• 대한화장품학회지
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• 제30권1호
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• pp.73-77
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• 2004

셀레늄을 함유하는 펩타이드(셀레늄 펩타이드)는 셀레늄을 함유하는 배지에서 효모를 배양함으로써 생산 하였다. 효모 단백질의 GPC 분석을 통해서 다양한 크기의 단백질 내 셀레늄 분포를 조사한 결과 셀레늄이 효모 내 단백질에 균일하게 분포하는 것을 확인하였다. 단백질당 셀레늄 양은 배지에 첨가한 셀레늄 양이 증가함에 따라 증가하였고 펩타이드 내의 셀레늄 함량이 높아질수측 항산화 효과 (glutathione peroxidase 유사 활성)가 증가하였다. 단백질 가수분해효소 XIV를 이용하여 여러 분자량의 펩타이드를 생산하였으며 평균 분자량을 GPC로 분석하였다 셀레늄 펩타이드의 glutathione peroxidase (GPx) 활성은 펩타이드의 분자량이 감소할수록 증가하였다. Sodium selenate은 sodium selenite에 비해 효모의 성장 저해를 적게 받았고 단백질 내 셀레늄 함량이 sodium selenite보다 높았다. 이 결과는 효모 배양에 의한 셀레늄 펩타이드의 생산의 가능성과 이를 이용한 항산화 제로서의 응용가능성을 보여주었다.

• KSBB Journal
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• 제24권5호
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• pp.463-468
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• 2009

셀레늄 함유 펩타이드 (셀레늄 펩타이드)는 무기 셀레늄이 포함된 배지에서 효모를 배양하여 효모의 자가분해에 의해 만들었다. 효모 배양에 의해 만들어진 셀레늄 펩타이드는 GPx 유사활성을 보였으며, UVB 조사가 된 인간 섬유아세포에 대하여 세포 보호효과를 나타냈다. 셀레늄 나이트레이트는 $10^{-9}$ 몰 농도에서 낮은 세포독성을 보인반면 셀레늄 펩타이드는 최소의 독성만을 보였다. 또한 셀레늄 펩타이드는 인간 섬유아세포의 성장과 procollagen type I을 증가시킨 반면 MMP-1의 감소를 가져왔다. 연구결과 셀레늄 펩타이드가 무독성의 항산화제로서의 가능성을 보여주었다.

• 한국응용과학기술학회지
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• 제26권4호
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• pp.457-466
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• 2009

This study is manufacturing method and analysis of feasibility about collagen peptide from fish scale. This is processed by enzyme hydrolysis, isolating and refining etc. The results of analysis of nutritional composition showed protein content of collagen peptide. In the analysis of constitutive amino acids, the ratio of contents of hydroxyproline and glycine, the characteristics of collagen peptides appeared similar and the contents of glutamic acid and aspartic acid which are involved in protein metabolism. As a result of measurement of total polyphenol content and total flavonoid, it showed that collagen peptide had more contents generally, and the effect of bioactivity of pig-skin collagen peptide appeared higher although different kinds of scale collagen peptide showed a little DPPH radical scavenging ability, total antioxidant capacity by ABTS, ACE inhibitory.

• 한국축산식품학회지
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• 제34권3호
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• pp.325-332
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• 2014

The antioxidant capacity of porcine splenic hydrolysate (PSH) was studied in vitro and in vivo. Peptide hydrolysates were prepared, using the proteolytic enzyme $Alcalase^{(R)}$. The molecular weights of PSH were 37,666, 10,673, 6,029, and 2,918 g/mol. Rats were fed a 5% (w/v) PSH diet, instead of a casein diet, for 4 wk. The food intake, body weight gain, and liver weight of rats in the PSH group were similar to those in the control (CONT) group. There were no differences in the serum total cholesterol, triglyceride, total protein, or albumin levels between PSH and CONT groups. However, the level of in vivo hepatic lipid peroxidation in PSH group was significantly lower than that in CONT. In vivo hepatic catalase and glutathione peroxidase activities in the PSH group were significantly higher than those in the control group. The in vitro protein digestibility of PSH was lower than that of casein. The in vitro trolox equivalent antioxidant capacity of PSH was significantly higher than that of the peptide hydrolysate from casein. The in vitro radical scavenging activities of PSH were significantly higher than those of the peptide hydrolysate from casein. The present findings suggest that porcine splenic peptides improve the antioxidant status in rats by enhancing hepatic catalase and GSH-Px activities, and indicate a potential mechanism of radical scavenging activity during gastrointestinal passage.

