• Title/Summary/Keyword: 가수분해물

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Stimulation of Nitric Oxide Production in RAW 264.7 Macrophages by the Peptides Derived from Silk Fibroin. (실크 피브로인 유래 펩타이드에 의한 RAW 264.7 Macrophage의 Nitric Oxide 생성 촉진)

  • 박금주;현창기
    • Microbiology and Biotechnology Letters
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    • v.30 no.1
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    • pp.39-45
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    • 2002
  • It was found that the peptides originated from the hydrolysates of silk fibroin have in vitro immunostimulating effects in murine macrophage RAW264.7 cells. The stimulation effects on nitric oxide (NO) production resulted from treatments of acid or enzymatic hydrolysates were measured. The silk fibroin preparation isolated from cocoon was most efficiently digested by acid hydrolysis. Even though the sole treatment of acid hydrolysate stimulated the NO production in dose-dependent pattern, a part of its activity was found to be caused by the contaminated endotoxin, LPS. When each endotoxin-free hydrolysates obtained by filtering it through an ultrafiltration membrane of molecular weight (MW) cut-off 10,000 to eliminate LPS was used, the peptic hydrolysate with lowest degree of hydrolysis showed the highest activity. The fractions of peptic hydrolysate with MW ranges of 1,000∼10,000, 500∼1,000 and below 500 also showed a higher MW-higher activity correlation. From the analyses of amino acid composition of each hydrolysate, it was found that the contents of arginine, lysine, alanine and glycine residues affected the activity level of hydrolysate. The results of this study showed a possibility of utilizing fibroin as a source for immunostimulating (chemopreventive) functional peptides.

한우 등심과 우둔에서 추출한 Myosin B를 pepsin으로 가수분해한 단백질의 변화와 Angiotensin converting enzyme(ACE) 저해 효과

  • Kim, Yeong-Ju;Choe, Dam-Mi;Jin, Gu-Bok
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.05a
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    • pp.226-230
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    • 2005
  • 본 연구는 고혈압을 억제하는 ACE inhibitory peptide가 한우에 함유되어 있는지를 조사하기 위한 기초연구로 한우의 우둔과 등심으로부터 Myosin B를 추출하여 가열한 것과 가열하지 않은 것으로 구분하여 pepsin으로 0, 1, 3, 6시간 동안 $37^{\circ}C$에서 가수분해 시켰다. 가수분해물을 전기영동을 실시하여 pepsin 처리시간에 따른 단백질의 변화를 검토하였고, ACE 저해 활성을 측정하였다. 전기영동의 결과 가열한 것은 가열하지 않은 것에 비해서 단백질의 변성과 소멸이 많이 일어나 밴드의 수가 적었다. Pepsin으로 가수분해한 시간이 길어짐에 일부 단백질이 소실되었고, 저분자의 단백질이 생성되었다. Pepsin으로 가수분해함에 따라 등심과 우둔에서 25, 32, 40 및 44 kDa는 소실되었고, 37 kDa의 분자량을 갖는 밴드는 생성되었으며, 27 kDa의 단백질은 처음상태 그대로 유지되었다. 가수분해물을 이용하여 ACE 저해활성도를 측정한 결과, 등심은 1시간 가수분해시 유의차가 있었으나, 우둔은 가열여부에 따라 유의차가 발견되지 않았다. 반면 등심과 우둔 모두 가수분해 시간이 증가하면 ACE 저해율은 상승하는 경향을 보였다. 이와 같은 결과를 토대로 한우로부터 추출한 Myosin B의 ACE 억제활성이 우수한 단백질분획을 찾아 아미노산 염기서열을 밝히고 고혈압 억제제로 합성 개발하는 연구를 차후 추진할 예정이다.

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Hydrolysis of Aluminum Nitride Powder (AlN 분말의 가수분해 특성)

  • 최상욱;정홍식;황진명
    • Journal of the Korean Ceramic Society
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    • v.31 no.1
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    • pp.79-87
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    • 1994
  • Aluminum nitride was hydrolyzed in contact with water, evolving the reaction heat of 172 cal/g within 12 hours to form alumina trihydrates. At 4$0^{\circ}C$ >, amorphous alumina hydrate was easily produced by the spontaneous breaks of AlN particle at the beginning of the hydrolysis process, while bayerite was formed by the dissolution-recrystallization processes of amorphous alumina hydrate at the temperature between 4$0^{\circ}C$ and 6$0^{\circ}C$, and pseudo-boehmite was generated on the surface of AlN particle by the condensation process of the corresponding phase at 6$0^{\circ}C$ <. The longer the hydrolysis timje or the higher the value of pH in solution, the more the bayerite phase was produced. However, pseudo-boehmite was easily generated under the following favorable conditions; when the hydrolysis reaction occured rapidly at the beginning and when the absorption of OH radical on the surface of AlN particle was disturbed by ethyl alcohol in a solution. However, aluminum nitride was hardly hydrolyzed in a solution of pH 2.0.

