• 제목/요약/키워드: pepsin hydrolysis

검색결과 66건 처리시간 0.031초

번데기 가수분해물의 ACE 저해활성과 항산화활성 (ACE Inhibitory and Antioxidative Activities of Silkworm Larvae (Bombyx mori) Hydrolysate)

  • 유정식;우관식;황인국;이연리;강태수;정헌상
    • 한국식품영양과학회지
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    • 제37권2호
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    • pp.136-140
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    • 2008
  • 번데기 단백질의 최적 가수분해 조건을 선정하기 위해 4종의 가수분해 효소를 이용하여 번데기분말 첨가량별 및 가수분해시간에 따른 단백질 용해지수, 각각의 가수분해물의 ACE 저해활성 및 항산화활성 등을 조사하였다. 탈지번데기 분말의 최적 분산농도는 $5{\sim}10%$ 범위였으며 가수분해시간은 18시간이었고, ACE 저해활성은 neutrase, trypsin, pepsin 및 alcalase 효소처리 시 각각, 85.16, 83.46, 70.45 및 65.39%로 모든 효소 처리구가 비효소 처리구(24.94%)에 비해 높은 활성을 나타내었다. 가수분해물의 항산화활성($IC_{50}$)은 상업용 효소인 neutrase와 alcalase의 경우 각각 352.75 및 $396.09\;{\mu}g/mL$로 비효소처리구($327.24\;{\mu}g/mL$)와 유사한 값을 보였고, pepsin 및 trypsin은 각각 626.09 및 $677.44\;{\mu}g/mL$로 비효소처리구보다 낮게 나타났다.

인삼(人蔘) 사포닌을 비롯한 계면활성제(界面活性劑)가 위장관내(胃腸管內)의 단백질(蛋白質) 가수분해효소(加水分解酵素) 반응(反應)에 미치는 영향(影響) (The Effects of Surfactants Including Ginseng Saponins on the Gastric Enzyme-Catalyzed Hydrolysis)

  • 김영재;이상직;박기태
    • 대한한의학회지
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    • 제27권2호
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    • pp.103-110
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    • 2006
  • Objectives : This study was conducted to investigate the effects of ginseng saponins and commercial surfactants such as Triton X-100, sodium deoxycholate, and sodium dodecyl sulfate on the gastric enzyme-catalyzed hydrolysis. Methods : Saponins (a surface-active plant component) from fresh ginseng root were extracted to examine its effect on the gastric enzyme-catalyzed hydrolysis. Commercial surfactants such as Triton X-100, sodium deoxycholate, and sodium dodecyl sulfate were also employed in the hydrolysis system to compare their effects with that of the ginseng saponins. The effects of surfactants on the gastric enzyme-catalyzed hydrolysis were measured by using a spectrophotometer. A spectropolarimeter was used to examine the conformational change of enzymes and substrates by the addition of ginseng saponins into the system. Results : Both the tryptic and the peptic digestion of milk casein or eggalbumin were slightly improved with an increase in the amount of ginseng saponins in the system. Triton X-100 showed an effect similar to that of ginseng saponins, while sodium dodecyl sulfate and sodium deoxycholate diminished the hydrolysis. Circular dichroism spectra of enzymes and substrates was significantly changed by the addition of ginseng saponins into the system. Conclusions : These results show that ginseng saponins affect positively the gastric enzyme-catalyzed hydrolysis, and suggest that the digestion of substrates by gastric enzymes is affected by the change of enzyme conformation by ginseng saponins.

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Antioxidant and antimicrobial activities of different enzymatic hydrolysates from desalted duck egg white

