovery rates with the activation of florisil, when 2% of water was added to florisil, the highest recovery rates for TBHQ, BHA, BHT were obtained by sweep co-distillation method. Therefore, sweep co-distillation method showed less solvent, simple operation and high recovery rate compared with solvent/solvent extraction method.

콩단백질의 대장균 발현과 정제

오문헌,정재홍,노영희,이희봉 한국식품영양학회 1996 韓國食品營養學會誌 Vol.9 No.4

콩단백질은 글리시닌과 β-콘글리시닌을 주요 성분으로 한다. 영양성 및 가공 특성을 개선하기 위하여 유전자공학적인 방법을 시도하였다. 즉 β-콘글리시닌의 β-서브유니트롤 유전자 클로닝하고 대장균에서 발현시켰다. 발현벡타는 pET 21d이며 플라스미드를 구축하여 E.coli BL21(DE3)에 형질전화시켰다. 발현된 단백질은 균체 전체 단백질의 20%이며 가용화 상태로 축적되었다. 축적 발현단백질은 천연의 β-콘글리시닌과 동일항 트러머로 확인되었다. 정제는 호아산암모늄 20∼40%분별침전, Q-Sepharose 이온교환크로마토그라피, Butyltoyoperal 소수성 컬럼크로마토그라피로 하였다. 이것은 콩단백질의 특성을 규명하는데 필요한 대장균 대량 발현계를 확입하고 발현단백질의 정제방법을 확립한 결과이다. One of the major objectives of the food industry is the enrichment of the functional properties and nutritional value of soybean protein. To attain this goal, an expression system of cDNA encoding native and protein-engineered soybean proteins in a microorganism must be developed and the function then ability of self-assembly and the functionalities of the expressed proteins should be evaluated before the modified genes are transfered to soybean plants. The pro-β-conglycinin synthesized in E. coli BL21(DE3)comprised approximately 20% of the total bacterial proteins and the expressed protein are formed soluble and trimer such as native protein in E. coli cells. The highly expressed protein was purified to homogeneity by salt precipitation with 20∼40% Ammonium sulfate ion-exchange chromatography with Q-Sepharose and hydrophobic column chramatography with Butyltoyoperal. Therefore, we concluded that the high-level expression system of β-conglucinin cDNA was established and a relatively simple and rapid method for purifying pro-β-conglicinin was also developed.

밀 β-Amylase의 정제 및 특성

김준평,오문헌 中央大學校 遺傳工學硏究所 1991 遺傳工學硏究論集 Vol.4 No.1

β-Amylase (α-1, 4-D-glucan maltohydrolase, EC 3.2.1.2) was isolated and purified from wheat(Triticum aestivum var. Gerumil) produced in Korea. The homogeneity of β-amylase was examined by polyacrylamide disc gel electrophoresis(PAGE), Wheat β-amylase was purified by using the methods of ammonium sulfate fractionation, ion-exchange chromatography on DEAE-cellulose, calcium phosphate gel absorption, Sephadex G-100 gel filtration, hydroxyapatite column chromatography. The enzyme was futher fractionated into three fractions A, B and C by hydroxyapatite column chromatography. The two major fractions A and C showed 37.9 and 33.1 times higher activity than crude enzyme, respectively, and the specific activity was found to be 246.1 and 215.2 unit/mg, respectively. The molecular weight of β-amylase was determined by SDS electrophoresis and it was found to be 54,500 daltons. The isoelectric points of fractions A and C were 4.96 and 4.61, respectively. The N-terminal amino acids of the fractions A and C determined by DABITC's method were glycine. The fractions A and C of wheat β-amylase were estimated to have 512 and 516 amino acid residues/mole, respectively. The activity of wheat β-amylase was decreased by ??, ??, ?? and ?? ions, whereas it was increased by ?? and ?? ions. Km values of the fractions A and C of wheat β-amylase for soluble starch were 0.19 and 0.56%, respectively, indicating high affinity between fraction A and substrate. Optimum temperature and pH for the fractions A and C of wheat β-amylase were 50℃ and 6.0. and both the fractions were stable at 0-60℃ anc at pH 4.5-7.5.