• 한국작물학회지
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• 제56권4호
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• pp.349-360
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• 2011

The objectives of present study were to characterize the peptides which were isolated from Korean fermented soybean paste, chungkukjang, and to determine their antioxidant activities. Four fractions were collected from the methanol extract of chungkukjang by using a recycling preparative HPLC. Among fractions, Fr-2 was identified to be highly potent free radical scavenging activity in the assay of 1,1-diphenyl-2-picryl-hydrazyl (DPPH) and nitroblue tetrazolium(NBT)-reduction inhibition. Base on antioxidant effects, fraction Fr-2 was employed for the refraction with a prep-column and separated into five fractions of which two fractions were identified to have higher antioxidant activity. To confirm the amino acid constituents of antioxidant fractions Fr-2-2 and Fr-2-3 were analyzed, and eight kinds of amino acids such as aspartic acid, threonine, serine, glutamic acid, glycine, lysine, histidine, and arginine were identified as the constituent amino acids. Antioxidant activities of the separated peptides were further assessed cell viability with 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl terazolium bromide (MTT), and fluorescence-activated cell sorting (FACS) analysis of H4IIE cells treated with hydrogen peroxide (H2O2). Chungkukjang peptides have shown their ability to protect H4IIE rat hepatoma cells against H2O2- induced oxidative stress by concentration and time-dependent manner. Therefore, These results indicated that fermented soybean paste chungkukjang will be promoted the antioxidant and radical scavenging activities, and beneficial for health. The antioxidant peptide fractions Fr-2-2 and Fr-2-3 were denominated as P-NICS-1 and P-NICS-2, respectively. However, further studies were required to clarify their amino acid sequences and molecular properties, and physiological significances.

• 한국축산식품학회지
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• 제34권6호
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• pp.769-776
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• 2014

The goat placenta was fermented by Bacillus subtilis and the optimal fermentation parameters of strongest antioxidant capacity of peptides were obtained using response surface methodology (RSM). The effects of fermentation time, initial pH value and glucose content on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity of the goat peptides were well fitted to a quadric equation with high determination coefficients. According to the data analysis of design expert, the strongest DPPH radical scavenging capacity value was obtained with the following conditions: content of glucose was 2.23%, initial pH value was 7.00 and fermentation time was 32.15 h. The DPPH radical scavenging capacity commonly referring antioxidant activity showed a concentration dependency and increased with increasing peptide concentration. The effects of temperature and pH were assessed to determine the stability of antioxidant peptides prepared from goat placenta. Antioxidant peptides showed good stabilities when temperature was lower than $70^{\circ}C$. However, the antioxidant peptides lost antioxidant activities rapidly under alkaline and excessive acid condition. Ultrafiltration technique was performed to separate fermentation broth with different Mw (molecular weight). It was found that peptides in the range of < 3 KDa mainly accounted for the antioxidant activities.

• 한국축산식품학회지
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• 제37권5호
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• pp.752-763
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• 2017

Marine fish skin peptides (FSP) have been widely studied due to their antioxidant and antimicrobial properties. We aimed to use a natural antioxidant, FSP, to replacing synthetic preservatives in a pork patty model, which is safer for human body. Moreover, nano-liposome technology can be applied for masking the fishy smell and improving the stability of this peptide. Therefore, in this study, the effects of FSP and FSP-loaded liposomes (FSPL) on pork patty were evaluated through the tests of thiobarbituric acid reactive substances (TBARS), color, cooking loss, texture, volatile basic nitrogen (VBN), and the pH value, during 14 d of refrigerated ($4^{\circ}C$) storage. The results showed that all FSP-treated patties had lower TBARS values than control patties, which indicated an inhibitory effect of FSP on lipid oxidation. This effect in the patties depended on the FSP concentration. However, FSPL-treated patties showed significantly higher and undesirable TBARS values compared to the control, and this effect depended on the FSPL concentration. None of the physicochemical results showed remarkable changes except the pH and VBN values. Therefore, this study provides evidence that FSP has great potential to inhibit the lipid oxidation of pork patties and is capable of maintaining the quality and extending the shelf life. However, it is necessary to study the application of FSP treatments greater than 3% to improve the antioxidant effect on pork patties and search for other coating materials and technology to reduce the drawbacks of FSP.

