• 제목/요약/키워드: Enzymatic Activity

검색결과 1,472건 처리시간 0.022초

사과농축액에 대한 갈변억제제 처리효과 (The Effect of Antibrowning Agents on Enzymatic Reaction in Apple Concentrate)

  • 김현위;배수경
    • 한국식품과학회지
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    • 제34권3호
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    • pp.454-458
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    • 2002
  • 과실가공품에서의 갈변을 억제하기 위하여 사과농축액에 갈변억제제 즉, PVPP (polyvinylpolypyrrolidone), bentonite, gelatin, celite 545, tannic acid, sodium sulfite를 첨가하여 여과한 후 갈변억제효과를 측정하였다. 색도의 변화는 PVPP를 첨가한 농축액에서 L값(lightness)이 8.16으로 대조구와 다른 농축액에 비해 갈변억제에 효과가 있음을 알 수 있었으며, 탁도(660 nm에서의 흡광도)는 대조구 0.05인데 비해, PVPP, gelatin celite 545, tannic acid, sodium sulfite를 함유한 사과농축액은 각각 0.003, 0.038, 0.038, 0.018, 0.022로 다소 낮은 수치를 보여 부유물 등의 제거효과가 나타났으며 특히 PVPP의 효과가 뚜렷하였다. 또한, PVPP 처리된 사과농축액 중의 PPO(polyphenoloxidase)활성과 폴리페놀화합물(catechol, catechin, chlorogenic acid, epicatechin 등) 함량에서도 현저하게 감소하여 효소적 갈변이 억제되었음을 알 수 있었다. 따라서, PVPP가 사과농축액의 색상, 탁도, PPO활성 및 폴리페놀화합물 함량 등 효소적 갈변특성을 개선시키는 우수한 갈변억제제임을 확인하였다.

Enzymatic Activities of Allergen Extracts from Three Species of Dust Mites and Cockroaches Commonly Found in Korean Home

  • Jeong, Kyoung-Yong;Kim, Chung-Ryul;Yong, Tai-Soon
    • Parasites, Hosts and Diseases
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    • 제48권2호
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    • pp.151-155
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    • 2010
  • Allergen extracts from dust mites and cockroaches commonly found in Korean homes were used to evaluate their enzymatic activity as they are believed to influence allergenicity. Allergen extracts were prepared from 3 dust mite species (Dermatophagoides farinae, D. pteronyssinus, and Tyrophagus putrescentiae) and 3 cockroach species (Blattella germanica, Periplaneta americana, and P. fuliginosa) maintained in the Korea National Arthropods of Medical Importance Resource Bank. Proteins were extracted in PBS after homogenization using liquid nitrogen. The activities of various enzymes were investigated using the API Zym system. No significant difference in phosphatase, lipase, or glycosidase activity was observed among the 6 allergen extracts, but much difference was observed in protease activity. Protease activity was assessed in more detail by gelatin zymography and the EnzChek assay. Extract from T. putrescentiae showed the highest protease activity, followed by those of the cockroach extracts. Extracts from D. farinae and D. pteronyssinus showed only weak protease activity. Gelatinolytic activity was detected mainly in a 30-kDa protein in D. farinae, a 28-kDa protein in D. pteronyssinus, a > 26-kDa protein in T. putrescentiae, a > 20-kDa protein in B. germanica, and a > 23-kDa protein in P. americana and P. fuliginosa. The information on various enzymatic activities obtained in this study may be useful for future studies. In particular, the strong protease activity found in cockroach extracts could contribute to sensitization to cockroach allergens, which is known to be associated with the development of asthma.

Immobilization of Lipase using Alginate Hydrogel Beads and Enzymatic Evaluation in Hydrolysis of p-Nitrophenol Butyrate

  • Zhang, Shuang;Shang, Wenting;Yang, Xiaoxi;Zhang, Shujuan;Zhang, Xiaogang;Chen, Jiawei
    • Bulletin of the Korean Chemical Society
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    • 제34권9호
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    • pp.2741-2746
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    • 2013
  • The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.

