• 대한화학회지
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• 제7권1호
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• pp.6-12
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• 1963

Amino acid composition of Makjang was determined by combined usage of ion exchanged resin and paper chormatography in the following states. a. A fraction soluble in water b. Hydrolysate of the whole Makjang c. Same as a. (p.p.t. formed by tungstic acid or trichloroacetic acid being removed) d. Hydrolysate of c. (T and TCA) By comparing amino acid composition of Makjang with that of its raw material, we found that decomposition of essential amino acids during brewing is slight. From the amino acid composition of a,b,c,d, we discussed the ratio of amino acid liberation during brewing and assumed that Makjang contains peptide-like substances composing of glutamic acid and aspartic acid.

• 한국어업기술학회:학술대회논문집
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• 한국어업기술학회 2001년도 추계 수산관련학회 공동학술대회발표요지집
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• pp.183-184
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• 2001

Angiotensin I converting enzyme (ACE) in renin-angiotensin system is a cause of essential hypertension, which covers most hypertension, one of the major adult diseases. Thus, the inhibition of ACE would be indispensable for the prevention and cure of hypertension. Therefore, a lot of studies on the ACE inhibitor have been conducted. Peptides from the protein hydrolysate have been reported as an remarkable inhibitor. Especially, various ACE inhibitory peptides were isolated and identified from marine products for their utilization as value added products. (omitted)

• 한국키틴키토산학회지
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• 제23권4호
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• pp.220-227
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• 2018

Amyloid plaque is a product of aggregation of ${\beta}$-amyloid peptide ($A{\beta}$) and is an important factor in the pathogenesis of Alzheimer's Disease (AD). $A{\beta}$ is a major component of amyloid plaque and vascular deposits in the AD brain. The enzyme ${\beta}$-secretase is required for the production of $A{\beta}$; thus, prevention of the formation of $A{\beta}$ through the inhibition of ${\beta}$-secretase is a major focus in the study of the treatment of AD. In this study, we investigated ${\beta}$-secretase inhibitory activity of an Arctoscopus japonicus peptide. An Alcalase hydrolysate had the highest ${\beta}$-secretase inhibitory activity. A ${\beta}$-secretase inhibitory activity peptide was separated using ion exchange column chromatography (carboxy-methyl: CM, quaternary methyl ammonium: QMA) and reverse phase high performance liquid chromatography (RP-HPLC) on a C18 column. The $IC_{50}$ value of the purified peptide was $248.2{\pm}1.73{\mu}g/mL$. The ${\beta}$-secretase inhibitory peptide was identified as a six amino acid residue of Gly-Pro-Val-Gly-Ala-Pro (MW: 497.27 Da). In cell viability experiments, the final purified fraction, the carboxy-methyl ion exchange column fraction (CM-F1) showed no significant cytotoxic effect in SH-SY5Y cells at concentrations below $100{\mu}g/mL$ in 24 h. The results of this study suggest that peptides separated from Arctoscopus japonicus may be beneficial as ${\beta}$-secretase inhibitor compounds in functional foods.

• 한국식품영양과학회지
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• 제42권11호
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• pp.1759-1766
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• 2013

본 연구는 오징어 간에 분포하는 효소를 활용한 은연어 육가수분해물 제조의 최적 조건과 생성된 가수분해물의 식품 및 생물 활성 특성을 조사하였다. 가열 처리한 은연어 육가수분해물 제조의 최적 조건은 가수분해 온도 $55^{\circ}C$, pH 5.5, 오징어 간의 첨가 비율 0.67%이었다. 총 구성 아미노산은 함량은 가열 및 산 처리 가수분해물에서 유의적인 차이를 보이지 않았으나, 총 유리 아미노산 함량은 조성은 산 처리가수분해물이 높았다. 한편 무기질 함량은 가열 처리 가수분해물이 높았다. Cd의 허용 기준을 고려할 때 가수분해물 제조 시 전처리 공정은 가열이 적합한 것으로 나타났다. 가열 처리한 가수분해물의 분자량은 1,000~9,500 Da이 40.0%, 500 Da이 6.7%, 200~250 Da은 12.6%, 그 이외 분자량 물질이 34.8%인 반면, 산 처리 가수분해물은 450~5,600 Da이 40.9%, 200~300 Da이 16.8%, 그 이외의 분자량이 42.3%에 해당하였다. 가수분해물은 $200{\mu}g/mL$의 농도에서 HepG2 세포에 대한 독성은 관측되지 않았다. 가수분해물의 잠재적인 적용 분야를 확인하기 위해 식품 및 건강 기능성에 대한 연구를 진행하고 있는 중이다.

• Fisheries and Aquatic Sciences
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• 제12권4호
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• pp.249-257
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• 2009

This study is conducted to partially purify an antioxidative peptide in a two-step gelatin hydrolysate from Alaska pollock surimi refiner discharge, which was obtained by sequential treatment with Pronase E and Flavourzyme. The two-step gelatin hydrolysate was fractionated using chromatographic methods. Based on the same protein concentration of each fraction, the antioxidative activities (85.1-95.4%) of positive fractions fractionated by ion-exchange chromatography were higher than those (27.2-87.8%) from gel filtration. Then, further purification of the positive fractions was performed. Among them, the partially purified A1C1L2G1 and A1C1L2G2 fractions showed 96.2% and 85.1% inhibition, respectively, of linoleic acid peroxidation. The A1C1L2G1 fraction was composed of 15 kinds of amino acids and the predominant amino acids were proline, glycine and alanine. The results obtained in this study suggested that the fraction partially purified through chromatographic methods from the two-step gelatin hydrolysate of Alaska pollock surimi refiner discharge could be useful as a supplementary source for improving health functionality.