  • Thammasena, Rommanee;Liu, Deng Cheng
    • Asian-Australasian Journal of Animal Sciences
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    • 제33권9호
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    • pp.1487-1496
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    • 2020
  • Objective: The objective of this study was to look for optimal preparation of hydrolysates of desalted duck egg white powder (DDEWP) by the three different proteases and to investigate their antioxidant and antimicrobial properties. Methods: DDEWP was hydrolyzed by three proteases, including pepsin (PEP), Bacillus spp. (BA) and natokinase (NAT) with three different enzyme concentrations (0.1%, 0.3%, and 0.5%), individually. The important key hydrolysis parameters such as hydrolysis degree, yield, antioxidant and antimicrobial activity were evaluated in this experiment. Results: The results showed that the degree of hydrolysis (DH) of all treatments increased with increasing hydrolysis time and protease concentrations. The antioxidant and antimicrobial activities of the hydrolysates were affected by type and concentration of protease as well as hydrolysis time. Hydrolysis of PEP significantly (p<0.05) obtained the highest yield of hydrolysates, however, both of BA and NAT showed substantially lower DH values and still did not exceed 5% by the end of hydrolysis. Among the different hydrolysates, PEP exhibited significantly higher 2, 2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity than BA and NAT. All DDEWP hydrolysates from PEP had low ferrous ion chelating activity (<37%) that was significantly lower than that of NAT (>37% to 92%) and BA (30% to 79%). Besides, DDEWP hydrolysates of PEP presented significantly higher reducing power than BA and NAT. In antimicrobial activities, Escherichia coli, Salmonella typhimurium, and Pseudomonas aeruginosa were not effectively inhibited by any DDEWP hydrolysates of PEP except for Staphylococcus aureus. Especially, the excellent antibacterial activity against S. aureus only was displayed in DDEWP hydrolysates of PEP 0.1%. Conclusion: DDEWP hydrolysates from PEP demonstrated significantly better DH, yield, DPPH radical scavenging activity and reducing power, furthermore, had excellent inhibitory on S. aureus due to large clear zone and moderated inhibitory in bactericidal inhibition.

상업적 응유효소의 탈지유에 대한 단백질 분해 작용 (Comparative Study of Proteolytic Activities of Some Commercial Milk Clotting Enzymes on Bovine Skim Milk)

  • 신현수;김상범;임종우
    • Journal of Animal Science and Technology
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    • 제44권6호
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    • pp.801-808
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    • 2002
  • 상업적 단백질 분해 효소에 0.02% $CaCl_2$를 첨가하여 응유 활성화를 시킨 탈지유에 대한 분해 작용의 결과를 요약하면 다음과 같다. 다양한 효소별 가수분해 시간에 따른 가수분해도는 미생물 유래 효소와 trypsin은 pepsin과 papain W-40보다 높은 분해도를 나타냈다. 12% TCA 용액에 가용성인 NPN의 양은 trypsin이 가장 높은 분해도를 나타내었고 rennet과 pepsin이 가장 낮은 분해도를 보였다. 전기영동에 있어서 trypsin과 protease S는 $\alpha$- lactalbumin을 분해하였고 papain w-40은 $\beta$- lactoglobulin을 미약하게 분해하였으며 neutrase 1.5는 90분 이후부터 $\alpha$-lactalbumin과 $\beta$-lactoglobulin을 분해하였다. Rennet과 비교한 전기영동상에서는 rennet에 의해 분해 되지 않은 ${\alpha}_s$- casein과 $\beta$-casein을 trypsin과 protease S가 다량 분해하였고 $\kappa$-casein은 rennet에 비해 papain W-40이 상당 수준의 분해상을 나타내었다. 이상의 결과 가수분해도 및 NPN 양은 trypsin, neutrase 1.5 및 protease S가 다른 효소에 비해 높게 나타났으며, 전기영동상에서는 pepsin과 neutrase 1.5가 rennet과 유사한 경향을 나타내었다.

Purification of a Novel Anticancer Peptide from Enzymatic Hydrolysate of Mytilus coruscus

  • Kim, Eun-Kyung;Joung, Hong-Joo;Kim, Yon-Suk;Hwang, Jin-Woo;Ahn, Chang-Bum;Jeon, You-Jin;Moon, Sang-Ho;Song, Byeng Chun;Park, Pyo-Jam
    • Journal of Microbiology and Biotechnology
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    • 제22권10호
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    • pp.1381-1387
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    • 2012
  • We applied enzymatic hydrolysis and tangential flow filtration (TFF) to purify a novel anticancer peptide from Mytilus coruscus (M. coruscus) and investigated its anticancer properties. To prepare the peptide, eight proteases were employed for enzymatic hydrolysis. Pepsin hydrolysates, which showed clearly superior cytotoxic activity on prostate cancer cells, were further purified using a flow filtration system using a TFF and consecutive chromatographic methods. Finally, a novel anticancer peptide was obtained, and the sequence was identified as Ala-Phe-Asn-Ile-His-Asn-Arg-Asn-Leu-Leu. The peptide from M. coruscus effectively induced cell death on prostate, breast and lung cancer cells but not on normal liver cells. This is the first report of an anticancer peptide derived from the hydrolysates of M. coruscus.

