• 한국식품과학회지
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• 제25권1호
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• pp.39-45
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• 1993

대두 단백분해효소(pepsin, actinidin)를 작용시켜 단백질 분자에 변형을 줌으로써 이에 따른 식품학적인 기능성의 변화에 대하여 연구하였다. 효소와의 반응시간에 따른 변화에 대하여 연구하였다. 효소와의 반응시간에 따른 대두단백질의 가수분해도를 측정한 결과, pepsin은 초기부터 매우 급격히 대두단백을 가수분해 시켰으며 반면 actinidin에 의한 가수분해는 반응시간이 경과함에 따라 완만하게 진행되었다. PAGE에 의한 결과는 두 효소가 비슷한 경향을 보여 반응이 진행될수록 아랫쪽으로 점차 이동하는 하나의 넓은 band를 보였다. SDS-PAGE에 서는 native SPI가 약 9개의 뚜렷한 band를 보였으나 actinidin에 의한 경우 $3{\sim}4$개의 band를 나타내었다. 그러나 pepsin으로 5분 반응시킨 경우 MW $24,000{\sim}13,000$에 이르는 하나의 band를 나타내어 actinidin이 특정한 band를 선택적으로 가수분해하는 경향과는 다른 결과를 보였다. 대두 단백 가수분해물의 기능적 특성을 측정한 결과, pepsin으로 반응시킨 경우 용해도는 대조군이나 actinidin의 경우보다 뚜렷이 증가했고, 전 pH 범위에서 유화형성력이 향상되었다. 또한 모든 실험군의 기포형성력이 전 pH에서 증가했으며, 등전점 부근에서는 효소반응 시간이 경과할수록 기포안정성도 증가하였다. 그러나 actinidin 처리시 등전점 부근에서만 유화형성력이 향상되었고, 5분 반응시킨 실험군의 기포형성력이 가장 높았으며, alkaline 범위에서 기포안정성이 증가되었다. 이와 같이 각 가수분해물의 기능성의 차이는 단백분해효소마다 그 작용부위가 다르고 이에 따른 단백 가수분해물의 물리, 화학적 특성이 달라져, 그 결가 가수분해물의 기능적 특성에 영향을 끼치는 것으로 사료된다.

• 한국식품저장유통학회지
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• 제17권1호
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• pp.91-99
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• 2010

상어의 껍질과 육 조직으로부터 산 (citric acid) 가용성 콜라겐 (ASC)과 pepsin 가용성 콜라겐 (PSC)의 추출 및 탈색조건을 조사하였다. 비 콜라겐 단백질을 제거하기 위한 적정 NaOH 농도는 0.3 N이었으며 처리시간은 9시간이었다. 상어껍질의 탈색은 생 원료에 대하여 10배량의 0.48% sodium hypochlorite로 60분간 처리하는 것이 적절하였다. ASC 및 PSC의 추출시 산의 적정농도는 각각 0.3 M 및 0.1 M이었고, 추출시간은 각각 72시간 및 24시간 이었다. 산가용성 콜라겐인 ASSC (citric acid soluble shark skin collagen)와 ASMC (citric acid soluble shark muscle collagen), pepsin 가용성 콜라겐인 PSSC(pepsin and citric soluble shark skin collagen)와 PSMC (pepsin soluble shark muscle collagen)에 함유된 총 단백질 함량은 각각 88.66, 83.09, 90.33 및 84.81% (dry basis)이었으며 시판 표준 콜라겐의 88.86%와 대등하였다. Hydroxyproline의 함량으로부터 산출한 순 콜라겐 함량은 ASC에서는 25.70~70.31%, PSC에서는 32.94~83.09%이었다. 상어육과 껍질 (dry basis) 100 g으로부터 얻을 수 있는 콜라겐의 수율은 ASC는 53.85~57.22%, PSC는 20.81~23.28%이었다.

• 한국축산식품학회지
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• 제18권2호
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• pp.157-163
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• 1998

This study was carried out to examine that pepsin-hydrolyzed bovine lactoferrin has applicabilities which are market milk and dairy products. The stability of pepsin-hydrolyzed bovine apo-lactoferrin and the change of its antibacterial character has been studied under various method for pasteurization (LTLT; 65$^{\circ}C$ / 30min., HTST ; 75$^{\circ}C$ / 15sec., UHT ; 135$^{\circ}C$ / 3sec.) and pH Values (pH 2.0, pH 4.0, pH 6.8). The ehated samples were assayed for minimal bacteriocidal concentrations (MBCs) and bacteriocidal effect against E. coli. The results obtained were summarized as follows: After fractionation of pepsin-hydrolyzed bovine lactofeerin by gel filtration. several peptide fractions were found that had strong antibacterial activity. SDS-PAGE showed that the one of these fractions with strong antibacterial activity, which had a molecular mass a range of 30∼33KDa. The MBCs for pepsin-hydrolyzed bovine lactoferrin fraction No. 2 against E. coli required to cause complete inhibition of growth varied within the range of 200∼400 $\mu\textrm{g}$/ml, depending on heat treatments and pH conditions. The peptide fraction No. 2 showed strong bacteriocidal activity against E. coli at LTLT and HTST treatments under acidic pH conditions. and was reduced activity at UHT treatment under pH 6.8 condition.

