• Title, Summary, Keyword: 가수분해

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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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    • 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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Physicochemical and Functional Properties of Pepsin-modified Myofibrillar protein from Sardine, Sardinops melanostica (Pepsin으로 수식된 정어리 myofibrillar protein의 특성)

  • Kim, Byung-Mook;Kim, Byung-Ryul
    • Korean Journal of Food Science and Technology
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    • v.26 no.2
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    • pp.110-116
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    • 1994
  • In order to study the effects of enzyme modification on the physico-chemical and functional properties of myofibrillar protein prepared from the frozen sardine, Sardinops melanostica, the protein was hydrolyzed with pepsin under the enzyme-substrate ratio 1:100 at $37^{\circ}C$ and pH 1.65 for 1, 4, 8, 12, and 24 hr, respectively. The properties of pepsin-modified sardine myofibriliar protein were determined. The extents of proteolysis with pepsin as a fuction of time was showed a typical enzyme hydorlysis curve with an initial region of 4 hour period followed by plateau region. The SDS-acrylamide slab gel electrophoresis patterns of pepsin-modified proteins showed mainly disappearances of minor protein bands, but no changes of main protein bands. The gel filtration patterns through Sephadex G-75 of sardine myofibrillar protein showed two big peaks and three small peaks. All the small peaks were disappearanced by proteolysis with pepsin in one hour. and during the period of proteolysis the fast big peak became gradually smaller and the late big peak eluted more slowly. By proteolysis, the emulsifying activity and emulsifying capacity of sardine myofibrillar protein were all decreased. The effects of pepsin-modification on emulsifying capacity were greater than those on emulsifying activity of protein. The aeration capacity of the protein was increased about 1.9 folds and the foam stability decreased to 0.6 folds of control by pepsin-modification. The pepsin-modified sardine myofibrillar proteins showed about 0.6 folds of heat coagulation and 1.4 folds of viscosity of control. The pH dependence of solubilities of sardine myofibrillar protein showed two isoelectric areas of pH 5 and 9. The pepsin-modified protein showed more clear pH dependences at the early stage but not at the late stage of proteolysis.

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Optimal conditions of enzymatic hydrolysis for producing anti-inflammatory peptides from sandfish (Arctoscopus japonicus) hydrolysate (도루묵 가수분해물 유래 항염증 펩타이드 제조를 위한 효소 가수분해 최적 조건)

  • Jang, Hye Lim;Yoon, Kyung Young
    • Korean Journal of Food Science and Technology
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    • v.50 no.2
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    • pp.203-208
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    • 2018
  • In this study, the hydrolysis conditions for the production of anti-inflammatory peptides from meat and roe hydrolysates of sandfish (Arctoscopus japonicus) were determined by measuring the nitric oxide (NO) scavenging enzymatic activity, experimental pH, temperature, enzyme concentration, and hydrolysis time. The optimal conditions determined when using meat hydrolysate were a pH value of 5.0, at a temperature of $30^{\circ}C$, 1% enzyme concentration, and 4 h hydrolysis time. The optimal conditions when using roe hydrolysate were a pH of 5.0, a temperature of $70^{\circ}C$, enzyme concentration of 3%, and hydrolysis time of 3 h. The NO scavenging activities of meat and roe hydrolysate were determined to be 18.94 and 19.81%, respectively. In summary, this study determined the optimum enzymatic hydrolysis conditions for the production of anti-inflammatory peptides from sandfish.

Evaluation of Angiotensin -I- Converting Enzyme Inhibitory Activity and Protein Changes of Enzymatic Hydrolysate Extracted from Hanwoo Loin and Round Myosin B (한우 등심과 우둔에서 추출한 Myosin B의 효소적 가수분해물의 단백질 변화와 Angiotensin -I- Converting Enzyme(ACE) 저해효과)

  • Kim, Y.J.;Chin, Koo-Bok
    • Journal of Animal Science and Technology
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    • v.49 no.1
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    • pp.129-136
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    • 2007
  • This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.

