• 제목/요약/키워드: Flavourzyme

검색결과 120건 처리시간 0.028초

Fractionation and Characterization of Fractions with High Antioxidative Activity from the Gelatin Hydrolysates of Korean Rockfish Sebastes schlegelii Skin

  • Kim, Hyung-Jun;Park, Kwon-Hyun;Shin, Jun-Ho;Lee, Ji-Sun;Heu, Min-Soo;Lee, Dong-Ho;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • 제14권3호
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    • pp.168-173
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    • 2011
  • The purpose of this study was to obtain a fraction with high antioxidative activity from second rockfish gelatin hydrolysates (SRSGHs), which were hydrolyzed with Alcalase and Flavourzyme through ultrafiltration membranes with serial digestions for 1 and 2 h, respectively, and to investigate the feasibility of this fraction as a potential functional food ingredient. Among various fractions that were ultrafiltered from the SRSGH with four types of membrane (1, 5, 10, and 30 kDa), the SRSGH-III fraction, which permeated the 10 kDa membrane but not the 5 kDa membrane, showed the highest antioxidant activity (protection factor=5.13) and angiotensin-I-converting enzyme-inhibiting activity ($IC_{50}$=0.82 mg/mL). These results suggest that the SRSGH-III fraction from the SRSGH can be used as a functional food ingredient. However, further studies examining its antioxidant activity in vivo as well as the different antioxidant mechanisms are needed.

Partial Purification of Antioxidative Peptides from Gelatin Hydrolysates of Alaska Pollock Surimi Refiner Discharge

  • Heu, Min-Soo;Park, Chan-Ho;Kim, Hyung-Jun;Park, Jae-W.;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • 제12권4호
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    • pp.249-257
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    • 2009
  • This study is conducted to partially purify an antioxidative peptide in a two-step gelatin hydrolysate from Alaska pollock surimi refiner discharge, which was obtained by sequential treatment with Pronase E and Flavourzyme. The two-step gelatin hydrolysate was fractionated using chromatographic methods. Based on the same protein concentration of each fraction, the antioxidative activities (85.1-95.4%) of positive fractions fractionated by ion-exchange chromatography were higher than those (27.2-87.8%) from gel filtration. Then, further purification of the positive fractions was performed. Among them, the partially purified A1C1L2G1 and A1C1L2G2 fractions showed 96.2% and 85.1% inhibition, respectively, of linoleic acid peroxidation. The A1C1L2G1 fraction was composed of 15 kinds of amino acids and the predominant amino acids were proline, glycine and alanine. The results obtained in this study suggested that the fraction partially purified through chromatographic methods from the two-step gelatin hydrolysate of Alaska pollock surimi refiner discharge could be useful as a supplementary source for improving health functionality.

Antioxidant and angiotensin I-converting enzyme inhibitory activities of northern shrimp (Pandalus borealis) by-products hydrolysate by enzymatic hydrolysis

  • Kim, Sang-Bo;Yoon, Na Young;Shim, Kil-Bo;Lim, Chi-Won
    • Fisheries and Aquatic Sciences
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    • 제19권7호
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    • pp.29.1-29.6
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    • 2016
  • In the present study, we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis. The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase, protamex, flavourzyme, papain, and trypsin) of PBB were evaluated by the 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities, reducing power and Li's method for ACE inhibitory activity. Of these PBB hydrolysates, the protamex hydrolysate exhibited the most potent ACE inhibitory activity with $IC_{50}$ value of $0.08{\pm}0.00mg/mL$. The PBB protamex hydrolysate was fractionated by two ultrafiltration membranes with 3 and 10 kDa (below 3 kDa, between 3 and 10 kDa, and above 10 kDa). These three fractions were evaluated for the total amino acids composition, antioxidant, and ACE inhibitory activities. Among these fractions, the < 3 kDa and 3-10 kDa fractions showed more potent $ABTS^+$ radical scavenging activity than that of > 10 kDa fraction, while the > 10 kDa fraction exhibited the significant reducing power than others. In addition, 3-10 kDa and > 10 kDa fractions showed the significant ACE inhibitory activity. These results suggested that the high molecular weight enzymatic hydrolysate derived from PBB could be used for control oxidative stress and prevent hypertension.