Dephosphorylation of Phytate from Rice Bran and Soybean Meal Using Phytases from Aspergillus sp. 5990

  • Kim Jong Soon;Kim Doo-Sang;Kim Hyeng-Rak;Shin Tai-Sun;Kim Heung-Yoon;Oh Myong-Joo;Byun Dae-Seok
    • Fisheries and Aquatic Sciences
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    • 제7권2호
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    • pp.51-57
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    • 2004
  • Total phosphorus contents in rice bran and soybean meal were determined to be 5.81 and $2.77\%$, respectively, and $97.2\%$ of phosphorus in rice bran and $66.4\%$ in soybean meal were presented as phytate phosphorus. Optimum pH condition for hydrolysis of phytate in rice bran and soybean was determined to be in the pH range of 3.7 and 5.3. The highest activity of phytase for hydrolysis of phytate in both samples was determined to be at $55^{\circ}C$ for rice bran and $55-60^{\circ}C$ for soybean. Hydrolysis of phytate in soybean meal at pH 5.0 increased with the co-reaction or consecutive reaction with protease; however, in rice bran hydrolysis decreased with co-reaction with protease. Phytate degradation of soybean meal in the presence of pepsin at pH 2.5 showed higher than that of rice bran. Phytate degradation of rice bran in the presence of trypsin or pancreatin at pH 7.0 increased the activity around 2-times compared with the activity in the absence of trypsin or pancreatin. The results of this study suggest that hydrolysis of phytate in rice bran or soybean meal with phytase and protease may provide an alternative process for the preparation of aquacultural feed with a low level of organic phosphorus.

비스페놀A 유도 간 손상 마우스에서 해삼(Stichopus japonicas) 추출물 및 가수분해물의 간 기능 개선 효과 (Extracts and Enzymatic Hydrolysates Derived from Sea Cucumber Stichopus japonicas Ameliorate Hepatic Injury in BisphenolA-treated Mice)

  • 김세정;조윤호;박비오;유대석;김두호;김민정;곽연길;김진성
    • 한국해양바이오학회지
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    • 제14권2호
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    • pp.61-68
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    • 2022
  • This study aimed to investigate the hepatoprotective activities of the sea cucumber products, including extracts and hydrolysates, in vitro and in vivo. Dried sea cucumber, produced on the western coast of Korea, was boiled in water or 70% ethanol at 85℃ or 100℃ for 18 or 24 h, respectively, to extract bioactive compounds. The enzymatic hydrolysates were prepared by reacting the dried sea cucumber with pepsin or neutral protease (PNL) under optimal enzyme conditions. The anti-inflammatory effect of the samples was investigated using RAW 264.7 cells treated with lipopolysaccharide (LPS). The amount of nitric oxide (NO) was produced from the cells treated with LPS and each sample was compared. Therefore, the pepsin hydrolysate treatment decreased NO production compared to LPS sole treatment. Furthermore, the effects of the samples on cell injury in the hepatic cell line and bisphenolA-induced hepatic injury mouse model were investigated. The water extracts and the pepsin hydrolysates of sea cucumber significantly inhibited cell injury generated in the hepatocytes without cytotoxicity (p < 0.05), whereas the ethanol extracts were cytotoxic. However, these results indicate that the extracts and the enzymatic hydrolysates derived from sea cucumber can be used as beneficial materials for inhibiting liver damage.

멸치육 단백질 효소가수분해물의 항산화작용 (Antioxidative Activity of Enzymatic Hydrolysates Derived from Anchovy Muscle Protein)

  • 염동민;이태기;박영호;김선봉
    • 한국수산과학회지
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    • 제30권5호
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    • pp.842-849
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    • 1997
  • Pepsin, trypsin, $\alpha-chymotrypsin$, papain, bromelain, 복합효소, Novozym 89, Neutrase 0.51., Protamex 및 Alcalase 0.6L 등으로 가수분해하여 얻은 멸치육 단백질 효소 가수분해물의 항산화작용을 살펴본 결과, 항산화작용이 매우 우수한 것으로 나타났으며 특히 생체내 소화효소의 하나인 pepsin과 식품가공용 단백분해효소인 Protamex에 의한 가수분해물의 항산화작용이 우수한 것으로 나타났다. 이들의 다른 항산화제와의 상승작용에 있어서는 $\alpha-tocopherol$과는 상승작용이 있는 것으로 나타났으나 BHT에 대해서는 BHT 자체의 강한 항산화능으로 상승작용을 확인할 수 없었다. 금속이온 $(Fe^{3+},\;Cu^{2+})$에 대한 봉쇄작용 또한 우수한 것으로 나타났으며, 특히 pepsin, $\alpha-chymotrypsin$ 및 papain유래 가수분해물이 $Cu^{2+}$이온에 대하여 높은 억제작용을 나타내었다. Pepsin유래 멸치육 단백질 효소가수분해물을 이온교환크로마토그래피 및 겔 크로마토그래피에 의하여 분획하고 얻어진 획분별 항산화작용은 P-2 (fraction No. $26\~31$)획분에서 가장 큰 것으로 나타났다. 이 때 가수분해전후 및 활성획분의 아미노산조성은 aspartic acid와 glutamic acid가 증가한 반면 alanine, cysteine, tyrosine 및 phenylalanine은 감소한 것으로 나타났다.

