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      열수 및 효소적 가수분해로 제조된 틸라피아 비늘 젤라틴 가수분해물의 ACE 저해 활성 = Angiotensin I Converting Enzyme Inhibitory Effects of Gelatin Hydrolysates Prepared from Tilapia mossambica Scales by Hot Water and Enzymatic Extraction

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      https://www.riss.kr/link?id=A103875469

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      다국어 초록 (Multilingual Abstract)

      Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of tilapia scales were prepared by enzymatic extraction using five proteases (α-chymotrypsin, Alcalase, Kojizyme, Protamex and trypsin) after scales were treated with hot water for 3 hr. Scale enzymatic hydrolysates prepared using both hot water and enzyme treatments exhibited elevated hydrolysis (about 25%–55%) compared to only enzyme treatment (about 15%–45%). Enzymatic hydrolysates (1 mg/mL) prepared by both hot water and enzyme treatments also showed significantly increased ACE inhibitory activities from about 20%–75%. The pattern of ACE inhibitory activities was similar to the degree of hydrolysis. Alcalase and α-chymotrypsin hydrolysates displayed the highest ACE inhibitory activities (IC50 = 0.83 mg/mL and 0.68 mg/mL, respectively). In addition, the ACE inhibitory effects of α-chymotrypsin hydrolysates increased with decreasing molecular weight (5 kDa>, 10 kDa> and 30 kDa>), with the 5 kDa> fraction displaying the highest ACE inhibitory activity (about 89.9% and IC50 = 0.1 mg/mL). We suggest that the peptide compounds of enzymatic hydrolysates prepared from tilapia scale enhances ACE inhibitory activity and might be useful as an antihypertensive material.
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      Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of til...

      Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of tilapia scales were prepared by enzymatic extraction using five proteases (α-chymotrypsin, Alcalase, Kojizyme, Protamex and trypsin) after scales were treated with hot water for 3 hr. Scale enzymatic hydrolysates prepared using both hot water and enzyme treatments exhibited elevated hydrolysis (about 25%–55%) compared to only enzyme treatment (about 15%–45%). Enzymatic hydrolysates (1 mg/mL) prepared by both hot water and enzyme treatments also showed significantly increased ACE inhibitory activities from about 20%–75%. The pattern of ACE inhibitory activities was similar to the degree of hydrolysis. Alcalase and α-chymotrypsin hydrolysates displayed the highest ACE inhibitory activities (IC50 = 0.83 mg/mL and 0.68 mg/mL, respectively). In addition, the ACE inhibitory effects of α-chymotrypsin hydrolysates increased with decreasing molecular weight (5 kDa>, 10 kDa> and 30 kDa>), with the 5 kDa> fraction displaying the highest ACE inhibitory activity (about 89.9% and IC50 = 0.1 mg/mL). We suggest that the peptide compounds of enzymatic hydrolysates prepared from tilapia scale enhances ACE inhibitory activity and might be useful as an antihypertensive material.

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      참고문헌 (Reference)

      1 홍장희, "감태 (Ecklonia cava) 추출물의 항고혈압 효과" 한국생약학회 37 (37): 200-205, 2006

      2 Kim JS, "The suitable processing condition for gelatin preparation from yellowfin sole skin" 25 (25): 716-723, 1993

      3 Ursula C, "The renin-angiotensin-aldosterone system and the kidney: Effects on kindney disease" 116 : 263-272, 2004

      4 Bowes JH, "The com- position of collagen and acidsoluble collagen of bovine skin" 61 (61): 143-150, 1955

      5 Richard N, "The clinical implication of tissue renin angiotensin systems" 16 : 317-327, 2002

      6 Kim JS, "Screening for the raw Material of gelatin from the skins of some pelagic fishs and squid" 30 (30): 55-61, 1997

      7 Hoyle NT, "Quality of fish protein hydrolysates from Herring. (Clupea harengus)" 59 (59): 76-79, 1994

      8 Lowry OH, "Protein Measurement with the folin phenol reagent" 193 : 265-275, 1951

      9 Jamilah B, "Properties of ge- latins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica)" 77 (77): 81-84, 2002

      10 Kim JS, "Preparation of conger eel skin gelatin by precipitation with ethanol and its properties" 12 : 51-57, 1999

      1 홍장희, "감태 (Ecklonia cava) 추출물의 항고혈압 효과" 한국생약학회 37 (37): 200-205, 2006

      2 Kim JS, "The suitable processing condition for gelatin preparation from yellowfin sole skin" 25 (25): 716-723, 1993

      3 Ursula C, "The renin-angiotensin-aldosterone system and the kidney: Effects on kindney disease" 116 : 263-272, 2004

      4 Bowes JH, "The com- position of collagen and acidsoluble collagen of bovine skin" 61 (61): 143-150, 1955

      5 Richard N, "The clinical implication of tissue renin angiotensin systems" 16 : 317-327, 2002

      6 Kim JS, "Screening for the raw Material of gelatin from the skins of some pelagic fishs and squid" 30 (30): 55-61, 1997