Pig Skin Gelatin Hydrolysates Attenuate Acetylcholine Esterase Activity and Scopolamine-induced Impairment of Memory and Learning Ability of Mice

  • Kim, Dongwook;Kim, Yuan H. Brad;Ham, Jun-Sang;Lee, Sung Ki;Jang, Aera
    • 한국축산식품학회지
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    • 제40권2호
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    • pp.183-196
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    • 2020
  • The protective effect of pig skin gelatin water extracts (PSW) and the low molecular weight hydrolysates of PSW generated via enzymatic hydrolysis with Flavourzyme® 1000L (LPSW) against scopolamine-induced impairment of cognitive function in mice was determined. Seventy male ICR mice weighing 20-25 g were randomly assigned to seven groups: Control (CON); scopolamine (SCO, 1 mg/kg B.W., intraperitoneally (i.p.); tetrahydroaminoacridine 10 [THA 10, tacrine; 10 mg/kg B.W. per oral (p.o.) with SCO (i.p.)]; PSW 10 (10 mg/kg B.W. (p.o.) with SCO (i.p.); PSW 40 (40 mg/kg B.W. (p.o.) with SCO (i.p.); LPSW 100 (100 mg/kg B.W. (p.o.) with SCO (i.p.); LPSW 400 (400 mg/kg B.W. (p.o.) with SCO (i.p.). All treatment groups, except CON, received scopolamine on the day of the experiment. The oxygen radical absorbance capacity of LPSW 400 at 1 mg/mL was 154.14 μM Trolox equivalent. Administration of PSW and LPSW for 15 weeks did not significantly affect on physical performance of mice. LPSW 400 significantly increased spontaneous alternation, reaching the level observed for THA and CON. The latency time of animals receiving LPSW 400 was higher than that of mice treated with SCO alone in the passive avoidance test, whereas it was shorter in the water maze test. LPSW 400 increased acetylcholine (ACh) content and decreased ACh esterase activity (p<0.05). LPSW 100 and LPSW 400 reduced monoamine oxidase-B activity. These results indicated that LPSW at 400 mg/kg B.W. is a potentially strong antioxidant and contains novel components for the functional food industry.

빅벨리 해마(Hippocampus abdominalis) 유래 펩신 가수분해물의 In vitro와 In vivo에서의 항산화 효능 (Antioxidant Activity of Pepsin Hydrolysate Derived from Edible Hippocampus abdominalis in vitro and in Zebrafish Models)

  • 김현수;신병옥;김서영;;이원우;김윤택;노섬;조문제;전유진
    • 한국수산과학회지
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    • 제49권4호
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    • pp.445-453
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    • 2016
  • Seahorse Hippocampus abdominalis a marine teleost fish, has long been used as one of the essential materials in traditional Chinese medicine. However, the uses of seahorse have been limited due to its high cost, despite its beneficial biological activities. Seahorse has not been widely explored for its biofunctional properties and active components. In the present study, the enzymatic hydrolysates of seahorse were prepared by using two digestive enzymes (trypsin and pepsin) and five food grade enzymes (neutrase, protamex, alcalase, kojizyme, and flavourzyme). The enzymatic hydrolysates indicated higher hydrolysis yields than its water extract. Among them, the distilled water-pepsin hydrolysate (DP) which was obtained by distilled water extraction followed by pepsin hydrolysis, showed the highest yield and protein content as well as the highest alkyl radical scavenging activity. Also, it provided protective effects against oxidative stress induced by AAPH in vero cell and zebrafish. Further fractionation based on the molecular weight was carried out to identify it’s active components, and < 5 kDa (less than 5 kDa) molecular weight fraction was confirmed to have the highest antioxidant activity. In conclusion, this study suggests that DP of seahorse has antioxidant properties, and might be a novel and useful material from the marine origin for healthy functional foods and cosmetics.

2단 가수분해에 의한 굴 가수분해물의 기능성 개선 (Improving the Functional Properties of Oyster Hydrolysates by Two-step Enzymatic Hydrolysis)

  • 정인권;김진수;허민수
    • 한국수산과학회지
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    • 제39권3호
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    • pp.269-277
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    • 2006
  • This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.

효소가수분해 조건에 따른 우유 케이신의 Angiotensin-I 전환효소 저해효과 (Angiotensin- I Converting Enzyme Inhibitory Properties of Bovine Casein Hydrolysates in Different Enzymatic hydrolysis Conditions)

  • 김현수;인영민;정석근;함준상;강국희;이수원
    • 한국축산식품학회지
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    • 제22권1호
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    • pp.87-93
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    • 2002
  • 최근 고혈압을 예방하기 위한ACE 저해 펩타이드에 대한 연구는 주로 여러 가지 식품 단백질의 효소 가수분해물로부터 얻어진 펩타이드를 중심으로 이루어지고 있다. 본 연구에서는 케이신을 여러 가지 상업용 단백질분해 효소를 사용하여 ACE저해 효과가 높은 가수분해물 제조시 가수분해 조건이 ACE저해효과에 미치는 영향을 알아보자 하였으며 적정 가수분해 조건을 설정하고자 하였다. ACE 저해효과를 가지는 케이신 가수분해 물을 제조하기 위한 효소 종류, 첨가량 및 가수분해시간은 효소는 Aspergillus oryzae 유래의 promod 192를 사용하고, 효소의 첨가량은 케이신에 대하여 1%, 반응시간은 47$^{\circ}C$에서 12시간으로 하는 것이 적당하였다. 이 때 케이신 가수분해물의 $IC_{50}$/값은 248.71ug/m1(통상법), 265.84ug/ml(전처리법)로서 ACE 저해효과가 높았다.

