• 제목/요약/키워드: peptic hydrolysate

검색결과 18건 처리시간 0.021초

광어껍질을 활용한 펩신가수분해물 제조공정 최적화와 피부건강 기능성 (Optimal Processing for Peptic Hydrolysate from Flounder Skin and Its Skincare Function)

  • 강유안;진상근;고종현;최영준
    • 한국해양바이오학회지
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    • 제14권1호
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    • pp.9-24
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    • 2022
  • Low-molecular weight peptides derived from fish collagen exhibit several bioactivities, including antioxidant, antiwrinkle, antimicrobial, antidiabetic, and antihypertension effects. These peptides are also involved in triglyceride suppression and memory improvement. This study aimed to investigate the optimal processing condition for preparing low-molecular weight peptides from flounder skin, and the properties of the hydrolysate. The optimal processing conditions for peptic hydrolysis were as follows: a ratio of pepsin to dried skin powder of 2% (w/w), pH of 2.0, and a temperature of 50℃. Peptic hydrolysate contains several low-molecular weight peptides below 300 Da. Gly-Pro-Hyp(GPHyp) peptide, a process control index, was detected only in peptic hydrolysate on matrix-assisted laser desorption/ionization-time-of-flight(MALDI-TOF) spectrum. 2,2'-azinobis-(3-3-ethylbenzothiazolline-6- sulfonic acid(ABTS) radical scavenging activity of the peptic hydrolysate was comparable to that of 1 mM ascorbic acid, which was used as a positive control at pH 5.5, whereas collagenase inhibition was five times higher with the peptic hydrolysate than with 1 mM ascorbic acid at pH 7.5. However, the tyrosinase inhibition ability of the peptic hydrolysate was lower than that of arbutin, which was used as a positive control. The antibacterial effect of the peptic hydrolysate against Propionibacterium acne was not observed. These results suggest that the peptic hydrolysate derived from a flounder skin is a promising antiwrinkle agent that can be used in various food and cosmetic products to prevent wrinkles caused by ultraviolet radiations.

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

  • Kim, Sung-Rae;Byun, Hee-Guk
    • Fisheries and Aquatic Sciences
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    • 제15권3호
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    • pp.183-190
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    • 2012
  • The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

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

  • 박금주;현창기
    • 한국미생물·생명공학회지
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    • 제30권1호
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    • pp.39-45
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    • 2002
  • 실크 피브로인의 가수분해를 통해 생산된 펩타이드 성분에 의해 murine macrophage RAW264.7 세포에 의한 nitric oxide 생성이 촉진됨을 발견하였다. 산 및 효소적 가수분해물의 가수분해도를 비교한 결과 실크 피브로인 단백질은 산 가수분해에 의해 가장 효과적으로 분해되었으며 효소적 가수분해의 경우에는 pepsin, trypsin, Alcalase의 순으로 가수분해도가 높았다. 산 가수분해물을 단독으로 macrophage에 처리하였을 때 처리농도에 따라 NO 생성촉진활성이 높아졌으나 이 활성은 가수분해물 내의 펩타이드 성분들과 오염되어 혼재하는 LPS 성분의 상호작용에 의한 것임이 확인되었다. 함유된 LPS 성분들을 한외여과에 의해 제거한 효소적 가수분해물들의 NO 생성촉진활성은 peptic hydrolysate가 가장 높았고 tryptic-, Alcalase hydrolysate 순이었다. 이러한 활성의 차이는 가수분해물 내의 고분자량 펩타이드 분포가 많을수록 활성이 높다는 관계에 기인하였으나 산 가수분해물의 경우에는 예외적으로 나타났다. 각 가수분해물의 아미노산 조성을 분석한 결과 arginine, lysine의 함량이 높을수록 활성이 높으며 alanine의 glycine에 대한 비율이 커질수록 활성이 높아졌다. 산 가수분해물의 경우에는 낮은 분자량의 펩타이드들이 많이 분포하지만 arginine 및 alanine의 함량이 높아 비교적 높은 NO 생성 촉진활성을 나타내는 것으로 확인되었다.

Angiotensin I-converting Enzyme Inhibitory Activities of Porcine Skeletal Muscle Proteins Following Enzyme Digestion

  • Katayama, K.;Fuchu, H.;Sakata, A.;Kawahara, S.;Yamauchi, K.;Kawamura, Y.;Muguruma, M.
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권3호
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    • pp.417-424
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    • 2003
  • Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

해바라기씨 단백질에서 plastein의 합성 (Plastein formation from sunflower seed protein)

  • 노재문;김재욱
    • Applied Biological Chemistry
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    • 제34권1호
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    • pp.1-7
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    • 1991
  • 해바라기씨 단백질에서 plastein을 합성 이용하기 위해 먼저 해바라기씨를 pepsin을 이용해 가수분해하는 최적 조건과, plastein을 합성하는 최적 조건을 구하였다. 최적 가수분해 조건은 pH 1.5, $45^{\circ}C$, 2% 기질농도와 2% pepsin 농도에서 24시간 반응시키는 것이었고 plastein 합성의 최적조건은 기질농도 50%, pH 4.5, $50^{\circ}C$, 0.25% pepsin 농도에서 18시간 반응시키는 것이었다. Plastein의 생성을 확인하기 위해 thin layer chromatography를 실시한 결과 해바라기씨 농축가수분해물의 TLC pattern과 plastein의 TLC pattern이 하나의 spot를 제외하고는 다르게 나타났는데 이는 plastein과 기질이 다른 것임을 표시하는 것이었다.