• 한국축산식품학회지
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• 제30권4호
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• pp.575-581
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• 2010

This investigation was aimed at developing a ready-to-reconstitute beverage by utilizing probiotics and whey protein hydrolysates carrying bioactive peptides. Cheddar cheese whey was ultrafiltered. The 18% protein retentate was subjected to protein hydrolysis using Neutrase. The hydrolyzed retentate was further condensed to 35% total solids and spray-dried at $75^{\circ}C$ outlet air temperature. Different levels of sugar, citric acid and stabilizer were blended for spray-dried hydrolysates. Spray-dried hydrolysate was further inoculated with different levels of probiotics grown in a whey medium and dried in fluidized-bed drier at $40^{\circ}C$ to obtain a ready-to-reconstitute beverage. Hydrolysis was greatest at an enzyme:substrate ratio of 1:25 for 3 h. Spray-dried hydrolysate reconstituted to 1% protein and blended with 15% sugar, 0.2% citric acid and 0.15% xantham gum resulted in a superior product with no sedimentation. Accordingly, sugar, citric acid and xanthum gum were dry-blended with spray-dried hydrolysates. Bifidobacterium bifidum and Lactobacillus acidophilus that was grown separately in a whey medium, blended to produce 2% spray-dried hydrolysate and dried as described above resulted in a readyto-reconstitute beverage mix. The fluidized dried product typically exhibited a probiotic count of $10^8$colony forming units (CFU)/g. However, blending of probiotic to the retentate and direct spray-drying precipitously reduced the probiotic count to $10^4$ CFU/g of powder.

• 한국식품과학회지
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• 제50권2호
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• pp.203-208
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• 2018

본 연구에서는 항염증 펩타이드를 생산하기 위해 도루묵(Arctoscopus japonicus)의 어육과 알로부터 가수분해물을 제조하였으며, 단백분해효소, pH, 온도, 효소 농도 및 가수분해 시간에 따른 NO 소거활성을 측정함으로써 최적 가수분해 조건을 설정하였다. 어육 가수분해물의 최적 조건은 pH 5.0, 온도 $30^{\circ}C$, 효소 농도 1%, 가수분해 시간 4시간으로 확인되었으며, 알 가수분해물의 최적 조건은 pH 5.0, 온도 $70^{\circ}C$, 효소 농도 3%, 가수분해 시간 3시간으로 확인되었다. 이러한 최적의 가수분해 조건에서 어육 및 알 가수분해물의 NO 소거활성은 각각 18.94 및 19.81%로 측정되었다. 이는 도루묵 단백질 가수분해물 유래 항염증 펩타이드를 생산하기 위한 기초자료로 활용할 수 있을 것으로 기대된다.

• KSBB Journal
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• 제29권5호
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• pp.380-384
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• 2014

Inhibition effects of peptide hydrolysates from Astragalus membranaceus Bunge. on the expression of the matrix metalloproteinases (MMPs) in human dermal fibroblasts were evaluated in vitro. Crude peptides were obtained by the hydrolysis of proteins extracted from A. membranaceus. Peptides were purified partially by the basis on the molecular weight using 40% polyacrylamide gel electrophoresis before treatment with human dermal fibroblasts. Basis on the doseeffect experiments, expressions of MMPs including MMP-1, MMP-3, MMP-8, MMP-13 in human dermal fibroblasts were evaluated. Expressions of MMP-1, MMP-3, MMP-8 and MMP-13 were reduced in 43%, 5%, 22% and 57% respectively. The mass spectrometric analysis of partially purified peptides from A. membranaceus, which strongly inhibit expressions of MMPs, indicated that the peptides were composed of molecules below 1500 Da.

• 한국식품영양과학회지
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• 제42권7호
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• pp.1162-1166
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• 2013

해바라기씨박 단백질 가수분해물로부터 철분 결합 펩타이드를 분리하기 위해 해바라기씨박 단백질을 단백 가수분해 효소인 alcalase와 flavourzyme을 이용하여 가수분해하였고, 가수분해물을 3 kDa 이하로 한외여과를 하였다. 한외여과된 가수분해물은 QAE Sephadex$^{TM}$ A-25 column과 Superdex$^{TM}$ peptide 10/300 GL column을 사용하여 철분 결합 펩타이드를 분리하였고, 분리된 분획 중 철분 결합력이 가장 높은 F22를 얻었다. 본 연구에서 얻어진 해바라기씨박 단백질 가수분해물로부터 분리된 분획들은 향후 기능성식품 소재 원료로 사용될 수 있다고 판단된다.

• Fisheries and Aquatic Sciences
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• 제19권2호
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• pp.11.1-11.7
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• 2016

In this study, purified peptides from shrimp waste hydrolysates (SWHs) were examined for their inhibitory effects against ${\beta}$-secretase. During consecutive purification using a Sephadex G-25 column chromatography and high performance liquid chromatography on a C18 column, a potent ${\beta}$-secretase inhibitory peptide Asp-Val-Leu-Phe-His (629 Da) was isolated and identified from SWH24 by Q-TOF MS/MS and the $IC_{50}$ value was determined to be $92.70{\mu}M$. The ${\beta}$-secretase inhibition patterns of the purified peptides were found to be competitive. Among synthesized ${\beta}$-secretase inhibitory peptides, Leu-Phe-His had higher ${\beta}$-secretase inhibitory activity than the others. The result of this study suggests that the ${\beta}$-secretase inhibitory peptide derived from SWH24 could be potential candidates to develop nutraceuticals and pharmaceuticals.