Stability and Reactivity of Vinylsulfonyl Reactive Dyes (Vinylsulfone계 반응성염료의 안정성과 반응성)

  • 김인회
    • Textile Coloration and Finishing
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    • v.10 no.4
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    • pp.24-29
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    • 1998
  • 11종류의 cellulose에 고착된 vinylsulfone(VS)계 반응성 염료(F-type)의 알칼리 가수분해 거동과 염료와 섬유의 결합 안정성을 cellophane film을 이용한 film권층법에 의하여 조사하였다. F-type은 알칼리욕에서 분해되어 VS type을 생성하고 VS type은 가수분해에 의해 hydroxyethylsulfone(Hy)을 생성하거나 cellulose와 재결합하여 F-type을 생성하였다. F-type은 알칼리 처리에 의해 cellulose의 수산기의 위치에 기인하는 bimodal 가수분해 거동(fast and slow hydrolysis)을 나타내었다. Orange 7과 Yellow 17는 cellulose와의 반응성이 높고 F-type의 초기 분해속도가 빠르며 일반적으로 fast 가수분해속도가 slow 가수분해 속도보다 약 5배정도 큼을 알 수 있었다. 또한 조사된 대부분의 염료의 경우 slow 가수분해 속도는 거의 유사함을 알 수 있었다.

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산양유 ${\beta}$-Casein의 효소 가수분해 특성과 가수분해물의 Angiotensin Converting Emzyme 저해효과

  • Park, Yong-Guk;Kim, Geo-Yu
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • pp.304-306
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    • 2004
  • 본 연구는 산양유 ${\beta}$-casein의 효소에 의한 가수분해 특성과 가수분해물의 Angiotensin Converting Enzyme의 저해 효과를 측정하고자 실시하였으며 그 결과는 다음과 같다. 1. 산양유 ${\beta}$-casein은 Mono S HR 5/5 양이온 교환 컬럼에서 분리하여 SDS-PAGE로 순수하게 분리된 것을 확인하였다. 2. 분리된 ${\beta}$-casein을 Trypsin으로 처리하여 가수분해물의 ACE저해 활성을 측정한 결과 가수분해 하지 않은 ${\beta}$-casein은 1.8%의 저해활성을 나타낸 반면, 가수분해한 ${\beta}$-casein은 25.36%의 저해활성을 나타내어 ACE 저해활성이 크게 증가한 것을 확인하였다. 3. 가수분해물의 $IC_{50}$을 측정한 결과 $308.7{\mu}{\ell}/m{\ell}$로 나타났다.

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장내 가수분해조건에 의한 Casein 가수분해물의 Angiotensin Converting Enzyme 저해 효과

  • Hwang, Yu-Jin;Yang, Hui-Jin;Do, Jeong-Ryong;Lee, Su-Won
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • pp.290-293
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    • 2005
  • 장내 단백질 가수분해효소에 의한 casein 분해산물들의 ACE 저해 활성을 비교하기 위하여 인공위액, 인공장액 및 인공위액과 장액 연속처리를 각각 반응조건으로 일정시간 casein을 가수분해한 후 각 효소 가수분해물이 혈압상승 peptide 생성효소인 Angiotensin converting enzyme(ACE)에 대한 저해활성을 측정하였다. 각 소화액에 따른 가수분해물은 모두 ACE 저해활성을 나타내었으며, 2시간 효소처리를 하였을 때, 인공위액, 인공장액, 인공위액과 장액 가수분해물은 각각 69%, 80% 및 88%로 최대 ACE 저해활성을 보였다. 그리고 casein의 가수분해 정도를 확인하기 위한 SDS-PAGE에서는 인공위액으로 처리한 군보다 인공장액으로 처리한 군이 더 작은 분자량으로 분해되는 것을 확인할 수 있었고, 인공위액과 장액을 함께 처리한 군에서는 1시간 안에 대부분의 분해가 이루지는 것을 관찰할 수 있었다.