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Isolation of Iron and Calcium-Binding Peptides from Cottonseed Meal Protein Hydrolysates (면실박 단백질로부터 가수분해물 제조 및 철분, 칼슘 결합 펩타이드의 분리)

  • Choi, Dong-Won;Kim, Nam-Ho;Song, Kyung Bin
    • Journal of Applied Biological Chemistry
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    • v.55 no.4
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    • pp.263-266
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    • 2012
  • Isolation of iron and calcium-binding peptides derived from cottonseed meal protein (CMP) hydrolysates was investigated. The degree of hydrolysis of CMP by Flavourzyme was monitored using trinitrobenzenesulfonic acid method and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymatic hydrolysis of CMP for 12 h was sufficient for the preparation of CMP hydrolysates, and the hydrolysates were membrane-filtered under 3 kDa as a molecular weight. The filtered solution was fractionated using Q-Sepharose fast flow, Sephadex G-15, and reversed phase-high performance liquid chromatography for iron and calcium-binding peptides. As a result, F51 fraction was obtained as the best candidate for calcium and iron chelation, and the isolated iron and calcium-binding peptides can be used as functional food additives, similar to iron and calcium supplements.

Development of Alginic Acid Hydrolysate as a Natural Food Preservative for Fish Meat Paste Products (알긴산 가수분해물을 이용한 어육연제품용 천연 식품보존료의 개발)

  • Chang, Dong-Suck;Cho, Hak-Rae;Lee, Hyun-Sook;Park, Mi-Yeon;Lim, Sung-Mee
    • Korean Journal of Food Science and Technology
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    • v.30 no.4
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    • pp.823-826
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    • 1998
  • It has been reported that alginic acid hydrolysate retains antimicrobial activity but the enzyme which hydrolyze alginic acid is not developed for industrial use. The authors developed chemical method for hydrolyzing alginic acid. For preparing alginic acid hydrolysate, equal quantity of alginic acid and ascorbic acid were added to water. Then the solution was heated at $121^{\circ}C$ for $20{\sim}30{\;}minutes$. The 4% solution of alginic acid hydrolysate was revealed relative viscosity 1.05, pH 3.2 and opaque whitish-yellow color. By addition of this hydrolysate to nutrient broth with the concentration of 0.1%, the growth of Bacillus sp. isolated from fish meat paste products was inhibited. The fish meat paste products containing 0.3% alginic acid hydrolysate prepared were prolonged their shelf life by 1 day stored at $30^{\circ}C$, 2 days at $20^{\circ}C$ and 4 days at $15^{\circ}C$.

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Angiotensin I Converting Enzyme Inhibitory Activity of Hot-Water Extract and Enzymatic Hydrolysate of Fresh Water Fish (담수어 열수추출물 및 효소가수분해물의 Angiotensin I 전환효소 저해작용)

  • 김태진;윤호동;이두석;장영순;서상복;염동민
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.25 no.5
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    • pp.871-877
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    • 1996
  • Hot-water extract and enzymatic hydrolysate prepared from fresh water fish such as carp, snakehead, eel and israeli cart were tested for inhibitory activity against Angiotensin I converting enzyme(ACE). ACE inhibitory activity of enzymatic hydrolysate was higher than that of hot-water extract, and was the highest in enzymatic hydrolysate of carp among the tested samples. ACE inhibitory activity of 70% ethanol soluble fraction was higher than that of precipitated fraction, the highest in enzymatic hydrolysate of carp. Molecular weight of active fraction was about 1,400 in hot-water extract and slightly above in enzymatic hydrolysate. Amino acid of active fraction of hot-water extract was abundant in glycine, alanine, leucine and proline, whereas amino acids of aspartic acid, glutamic acid, glycine, alanine, valine, leucine and proline were abundant in enzymatic hydrolysate. $IC_{50}$/(amounts of inhibitors need for 50% inhibition) of hot-water extract was the range of 50.3~56.9$\mu\textrm{g}$, those of enzymatic hydrolysate 42.6~57.7$\mu\textrm{g}$.

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Antioxidant Activities in Enzymatic Hydrolysates of Pumpkin Powder (Cucurbita spp.) (호박분말 효소가수분해물의 항산화활성)

  • Oh, Chang-Kyung;Kim, Myeong-Cheol;Oh, Myung-Cheol;Yang, Tai-Suk;Hyun, Jae-Suk;Kim, Soo-Hyun
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.2
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    • pp.172-178
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    • 2010
  • This study was conducted to investigate total polyphenol contents and antioxidative effects of the enzymatic hydrolysates digested by several kinds of carbohydrases from the powder of ripened pumpkin (Cucurbita moschata), sweet pumpkin (C. maxima) and green pumpkin (C. moschata). The total polyphenol contents of all enzymatic hydrolysates from green pumpkin powder were higher than those of ripened and sweet pumpkins. DPPH radical scavenging activities of the enzymatic hydrolysates digested by AMG and Termamyl from green pumpkin were also very strong compared to ripened and sweet pumpkins. However, the most enzymatic hydrolysates of ripened and sweet pumpkin powders, except Viscozyme digestion, were higher superoxide anion scavenging activities than green pumpkin powder. Hydrogen peroxide scavenging activities in the enzymatic digests (not Ultroflo) of green pumpkin were potent compared to other pumpkin powders whereas hydroxyl radical scavenging activities were low at less than 14% in hydrolysates of all pumpkin species. Nitric oxide scavenging activities were very effective in Viscozyme digests of sweet and green pumpkin, and other enzymatic hydrolysates also showed higher activity than $\alpha$-tocopherol control (not BHT).