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멸치육 단백질 효소가수분해물로부터 Angiotensin-I 전환효소 저해제의 분리 및 그 특성 (Isolation and Characteristics of Angiotensin-I Converting Enzyme Inhibitory Activity of Peptic Hydrolyzates of Anchovy Muscle Protein)

  • 김선봉;이태기;박영범;염동민;김외경;도정룡;박영호
    • 한국수산과학회지
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    • 제27권1호
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    • pp.1-6
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    • 1994
  • 수산식품중에 함유되어 있는 기능성 물질의 계통적 해석을 위한 연구의 일환으로 소화효소에 의한 멸치육 단백질 가수분해물의 angiotensin-I 전환효소(ACE) 저해물질을 추출, 분리하여 이들 각 획분들의 특성에 대하여 살펴보았다. 그 결과를 요약하면 다음과 같다. 1. 가수분해에 따른 ACE 저해효과는 pepsin에 의하 멸치육 단백질 가수분해물에 있어서는 peptide-nitrogen의 생성량이 급격히 증가한 가수분해 20시간째에 가장 우수한 것으로 나타났다. 2. Gel 여과에 의하여 분리된 멸치육 단백질 가수분해물의 획분별 ACE 저해작용을 검토한 결과, 획분 2와 4가 ACE 저해작용이 우수하여 이들을 rechromatography하여 분리한 단일획분인 2'와 4'획분의 $IC_{50}$은 각각 45, $76{\mu}g$인 것으로 나타났다. 3. 분리한 단일 획분인 2'와 4'획분의 아미노산 조성은 다소 차이가 있었으며, 2'획분은 glutamic acid, leucine 및 lysine의 함량이 많은 것으로 나타났으며, 4'획분은 aspartic acid와 threonine의 함량이 많은 것으로 나타났다.

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토끼 항 ${\alpha}-Lactalbumin$ 항혈청에 대한 유청단백질 가수분해물의 항원성 (Antigenicity of Whey Protein Hydrolysates Against Rabbit Anti ${\alpha}-Lactalbumin$ Antiserum)

  • 하월규;전석락;김정완;이수원;이재영;손동화
    • 한국식품과학회지
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    • 제26권4호
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    • pp.436-441
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    • 1994
  • Chymotrypsin, trypsin, pancreatin, 그리고 Aspergillus oryzae 유래 단백질분해효소의 in vitro처리에 의하여 유청단백질(WPI)의 가수분해물(WPH)중 ${\alpha}-LA$ 유래의 항원성변화를 조사하기 위하여 토끼 항 ${\alpha}-LA$ 항혈청을 이용한 competitive inhibition ELISA(cELISA)와 heterologous PCA를 실시하였다. cELISA에 의하여 WPH의 monovalent항원성을 분석한 결과, pepsin전처리는 chymotrypsin, trypsin 그러고 pancreatin 가수분해물의 항원성을 더욱 감소시키는 효과가 있었으며, 열 전처리는 Asp. oryzae 유래효소 및 trypsin 가수분해물의 항원성을 더욱 감소시켰다 전체적으로 ${\alpha}-LA$유래의 monovalent 항원성은 효소처리에 의하여 $10^{-2.5}-10^{-5.5}$배 또는 그 이하로 저하되었으며, 특히 열 및 pepsin 전처리후 trypsin으로 가수분해한 경우(TDP)의 항원성은 거의 상실되었다. WPH의 가수분해도와 ${\alpha}-LA$유래의 monovalent 항원성 감소는 그다지 일치하지 않았다. Guinea pig를 이용한 PCA test에 의하여 ${\alpha}-LA$유래의 polyvalent 항원성을 분석한 결과 WPI 및 ${\alpha}-LA$는 양성으로 높게 나타났으나, WPH는 전처리유무에 관계없이 모두 음성으로 나타났다. 이는 WPI의 가수분해로 생성된 ${\alpha}-LA$유래의 peptide가 특이항체와 결합은 가능하나 생체내에서 알레르기를 유발하지 않음을 뜻하였다. 따라서, 유청단백질을 효소로 가수분해하면 유청단백질중 ${\alpha}-LA$의 allergenicity는 쉬 파괴됨을 알 수 있었다.

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