• Journal of Animal Science and Technology
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• 제47권5호
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• pp.851-856
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• 2005

본 연구는 살균온도, pH 및 소화효소의 처리에 따른 anti-H. pylori IgY의 안정성을 평가하였다. 열 안정성 실험시 모든 처리구에서 anti- H. pylori IgY 함량은 대조구에 비해서 유의적으로 감소되었다(p＜0.05). 그러나 저온살균 처리구(63$^{\circ}C$, 30분)와 초고온살균 처리구(130$^{\circ}C$, 2초)에서 WSF 중 anti-H. pylori IgY 함량은 각각 76%와 78% 이었다. pH의 안정성은 pH를 7.0에서 1.5로 감소시킴에 따라 anti-H. pylori IgY의 함량은 감소되는 경향을 보였다. pH 5.0으로 조정한 WSF를 37$^{\circ}C$에서 1시간 처리한 후 anti-H. pylori IgY의 함량은 84.4%인데 비해서 pH 2.5에서는 28.6%의 anti-H. pylori IgY 함량을 보였다. 그리고 pepsin과 trypsin을 처리한 후 anti-H. pylori IgY의 안정성도 평가하였다. 100 unit의 pepsin에서 1시간과 2시간 처리시에는 시간에 따른 항체의 함량은 차이가 없었으나, 200 unit의 pepsin 처리구에서는 시간에 따른 항체 함량이 유의적으로 차이가 있었다(P＜0.05). 그러나 pepsin의 농도나 반응시간에 관계없이 pH 4.0에서 항체는 비교적 안정하였다. pH 7.0, 37 $^{\circ}C$에서 trypsin을 처리한 후 난황액과 WSF 중 anti-H. pylori IgY의 함량은 반응시간의 증가에 따라서 유의적으로 감소되었다(P＜0.05). 난황액 중 항체 함량은 120분 처리시 85%가 잔존하였으나, WSF 중 항체 함량은 30분 처리시 62%로 감소하였다. Trypsin을 처리한 후 난황중의 항체의 안정성은 WSF 보다 유의적으로 높았다(P＜0.05).

• Journal of Dairy Science and Biotechnology
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• 제14권2호
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• pp.135-146
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• 1996

본 연구는 UF에 의한 cheese base제조과정 중 calf rennet 과 대용효소인 porcine pepsin을 각각 단독, 또는 1:1로 혼합첨가하여 cheese base를 제조한 후, HPLC와 전기영동을 이 용하여 casein의 변화를 관찰하기 위여 실시하였으며 얻어진 결과는 다음과 같다. HPLC를 이용, Superose 12 column에 의하여cheese casein을 gel filtration한 결과, Cheddar cheese는 제조직후 5개의 분획이었던 것이 6개월 숙성후 8개의 분획으로 분별되었으며, 효소처리하지 않은 대조구 cheese base는 8주 숙성중 4개의 분획으로 분별되어 분획수의 큰 변동은 없었고, calf rennet 단독처리구는 4개에서 5개로, 1:1혼합효소처리구(calf rennet : porcine pepsin)는 4개에서 7개로, porcine pepsin 단독처리구는 4개에서 8개로 각각 분별되어 porcine pepsin이 혼합됨에 따라 casein의 분해 정도가 높았다. 효소처리하여 8주간 숙성시킨 cheese base의 casein을 전기영동한 결과, ${\alpha}$$_{s1}$-casein의 경우, calf rennet 단독처리구는 3개의 band로 분리되었고, 1:1혼합효소처리구(calf rennet :porcine pepsin)와 Porcine pepsin 단독처리구는 5개의 band로 분리되었으며, 대조구는 1개의 major band와 2개의 minor band를 나타내었다. ${\beta}$-casein은 porcine pepsin의 첨가비율이 증가할수록 그 농도는 감소하였고, ${\gamma}_1$ ${\gamma}_2$-casein으로 추정되는 band는 상대적으로 증가함을 나타내었다. 또한 para-${\kappa}$-casein은 대조구를 제외하고 calf rennet, porcine pepsin단독처리구, 1:1혼합효소처리구에서 분리되었다.

• Nutrition Research and Practice
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• 제7권1호
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• pp.3-8
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• 2013

Buckwheat is known as a health food but is one of the major food allergens triggering potentially fatal anaphylaxis in Asia, especially in Japan and Korea. This study was conducted to investigate the characteristic of enzymatic resistance of buckwheat protein and allergenic potential. Enzymatic resistance of buckwheat protein was performed with in vitro digestibility test in simulated gastric fluid (SGF), pH 1.2, using pepsin and simulated intestinal fluid (SIF) using chymotrypsin. Reactivity of buckwheat proteins to human IgE was performed using six allergic patients sensitized to buckwheat. Buckwheat's IgE levels were measured using the Phadia UniCAP-system. Buckwheat protein, 16 kDa, still remained after 30 min treatment of pepsin on SDS-PAGE. Even though 16 kDa almost disappeared after 60 min treatment, two out of the six buckwheat patients' sera showed reactivity to hydrolysate after 60 min treatment, indicating that allergenicity still remained. In simulated intestinal fluid (SIF) using chymotrypsin, buckwheat protein, 24 kDa, showed resistance to hydrolysis with chymotrypsin on SDS-PAGE, and still had allergenicity based on the result of ELISA. Our results suggest that buckwheat proteins have strong resistance to enzyme degradation. This may be attributed in part to the allergenic potential of buckwheat. Further study should be continued regarding buckwheat allergy.