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Preparation of the Hydrolyzate Using Crab Byproduct after Water Extraction (게의 열수추출 부산물을 이용한 가수분해물의 제조)

  • KIM Young-Myoung;LEE Young-Chul;KOO Jae-Geun;KIM Dong-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.23 no.2
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    • pp.77-86
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    • 1990
  • The residue after hot water extraction of blue crab, Portunus trituberculata, was hydrolyzed for utilizing the byproducts as seasonings. The acid(5N HCl) hydrolyzates were then neutralized with $Na_2CO_3$, 5N NaOH or 5N NaOH hydrolyzate, while the alkali hydrolyzates (5N NaOH) were also neutralized with 5N HCl or 5N HCl hydrolyzate. The total nitrogen and formol nitrogen contents increased, and the platability of the hydrolyzates was also enhanced by neutralization. The released amino acid contents from the neutralized hydrolyzates with $Na_2CO_3$, 5N NaOH and 5N NaOH hydrolyzate were $2,274mg\%,\;2,105.0mg\%$ and $2,683.5mg\%$, respectively. Amino acid contents from the neutralized hydrolyzates with 5N HCl and 5N HCl hydrolyzate were $1,352.5mg\%$ and $2,498.8mg\%$, respectively. In the decolorization of hydrolyzates using decolorization agent, powdered active carbon showed good decolorizing effect. Powdered active carbon decreased total nitrogen and formol nitrogen contents in direct relationship to the increase in its concentration. The effective concentration of active carbon used as decolorization agent showed as $1\~2\%$ of the crab hydrolyzate. Salt contents could be decreased at 37 brix by desalination method such as the evaporation of the hydrolyzate contents.

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Changes of Quality Characteristics of Low-Molecular Soymilk According to Hydrolysis Time (가수분해 시간에 따른 저분자 두유의 품질특성 변화)

  • Jang, Se-Young;Sin, Kyung-A;Park, Nan-Young;Kim, Dong-Hee;Kim, Mi-Jung;Kim, Jeong-Hoon;Jeong, Yong-Jin
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.37 no.10
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    • pp.1287-1293
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    • 2008
  • This study investigated quality changes and functions of low-molecular soymilk according to hydrolysis time (30, 60, and 90 minutes). According to the results, pH of hydrolyzed groups were lower than that of the control group but it did not show a large difference according to hydrolysis time while sugar content was reduced with longer hydrolysis time. Although degree of hydrolysis and calcium tolerance increased with longer hydrolysis time, there was not a significant difference according to the time. Among free sugars, contents of glucose and fructose grew while those of sucrose and maltose tended to decline with time. Total free sugar content was the largest with 60 minutes of hydrolysis time recording 827.65 mg%. Total amino acid content was also the highest with hydrolyzed for 60 minutes recording 85.80 mg% and those of all hydrolyzed groups were higher than that of the control group. In addition, the content of essential amino acid increased significantly with time. In SDS-PAGE, checked for the tendency of becoming low molecules, molecular weights were found to be 33 kDa or less kDa in all hydrolyzed groups. When functional characteristics of soymilk such as electron donating, superoxide radical scavenging and ACE inhibitory activities were compared, longer hydrolysis time led to higher activities. From these results, overall quality of low molecular soymilk was superior when hydrolyzed for 60 minutes and the findings should be viable in the development of various types of functionally strengthened low-molecular soymilk in the future.

Kinetic Studies on Enzymatic Hydrolysis of Cellulose(II) - Evaluation of Several Factors for Enzyme Adsorption and Initial Hydrolysis - (섬유소 가수분해반응에 관한 연구(II) - 효소흡착과 가수분해반응에 관여하는 여러인자의 영향 -)

  • Lee, Yong-Hun;Kim, Chul
    • KSBB Journal
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    • v.6 no.2
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    • pp.167-174
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    • 1991
  • Enzymatic cellulose hydrolysis depends on the several factors such as the structural features (CrI, particle size and surface area, etc.), the nature of cellulase enzyme system, the inhibitory effects of products, and enzyme deactivation. At the presence of products on the initial hydro- lysis rate of cellulose, cellobiose has more severe inhibitory effect than glucose. Othewise, the inhibition effect of products for adsorbed enzyme is related to the glucose and cellobiose conentration hyperbolically. Enzyme deactivation of FPA and ${\beta}-glucosidase$ were expressed by exponential decay profile.

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