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      오징어 간 가수분해물의 기능성

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      https://www.riss.kr/link?id=A99546064

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      부가정보

      국문 초록 (Abstract)

      북해도산 오징어 간의 유효이용을 목적으로 자가소화물과 Protamex 가수분해물을 제조하고 이들의 식품학적 특성과 몇 가지 기능성을 조사하였다. 자가소화를 위한 최적 조건은 간의 함량 93.5%, pH 6.4, 항온온도 47℃였으며, Protamex 가수분해의 최적 조건은 오징어 간에 대한 Protamex의 첨가비율 0.33%, pH 6.0, 가수분해온도 55℃이었다. Promatex 가수분해물의 총 아미노산 조성에서 proline, cysteine 및 methionine이 검출되지 않았으나, 유리아미노산 조성에서는 검출되었다. 오징어 간, 자가소화물 및 Promatex 가수분해물의 카드늄 함량은 건조 중량으로 각각 8.32±0.03mg/100 g, 3.56±0.02 mg/100 g, 13.26±0.04 mg/100 g으로서 식품안전 규정 이하의 농도로 감소시키기 위한 별도의 공정이 필요하다. 자가소화물의 주요 저분자 물질의 분자량은 1.0~1.5 kDa인 반면, Protamex 가수분해물은 210~470 Da이었다. 자가소화물과 Protamex 가수분해물 간에 표면소수성, 유화활성 지표, 유화안정성, 지방 및 수분 흡착능은 큰 차이를 보이지 않았으며, 높은 ACE 효소 저해효과가 관측되었다. 한편 HepG2 세포주에 대한 독성은 200 μg/mL까지 관측되지 않았다.
      번역하기

      북해도산 오징어 간의 유효이용을 목적으로 자가소화물과 Protamex 가수분해물을 제조하고 이들의 식품학적 특성과 몇 가지 기능성을 조사하였다. 자가소화를 위한 최적 조건은 간의 함량 93.5...

      북해도산 오징어 간의 유효이용을 목적으로 자가소화물과 Protamex 가수분해물을 제조하고 이들의 식품학적 특성과 몇 가지 기능성을 조사하였다. 자가소화를 위한 최적 조건은 간의 함량 93.5%, pH 6.4, 항온온도 47℃였으며, Protamex 가수분해의 최적 조건은 오징어 간에 대한 Protamex의 첨가비율 0.33%, pH 6.0, 가수분해온도 55℃이었다. Promatex 가수분해물의 총 아미노산 조성에서 proline, cysteine 및 methionine이 검출되지 않았으나, 유리아미노산 조성에서는 검출되었다. 오징어 간, 자가소화물 및 Promatex 가수분해물의 카드늄 함량은 건조 중량으로 각각 8.32±0.03mg/100 g, 3.56±0.02 mg/100 g, 13.26±0.04 mg/100 g으로서 식품안전 규정 이하의 농도로 감소시키기 위한 별도의 공정이 필요하다. 자가소화물의 주요 저분자 물질의 분자량은 1.0~1.5 kDa인 반면, Protamex 가수분해물은 210~470 Da이었다. 자가소화물과 Protamex 가수분해물 간에 표면소수성, 유화활성 지표, 유화안정성, 지방 및 수분 흡착능은 큰 차이를 보이지 않았으며, 높은 ACE 효소 저해효과가 관측되었다. 한편 HepG2 세포주에 대한 독성은 200 μg/mL까지 관측되지 않았다.

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      다국어 초록 (Multilingual Abstract)

      The autolysate and hydrolysate of a common squid liver, Todarodes pacificus, were prepared. Autolysis (liver ratio, pH, temperature) and Protamex-treated hydrolysis (pH, temperature, ratio of protease to liver) conditions were optimized by response surface methodology using central composite design for under 1 hr of hydrolysis time. The desirability profile indicated that maximum DH could be achieved at a squid liver of 93.5%, pH 6.4, and 47℃ in autolysis, while that of Protamex-treated hydrolysis did at a Protamex-to-squid liver level of 0.33%, pH 6.0, and 55℃. Three amino acids, proline, cysteine, and methionine, were not detected in the total amino acid composition of the Protamex-treated hydrolysate, while they were detected in the free amino acid composition. Cadmium was 8.32±0.03 mg/100 g-powder for raw, 3.56±0.02 mg/100 g-powder for the autolysate, and 13.26 ±0.04 mg/100 g powder for the Protamex-treated hydrolysate. The major molecular weight ranged from 1.0 to 1.5 kDa for the autolysate and from 210 to 470 Da for the Protamex-treated hydrolysate. Food functionalities of the autolysate, such as surface hydrolphobicity, emulsion activity index, emulsion stability, water, and fat adsorption, were similar to the Protamex-treated hydrolysate. Both the autolysate and Protamex-hydrolysate showed high inhibitory activities on the angiotensin-I converting enzyme. Cell toxicity against the HepG2 cell line was not detected in the autolysate or the Protamex-treated hydrolysate by 200 μg/mL.
      번역하기

      The autolysate and hydrolysate of a common squid liver, Todarodes pacificus, were prepared. Autolysis (liver ratio, pH, temperature) and Protamex-treated hydrolysis (pH, temperature, ratio of protease to liver) conditions were optimized by response su...