한우에서 추출한 Myosin B의 Pepsin 가수분해물의 Ultrafilteration에 의한 Angiotensin Converting Enzyme(ACE) 저해 활성 분석

  • Kim, Yeong-Ju;Choe, Dam-Mi;Jin, Gu-Bok
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.10a
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    • pp.168-171
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    • 2005
  • 한우의 Myosin B 단백질을 단백질 가수분해 효소인 pepsin으로 처리한 다음 단백질의 함량과 혈압상승 펩티드 생성효소인 angiotensin-I converting enzyme(ACE)에 대한 저해활성을 측정하였다. 등심이 우둔에 비해 단백질의 함량이 높았으며, 가수분해 처리 후 우둔과 다르게 등심은 3시간 가수분해 처리구에서 단백질의 함량이 높게 나타났다. ACE 저해활성은 등심에서는 3시간, 우둔에서는 6시간동안 가수분해시켰을 때 ACE 저해율이 유의적으로 가장 높게 나타났으며, 3, 6시간동안 가수분해시켰을 경우 부위 별로 유의적인 차가 있었으나(p<0.05), 0, 1시간동안 가수분해 시켰을 때는 부위간의 유의적인 차는 없었다(p>0.05). ACE 저해율이 가장 좋은 가수분해 처리구를 ultrafiltration시킨 결과, 저분자 peptide 상태의 가수분해물이 고분자에 비하여 ACE 저해율이 높은 것으로 나타났다. 차후 ACE 억제활성도가 높은 단백질을 분리하여 가장 우수한 분획을 찾아 아미노산 염기서열을 밝혀 고혈압 억제제로 합성 개발하는 연구를 추진할 예정이다.

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Response of hydrolyzed polyacrylonitrile fibers to pH (가수분해 폴리아크릴로니트릴 섬유의 pH 응답성)

  • 우종형;서영삼;윤기종;조재환;정재윤
    • Proceedings of the Korean Fiber Society Conference
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    • 2003.04a
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    • pp.345-346
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    • 2003
  • 폴리아크릴로니트릴을 NaOH로 가수분해시키면 carboxylate anion과 carboxamide기가 생성되며, 물을 흡수할 경우 sodium carboxylate기의 해리로 팽윤이 크게 일어나므로 고흡수성을 지니게 된다[l]. 일반적으로 섬유가 팽윤을 하면 수축하며, 가수분해된 폴리아크릴로니트릴 섬유는 흡수되는 물 속의 염의 농도 또는 pH에 따라 팽윤도가 다르기 때문에 가수분해된 시간과 pH조건 변화에 따라서 수축하는 정도가 다르다. 과거의 연구결과에 의하면 아크릴 섬유는 2M HCI에서 최소의 길이로 수축하며, 2M NaOH에서 최대의 길이가 나타난다고 하였다[2]. (중략)

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Antioxidant, Anti-inflammatory and Anti-photoaging Activities of Hydrolyzed Peony (Paeonia lactiflora Pall.) Flower (작약꽃 가수분해물의 항산화, 항염 및 광노화 억제 효능)

  • Kyung Ju Lee;You Ah Kim;Byoung Jun Park
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.49 no.3
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    • pp.259-267
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    • 2023
  • This study was conducted to evaluate physiological activity of flower extract of peony (Paeonia lactiflora Pall.) by hydrolysis and to use it as a valuable cosmetic ingredients. Four cultivar of peony flowers were extracted, and the highest active ingredient contents was selected, and that cultivar was used for hydrolyzing. The results showed that high concentration of hydrochloric acid (HCl) hydrolyzed, and biological hydrolysis using enzymes had no activity. The deglycosylation of peonidin 3,5-diglucoside occurred by hydrolysis. The hydrolysate contains 63.3 ppm of peonidin, a red-colored anthocyanin compound. The antioxidant activity of hydrolysate was compared with extract. The results showed the strong antioxidant activity in hydrolysate (96%) than extract (82%). In addition, hydrolysate of peony flower showed higher inhibitory activity of NO release than extract. UVA assay using fibroblast cell (CCD-986Sk) showed that hydrolysate increased cell viability than extract under UVA exposure. Based on these results, we anticipate that hydrolysate of peony flower can be used a valuable cosmetic ingredient.