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Peptic Hydrolysate of Porcine Crude Myosin Has Many Active Fractions Inhibiting Angiotensin I-converting Enzyme

  • Katayama, Kazunori;Fuchu, Hidetaka;Sugiyama, Masaaki;Kawahara, Satoshi;Yamauchi, Kiyoshi;Kawamura, Yukio;Muguruma, Michio
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권9호
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    • pp.1384-1389
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    • 2003
  • In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.

Characterization of an antioxidant peptide from katsuobushi (dried bonito) protein hydrolysates

  • Lee, Jung Kwon;Jeon, Joong-Kyun;Byun, Hee-Guk
    • 한국해양바이오학회지
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    • 제7권1호
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    • pp.19-27
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    • 2015
  • The objective of the current study was to evaluate the inhibitory and antioxidant activities of powdered katsuobushi (dried bonito) protein hydrolysates and their corresponding fractions. The powdered katsuobushi (dried bonito) hydrolysates were obtained by enzymatic hydrolysis using Alcalase, ${\alpha}$-chymotrypsin, Neutrase, pepsin, papain, and trypsin. The antioxidant efficacy of the respective hydrolysates were evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, and alkyl radical-scavenging activities. Among the hydrolysates, the peptic-derived hydrolysate exhibited the highest antioxidant activity compared to other enzymatic hydrolysates. Therefore, the peptic-derived hydrolysate was further analyzed, and was found to contain an active peptide with an amino acid sequence identified as Pro-Met-Pro-Leu-Asn-Ser-Cys (756 Da). The purified peptides from powdered katsuobushi (dried bonito) had an $EC_{50}$ value of $105.82{\mu}M$, and exhibited an inhibitory effect against DNA oxidation induced by hydroxyl radicals. Taken together, these results suggests that powdered katsuobushi (dried bonito) could be used as a natural antioxidant in functional foods and prevent oxidation reactions in food processing.

오징어(Todarodes pacificus) 껍질로부터 Angiotensin I 전환효소 저해 펩티드의 분리 정제 (Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin)

  • 이정권;전중균;변희국
    • 한국수산과학회지
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    • 제44권2호
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    • pp.118-125
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    • 2011
  • In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

Effect of Enzymatic Hydrolysis of 7S Globulin, a Soybean Protein, on Its Allergenicity and Identification of its Allergenic Hydrolyzed Fragments Using SDS-PAGE

  • Keum, Eun-Hee;Lee, Sang-Il;Oh, Sang-Suk
    • Food Science and Biotechnology
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    • 제15권1호
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    • pp.128-132
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    • 2006
  • This study was undertaken to investigate the effect of peptic and chymotryptic hydrolyses of 7S globulin, the major allergen of soybean protein, on its allergenicity, as measured by enzyme linked immunosorbent assay (ELISA), and to identify the allergenic hydrolyzed fragments of 7S globulin using SDS-PAGE. When 7S globulin was hydrolyzed by pepsin, the allergenicity was reduced by over 50%. However, the allergenicity of 7S globulin reduced by peptic hydrolysis was recovered in the sera from 5 out of 10 patients following sequential chymotryptic hydrolysis. Two fragments, with molecular weights 20-25 and 13-16 kDa, among the hydrolysate of 7S globulin by sequential pepsin and chymotrypsin showed reactivity with sera from 10 soybean-allergenic patients. As a result of the theoretical hydrolyses of ${\beta}$-conglycinin, which is a major protein of 7S globulin, it is suggested that the 20-25 kDa fragments were the fragments of the ${\alpha}$-subunit of ${\beta}$'-conglycinin and that the 10-16 kDa fragments were from the ${\alpha}$'-subunit.

한우와 젖소 초유로부터 분리한 Lactoferrin과 가수분해물의 항균활성 (Antimicrobial Activities of Lactoferrin and its Hydrolysate Obtained from the Colostrum of Hanwoo and Holstein Cattle)

  • 양희진;이수원
    • Journal of Animal Science and Technology
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    • 제48권4호
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    • pp.595-602
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    • 2006
  • 본 연구는 우리나라 재래종인 한우로부터 초유를 얻어 Lf을 분리정제한 후 한우 Lf와 젖소 Lf의 항균활성을 확인하였다. E. coli O111및 기타 미생물에 대한 항균성은 젖소 Lf가 한우 Lf 보다 높았으며, 젖소 Lf 가수분해물도 한우 Lf 가수분해물보다 마찬가지로 높았다. MIC에서는 E. coli O111 경우 젖소 Lf가 1.5mg/ml, 한우 Lf은 2.75mg/ml이며 젖소 Lf 가수분해물은 0.12mg/ml, 한우 Lf 가수분해물은 0.25mg/ml로 항균성 실험과 동일하게 젖소 Lf 가수분해물의 항균활성이 더 높은 것으로 나타났다. 한편 Lf과 lysozyme의 첨가는 항균활성을 상승시키는 효과를 나타내었다.