      The autolysate and hydrolysate of a common squid liver, Todarodes pacificus, were prepared. Autolysis (liver ratio, pH, temperature) and Protamex-treated hydrolysis (pH, temperature, ratio of protease to liver) conditions were optimized by response surface methodology using central composite design for under 1 hr of hydrolysis time. The desirability profile indicated that maximum DH could be achieved at a squid liver of 93.5%, pH 6.4, and 47℃ in autolysis, while that of Protamex-treated hydrolysis did at a Protamex-to-squid liver level of 0.33%, pH 6.0, and 55℃. Three amino acids, proline, cysteine, and methionine, were not detected in the total amino acid composition of the Protamex-treated hydrolysate, while they were detected in the free amino acid composition. Cadmium was 8.32±0.03 mg/100 g-powder for raw, 3.56±0.02 mg/100 g-powder for the autolysate, and 13.26 ±0.04 mg/100 g powder for the Protamex-treated hydrolysate. The major molecular weight ranged from 1.0 to 1.5 kDa for the autolysate and from 210 to 470 Da for the Protamex-treated hydrolysate. Food functionalities of the autolysate, such as surface hydrolphobicity, emulsion activity index, emulsion stability, water, and fat adsorption, were similar to the Protamex-treated hydrolysate. Both the autolysate and Protamex-hydrolysate showed high inhibitory activities on the angiotensin-I converting enzyme. Cell toxicity against the HepG2 cell line was not detected in the autolysate or the Protamex-treated hydrolysate by 200 μg/mL.

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      목차 (Table of Contents)

      • Abstract
      • 서론
      • 재료 및 방법
      • 결과 및 고찰
      • 요약
      • Abstract
      • 서론
      • 재료 및 방법
      • 결과 및 고찰
      • 요약
      • 문헌
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      참고문헌 (Reference)

      1 배윤정, "한국산 어류 8종 추출물의 생리활성" 한국수산과학회 37 (37): 445-454, 2004

      2 김혜숙, "원양산 오징어(Illex argentinus) 내장으로부터 Endoprotease" 한국수산과학회 41 (41): 176-181, 2008

      3 Sugiyama MX, "Utilization of squid" Koseisha Koseikaku 80-89, 1980

      4 최영준, "Use of Tetragenococcus halophilus as a Starter Culture for Flavor Improvement in Fish Sauce Fermentation" AMER CHEMICAL SOC 59 (59): 8401-8408, 201108

      5 Komai T, "Purification of serine carboxypeptidase from the hepatopancreas of Japanese common squid Todarodes pacificus and its application for elimination of bitterness from bitter peptides" 73 : 404-411, 2007

      6 제재영, "Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties" ELSEVIER SCIENCE BV 38 (38): 175-182, 200503

      7 Ono S, "Proteolytic conversion of squid hepatopancreas andupstream chum salmon muscle to angiotensin I-convertingenzyme inhibitory peptides" 68 : 192-196, 2002

      8 Lowry OH, "Protein measurement with Folin phenol reagent" 193 : 256-275, 1951

      9 Bhaskar N, "Protein hydrolysate from visceral waste proteins of Catla (Catla catla): Optimization of hydrolysis conditions for a commercial neutral protease" 99 : 4105-4111, 2008

      10 Pyeun JH, "Postmortem changes of the protein and amino acid composition of muscle in the partially frozen prawn. Pendalus japonica" 17 : 280-290, 1984

      1 배윤정, "한국산 어류 8종 추출물의 생리활성" 한국수산과학회 37 (37): 445-454, 2004

      2 김혜숙, "원양산 오징어(Illex argentinus) 내장으로부터 Endoprotease" 한국수산과학회 41 (41): 176-181, 2008

      3 Sugiyama MX, "Utilization of squid" Koseisha Koseikaku 80-89, 1980

      4 최영준, "Use of Tetragenococcus halophilus as a Starter Culture for Flavor Improvement in Fish Sauce Fermentation" AMER CHEMICAL SOC 59 (59): 8401-8408, 201108

      5 Komai T, "Purification of serine carboxypeptidase from the hepatopancreas of Japanese common squid Todarodes pacificus and its application for elimination of bitterness from bitter peptides" 73 : 404-411, 2007

      6 제재영, "Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties" ELSEVIER SCIENCE BV 38 (38): 175-182, 200503

      7 Ono S, "Proteolytic conversion of squid hepatopancreas andupstream chum salmon muscle to angiotensin I-convertingenzyme inhibitory peptides" 68 : 192-196, 2002

      8 Lowry OH, "Protein measurement with Folin phenol reagent" 193 : 256-275, 1951

      9 Bhaskar N, "Protein hydrolysate from visceral waste proteins of Catla (Catla catla): Optimization of hydrolysis conditions for a commercial neutral protease" 99 : 4105-4111, 2008