• 한국축산식품학회지
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• 제34권2호
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• pp.151-157
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• 2014

This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates. Because placenta was made up of insoluble collagen, the placenta was gelatinized by applying thermal treatment at $90^{\circ}C$ for 1 h and used as the sample. The placental hydrolyzing activities of the enzymes at varying concentrations and incubation times were determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC). Based on the SDS-PAGE, the best placental hydrolysis efficiency was observed in trypsin treatments where all peptide bands disappeared after 1 h of incubation as compared to 6 h of chymotrypsin. Pepsin hardly hydrolyzed the placenta as compared to the other two enzymes. The Mw distribution revealed that the trypsin produced placental peptides with Mw of 106 and 500 Da. Peptides produced by chymotrypsin exhibited broad ranges of Mw distribution (1-20 kDa), while the pepsin treatment showed Mw greater than 7 kDa. For comparisons of pre-treatments, the subcritical water processing (37.5 MPa and $200^{\circ}C$) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment ($90^{\circ}C$ for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

• Asian-Australasian Journal of Animal Sciences
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• 제8권5호
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• pp.433-441
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• 1995

A series of experiments was conducted to determine the influence of various pepsin-HCL pretreatment factor, hereby the factors of duration of washing for the retrieved bags, inherent to the mobile nylon bag technique (MNBT), on apparent ileal digestibility of crude protein (AIDCP) and apparent ileal digestibility of dry matter (AIDDM). At last, the AIDCP and apparent ileal digestibility of amino acids (AIDAA) in maize, barley, wheat, rapeseed meal, cottonseed meal and three mixed diets were determined with the MNBT and ileo-rectal anastomis pigs (IRAT). For the MNBT techniques, bag measuring $25{\times}40$ MM and containing 0.75 g feedstuff samples, after pre-digestion in vitro, were introduced into the ileo-rectal anastomis pigs (IRAT) gastrointestinal tract through a duodenal cannula and recovered in the ileal digesta between 6 and 12 h. later. 1. The apparent ileal digestibility of dry matter (AIDDM) and crude protein (AIDCP) of the tested samples, with the exception of fish meal, determined by MNBT were not affected by the different pepsin-HCL pretreatment times in vitro between 2.5 h. and 4 h. 2. There was no significant (p > 0.05) difference of the AIDCP and AIDDM of maize determined by the MNBT among different pepsin concentration (0.03%, 0.07% and 0.1 %) treatment in vitro. 3. The AIDCP determined with the MNBT was affected by the washed and unwashed recovered bags from the ileal digesta. 4. The AIDCP and AID amino acids (AIDAA) of maize, barley, wheat, rapeseed meal, soya-bean meal, cottonseed meal and three mixed diets from the MNBT, with a solution of 0.01N HCL (PH 2) and 0.1% of pepsin concentration, a pepsin-HCL pretreatment time in vitro or 4h. and a washing time of the recovered bag from the ileal digesta compared well with those from the IRAT. The linear regression analysis showed a significant correlation (p < 0.01) of AIDCP and AIDDA between the IRAT and MNBT.

• 한국축산식품학회지
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• 제33권4호
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• pp.493-500
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• 2013

Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was $87.8{\mu}M$, whereas $14.5{\mu}M$ GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to $45.7{\mu}M$ of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.

• 대한수의학회지
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• 제15권2호
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• pp.223-231
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• 1975

In mammals there are two distinct cellular units of the gastric glands which are responsible for the secretion of acid and pepsin respectively, namely, the parietal cells for acid and the peptic or chief cells for pepsin. On the other hand, the bird does net have separate parietal and chief cells in the glandular stomach. There exist only a single cell type in the asian gastric secretory-glands. In spite of this single cell type, however, variation in pepsin and acid secretion can he seen. Present study was conducted to know distribution, secretion and formation of the pepsinogen granules in chicken and rat stomach which observing by light and electron microscope. 1. In chicken, the pepsinogen granules are distributed in all submucosal gland cells and yet there are no distinction of parietal and chief cells. In rat, the pepsinogen granules are distributed in chief cells which lined the lower two-thirds of the gastric tubles and the parietal cells occupy upper third of the tuble. 2. Carbachol markedly stimulates the secretion of pepsinogen granules in chiken and rat, but Histamine is slightly. 3. After Histamine and Carbachol treatment, the pepsinogen granules are formated continuously and reaccmulated as control after 3 to 4 hours.