닭털 단백질로부터 가수분해물 제조 및 철분 결합 펩타이드의 분리 (Preparation of chicken feather protein hydrolysates and isolation of iron-binding peptides)

  • 김남호;최동원;송경빈
    • 한국식품저장유통학회지
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    • 제20권3호
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    • pp.435-439
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    • 2013
  • 닭털 단백질을 단백질 가수분해 효소인 Flavouzyme을 이용하여 8시간 동안 가수분해하여 가수분해물을 제조하였다. 닭털 단백질 가수분해물로부터 저분자량 펩타이드를 얻고자 한외여과를 하였고, 철분 결합 펩타이드를 분리하기 위해 Q-Sepharose와 Sephadex G-15 컬럼을 사용하여 분리하였다. 그 결과, 철분 결합력이 높은 펩타이드 분획, F12를 분리하였고, 향후 철분 보충제로써 활용이 가능하다고 판단된다.

RSM을 이용한 홍게(Chionoecetes japonicus) 자숙부산물의 최적 효소가수분해 조건 (Optimal Conditions for Enzymatic Hydrolysate of Snow Crab Chionoecetes japonicus Cooker Effluent Using Response Surface Methodology)

  • 백정화;정은정;전선영;차용준
    • 한국수산과학회지
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    • 제44권2호
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    • pp.99-103
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    • 2011
  • This study was performed to determine the optimal hydrolysis conditions for the production of a flavoring from the precipitation of snow crab cooker effluent (PSCCE) with commercial proteases. Based on cost-per-enzyme activity and sensory evaluations, Flavourzyme$^{(R)}$ 500 MG plus Protamex$^{(R)}$ (1:1 ratio, w/w) were selected as suitable enzymes. Three independent variables consisting of the substrate concentration (S), enzyme-to-substrate ratio (E/S), and hydrolysis time (T) were examined using response surface methodology (RSM). A model equation obtained from RSM was used to predict the degree of hydrolysis (DH) as follows: % DH = 52.285 - 6.371[S] + 5.469[E/S] + 7.599[T] - $5.818[S]^2$ - $5.633[E/S]^2$ - $6.528[T]^2$ - 3.265[E/S][S] - 5.415[T][S] + 4.315[T][E/S]. From the ridge analysis, the conditions favoring the highest degree of hydrolysis were pH 7.45, $55^{\circ}C$, a S of 21.82%, an E/S of 0.50%, and a T of 3.74 h.

Protective Effect of Enzymatic Extracts from Sargassum coreanum on H2O2-induced Cell Damage

  • Ko, Seok-Chun;Kang, Sung-Myung;Lee, Seung-Hong;Ahn, Gin-Nae;Kim, Kil-Nam;Kim, Yong-Tae;Kim, Jin-Soo;Heu, Min-Soo;Jeon, You-Jin
    • Fisheries and Aquatic Sciences
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    • 제13권1호
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    • pp.26-35
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    • 2010
  • In our previous study, we preliminarily demonstrated that Celluclast and Neutrase extracts exhibited the strongest $H_2O_2$-scavenging activities among five carbohydrases (Viscozyme, Celluclast, Termamyl, Ultraflo and AMG) and five proteases (Kojizyme, Alcalse, Flavourzyme Protamex and Neutrase) extracts. Thus, Celluclast and Neutrase extracts were selected for use in further experiments and were separated into four different molecular weight fractions (<5, 5-10, 10-30 and >30 kDa). Among them, the 5-10 kDa fraction showed the highest $H_2O_2$-scavenging activity. The 5-10 kDa fraction also strongly enhanced cell viability against $H_2O_2$-induced oxidative damage. Furthermore, the fraction reduced the proportion of apoptotic cells induced by $H_2O_2$, as demonstrated by decreased sub-G1 hypodiploid cells and decreased apoptotic body formation by flow cytometry. These results indicated that the 5-10 kDa fraction of the Celluclast and Neutrase extracts from S. coreanum exhibited strong antioxidant activity over $H_2O_2$-mediated cell damage in vitro.