• 한국축산식품학회지
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• 제35권3호
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• pp.360-369
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• 2015

Milk proteins have many potential sequences within their primary structure, each with a specific biological activity. In this study, we compared and investigated the bioactivities of hydrolysates of the domestic (A, B) and imported (C, D) skim milk powders generated using papain digestion. MALDI-TOF analysis revealed that all milk powder proteins were intact, indicating no autolysis. Electrophoretic analysis of hydrolysates showed papain treatment caused degradation of milk proteins into peptides of various size. The antioxidant activity of the hydrolysates, determined using 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and total phenolic contents (TPC) assays, increased with incubation times. In all skim milk powders, the antioxidant activities of hydrolysates were highest following 24 h papain treatment (TPC: A, 196.48 μM GE/L; B, 194.52 μM GE/L; C, 194.76 μM GE/L; D, 163.75 μM GE/L; ABTS: A, 75%; B, 72%; C, 72%; D, 57%). The number of peptide derived from skim milk powders, as determined by LC-MS/MS, was 308 for A, 283 for B, 208 for C, and 135 for D. Hydrolysate A had the highest antioxidant activity and the most potential antioxidant peptides amongst the four skim milk powder hydrolysates. A total of 4 β-lactoglobulin, 4 α_s1-casein, and 56 β-casein peptide fragments were identified as potential antioxidant peptides in hydrolysate A by LC-MS/MS. These results suggest that domestic skim milk could have applications in various industries, i.e., in the development of functional foods.

• 한국축산식품학회지
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• 제29권5호
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• pp.633-639
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• 2009

본 연구는 유단백질에 단백질 분해효소를 처리하여 가수분해 후 저분자 peptide를 ABTS법을 이용하여 항산화 활성을 측정하여 유단백질 유래 저분자 peptide의 항산화력을 측정하고자 하였다. Chymotrypsin 처리한 유청단백질의 가수분해도가 가장 높았으며, 유청단백질의 락트알부민 및 락토글로브린이 분해되어 분자량 20 kDa 이하의 저분자 단백질이 생성된 것을 전기영동을 통하여 확인하였다. 유단백질의 농도에 따른 항산화 활성을 측정한 결과, 카제인의 항산화 활성이 유청단백질보다 높게 나타났다. 유단백질을 효소에 의하여 가수분해 시 항산화 활성이 증가하였으며, 카제인 가수분해물이 유청단백질 가수분해물과 비교하여 항산화 활성이 더 높았으나, 가수분해도와 항산화 활성도의 관계는 일치하지 않았다. Trypsin에 의한 카제인 가수분해 물의 항산화 활성이 80.7%로 가장 높았다. 본 연구에서는 chymotrypsin과 trypsin에 의한 분자량 3 kDa의 카제인 분획물의 항산화 활성이 가장 우수 하였으며, 유청단백질을 trypsin으로 분해하였을 때 항산화 활성이 증가하였다.

• Fisheries and Aquatic Sciences
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• 제22권5호
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• pp.10.1-10.14
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• 2019

Fish skin waste accounts for part of the solid waste generated from seafood processing. Utilization of fish skin by bioconversion into high-grade products would potentially reduce pollution and economic cost associated with treating fish processing waste. Fish skin is an abundant supply of gelatin and collagen which can be hydrolyzed to produce bioactive peptides of 2-20 amino acid sequences. Bioactivity of peptides purified from fish skin includes a range of activities such as antihypertensive, anti-oxidative, antimicrobial, neuroprotection, antihyperglycemic, and anti-aging. Fish skin acts as a physical barrier and chemical barrier through antimicrobial peptide innate immune action and other functional peptides. Small peptides have been demonstrated to possess biological activities which are based on their amino acid composition and sequence. Fish skin-derived peptides contain a high content of hydrophobic amino acids which contribute to the antioxidant and angiotensin-converting enzyme inhibitory activity. The peptide-specific composition and sequence discussed in this review can be potentially utilized in the development of pharmaceutical and nutraceutical products.