      7 Hoyle NT, "Quality of fish protein hydrolysates from Herring. (Clupea harengus)" 59 (59): 76-79, 1994

      8 Lowry OH, "Protein Measurement with the folin phenol reagent" 193 : 265-275, 1951

      9 Jamilah B, "Properties of ge- latins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica)" 77 (77): 81-84, 2002

      10 Kim JS, "Preparation of conger eel skin gelatin by precipitation with ethanol and its properties" 12 : 51-57, 1999

      11 Sobral PJA, "Phase tran- sitions of pigskin gelatin" 15 : 377-382, 2001

      12 Yokokawa K, "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito" 56 : 1541-1545, 1992

      13 AOAC, "Official Methods of Analysis. 14th ed"

      14 Duncan DB, "Multiple-range and multiple F tests" 11 : 1-42, 1955

      15 Giles TD, "Lipid factors in the hypertension syndrome" 4 : 257-259, 1997

      16 Kim SK, "Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin" 49 : 1984-1989, 2001

      17 Kim SK, "Isolation and characterization of antioxidative pe- ptides from enzymatic hydrolysates of yellowfin sole skin gelatin" 29 (29): 246-255, 1996

      18 Matsui T, "Inhibition of angio- tensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle" 57 : 922-925, 1993

      19 Frohlich ED, "Hemodynamic factors in the path- ogenesis and maintenance of hyp" 41 : 2400-2408, 1982

      20 Gudmundsson M, "Gelatin from cod skins as affected by chemical treatm- ents" 62 (62): 37-39, 1997

      21 Songchotikunpan P, "Extraction and electrospinning of gelatin from fish skin" 42 : 247-255, 2008

      22 Cho SM, "Extracting opt- imization and physical properties of yellowfin tuna (Thunnus albacares) skin gelatin compared to mam- malian gelatins" 19 (19): 221-229, 2005

      23 Shahidi F, "Enzymes from fish and aquatic invertebrates and their application in the food industry" 12 : 435-464, 2001

      24 Cheung HS, "Binding of peptide substrates and inhibitors of angiotensin I-converting enzyme. Importance of the COOH-terminal dipeptide sequ- ence" 225 : 401-407, 1980

      25 Maruyama S, "Angiotensin-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and ileum of rats" 49 : 1405-1409, 1985

      26 Weiss D, "Angiotensin II-induced hypertension accelerates the development of atherosclerosis in apoE-deficient mice" 103 : 448-454, 2001

      27 Walmor C, "Angiotensin II and the Heart On the Intracrine Renin-Angiotensin System" 35 : 1183-1188, 2000

      28 Oh SJ, "Angiotensin I-converting enzyme inhibitory activity of the K-casein fragments hydrolyzated by chy- mosin, pepsin, and trypsin" 29 : 1316-1318, 1997

      29 Maruyama S, "Angiotensin I-converting enzyme activities of synthetic peptides related to the tandem repeated sequence of a maize endosperm protein" 53 : 1077-1081, 1989

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      공동연구자 (7)

      유사연구자 (20) 활용도상위20명

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2026 평가예정 재인증평가 신청대상 (재인증)
      2020-01-01 평가 등재학술지 유지 (재인증) KCI등재
      2017-01-01 평가 등재학술지 유지 (계속평가) KCI등재
      2014-08-06 학술지명변경 외국어명 : Korean Journal of Fisheries and Aquatic Sciences -> Korean Journal of Fisheries and Aquatic Sciences KCI등재
      2013-01-01 평가 등재학술지 유지 (계속평가) KCI등재
      2010-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-09-04 학회명변경 한글명 : 한국수산학회 -> 한국수산과학회
      영문명 : The Korean Fisheries Society -> The Korean Society of Fisheries and Aquatic Science
      KCI등재
      2009-07-03 학술지명변경 한글명 : 한국수산학회지 -> 한국수산과학회지
      외국어명 : Journal of The Korean Fisheries Society -> Korean Journal of Fisheries and Aquatic Sciences
      KCI등재
      2008-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2006-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2003-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2002-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      1999-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.47 0.47 0.43
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.43 0.43 0.59 0.17
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