      10 Pyeun JH, "Postmortem changes of the protein and amino acid composition of muscle in the partially frozen prawn. Pendalus japonica" 17 : 280-290, 1984

      11 Wanasundara PK, "Peptide with angiotensin I-converting enzyme (ACE) inhibiting activity from defibrinated hydrolyzed bovine plasma" 50 : 6981-6988, 2002

      12 Cheung IW, "Pacific hake(Merluccius productus) hydrolysates as cryoprotectiveagents in frozen pacific cod fillet mince" 74 : C588-C594, 2009

      13 Bhaskar N, "Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease" 99 : 335-343, 2008

      14 AOAC, "Official Method of Analysis of AOAC Intl.15th ed"

      15 Chen DW, "Non-volatile taste active compounds in the meat of Chinese mitten crab (Eriocheir sinensis)" 104 : 1200-1205, 2007

      16 Shetty Ak, "Isolation and characterization of a novel chondroitin sulfate from squid liver integument rich in N-acetylgalactosamine(4,6-disulfate) and glucuronate( 3-sulfate) residues" 344 : 1526-1532, 2009

      17 Kishimura H, "Isolation and characteristics of trypsin inhibitor from the hepatopancrease of a squid (Todarodes pacificus)" 130 : 117-123, 2001

      18 Bourseau P, "Fractionation of fish protein hydrolysates by ultrafiltration and nanofiltration: impact on peptidic populations" 244 : 303-320, 2009

      19 Kristinsson HG, "Fish protein hydrolysates: production, biochemical, and functional properties" 40 : 43-81, 2000

      20 Choi YJ, "Enzymatic hydrolysis of recovered protein from frozen small croaker and functional properties of its hydrolysates" 74 : C17-C24, 2009

      21 Hall SE, "Emulsions, In Methods of Testing Protein Functionality" Blackie Academic & Professional 153-185, 1996

      22 van der Van C, "Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics" 49 : 5005-5012, 2001

      23 Park EY, "Effects of protein and peptide addition on lipid oxidation in powder model system" 53 : 137-144, 2005

      24 Hossain MA, "Effect of proteolytic squid protein hydrolysate on the state of water and denaturation of lizardfish (Saurida wanieso) myofibrillar protein during freezing" 5 : 73-79, 2004

      25 Kato A, "Determination of protein hydrophobicity using sodium dodecyl sulfate binding method" 32 : 284-288, 1984

      26 Cardenas-Lopez JL, "Cysteine proteinase activity in jumbo squid (Dosidicus gigas) hepatopancreas extracts" 29 : 171-186, 2005

      27 Kurihara H, "Concentration of cadmium in livers of several kinds of squids and an approach to its elimination" 44 : 32-38, 1993

      28 Hatate H, "Comparison of protease activity in liver among several species of squid and cuttlefish" 66 : 182-183, 2000

      29 Spies, "Colorimetric procedure for determination of amino acid, In Methods in Enzymology I I I" Academic press 467-477, 1957

      30 Bueno-Solano C, "Chemical and biological characteristics of protein hydrolysates from fermented shrimp by-products" 112 : 671-675, 2009

      31 Xu W, "Biochemical changes associated with fast fermentation of squid processing by-products for low salt fish sauce" 107 : 1597-1604, 2008

      32 Nam SH, "Antioxidative, antimutagenic, and anticarcinogenicactivities of rice bran extracts in chemical and cell assays" 53 : 816-822, 2005

      33 Samaranayaka AG, "Antioxidative and angiotensin-I-converting enzyme inhibitory potential of a Pacific hake (Merluccius productus) fish protein hydrolysate subjected to simulated gastrointestinal digestion and Caco-2 cell permeation" 58 : 1535-1542, 2010

      34 Je JY, "Antioxidant and antihypertensive protein hydrolysates produced from tuna liver by enzymatic hydrolysis" 42 : 1266-1272, 2009

      35 Chen HM, "Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein" 44 : 2619-2623, 1996

      36 Klompong V, "Antioxidant activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type" 102 : 1317-1327, 2007

      37 Wako Y, "Angiotensin Iconverting enzyme inhibitors in autolysates of squid liver and mantle muscle" 60 : 1353-1355, 1996

      38 Bougatef A, "Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sadinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases" 111 : 350-356, 2008

      39 Folch J, "A simple method for the isolation and purification of total lipids from animal tissues" 226 : 497-509, 1957

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2014-06-24 학회명변경 한글명 : 한국식품영양과학회지 -> 한국식품영양과학회
      영문명 : Journal of the Korean Society of Food Science and Nutrition -> The Korean Society of Food Science and Nutrition
      KCI등재
      2014-04-02 학회명변경 한글명 : 한국식품영양과학회 -> 한국식품영양과학회지
      영문명 : 미등록 -> Journal of the Korean Society of Food Science and Nutrition
      KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2002-07-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2000-01-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 1.03 1.03 1.13
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      1.18 1.2 1.993 0.21
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