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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배양 간세포 (Chang)에서 황산화작용 및 항상화요소 활성에 미치는 계란 놀느자 단백질 가수분해물의 영향 (Effect of Enzymatic Hydrolysate from Egg Yolk Protein on the Activity of Antioxidative Enzyme in Cultured Hepatocytes (Chang))

  • 박표잠;송병권;남경수;김세권
    • 생명과학회지
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    • 제10권5호
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    • pp.475-483
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    • 2000
  • Normally, aerobic cells are protected from the damage of free radicals by antioxidative enzymes such as catalase, superoxide dismutase (SOD), glutathione (GSH) peroxidase and GSH-S-transferase. In this study, we have investigate the effect of egg yolk protein hydrolysates on antioxidative activity and the activity of antioxidative enzyme in cultured hepatocytes (Chang). Without the pretreatment with hydrolysate, about 50% of the hepatocytes were killed within 2h by 225$\mu$M tert-butyl hydroperoxide (t-BHP). By contrast, fewer than 20% of the 5 K hydrolysate (permeate from 5 kDa membrane and not passed through 1 kDa membrane)-pretreated hepatocytes were killed by the same concentrations of t-BHP. In addition, the activities of catalase, GSH peroxidase and GSH-transferase were significantly increasing with the treatment of 5 K hydrolysate. These results suggest that 5 K hydrolysate exerts antioxidative effect by increasing activity of antioxidative enzymes.

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개조개(Veneridae Saxidomus purpuratus Sowerby)의 소화효소에 대하여 (제 2 보) Proteinase의 효소적성질 (Studies on the Digestive Enzymes of Veneridae Soxidomus burpuratus Sowerby II)

  • 서석수;양한석;홍승철
    • 약학회지
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    • 제4권1호
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    • pp.39-42
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    • 1959
  • The enzymatic activity of proteinase which was isolated from a shell fish, Veneridae Soxidomus purpuratus Sowerby(Korean name "Gai-jo-gai") was studied, and the obtained results were as follows; (1) The optimum pH of the enzyme was around 7.5 (2) The prohibiting activity of metalic ions for the enzymatic activity was the order of 1/1000M-$Ag^{+}$>1/1000M-$Zn^{++}$>1/1000M-$Cd^{++}$>1/1000M-$Pb^{++}$. (3) Of 3 specimens of the enzyme from heptapancreas, gastro-intestine and crystalline style the highest activity was shown by one from crystalline style.

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레시틴 추출 잔사인 계란노른자의 효소적 단백질 가순분해물의 항산화 특성 (Antioxidative Effect of Enzymatic Protein Hydrolysate from Lecithin-Free Egg Yolk)

  • 박표잠;정원교;최영일;김세권
    • 생명과학회지
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    • 제10권2호
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    • pp.131-139
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    • 2000
  • Lecithin-free egg yolk protein (EYP), the by-product of lecithin extraction from egg yolk, which is denatured with an organic solvent, would normally be discarded. In this study, the denatured protein was renatured with alkali, and hydrolyzed with Alcalase in order to utilize by-product. The hydrolysate was separated through a series of ultrafiltration membranes with molecular weight cut-off (MWOO) of 10, 5 and 1 kDa, and the antioxidative activities of the hydrolysates was investigated. The 5K hydrolysate, permeate from 5 kDa membrane, showed stronger antioxidative activity than 10 K and 1 K hydrolysate which were permeated from 10 kDa and 1 kDa membrane, in a linoleic acid autoxidation system. In addition, the optimum concentration of antioxidative activity for 5 K hydrolysate was 1%, and the activity was about 37% higher as compared with α-tocopherol. The synergistic effect was also increased by using the hydrolysates with α-tocopherol.

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Induction of Indoleamine 2,3-dioxygenase (IDO) Enzymatic Activity Contributes to Interferon-Gamma Induced Apoptosis and Death Receptor 5 Expression in Human Non-small Cell Lung Cancer Cells

  • Chung, Ting Wen;Tan, Kok-Tong;Chan, Hong-Lin;Lai, Ming-Derg;Yen, Meng-Chi;Li, Yi-Ron;Lin, Sheng Hao;Lin, Chi-Chen
    • Asian Pacific Journal of Cancer Prevention
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    • 제15권18호
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    • pp.7995-8001
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    • 2014
  • Interferon-gamma (IFN-${\gamma}$) has been used to treat various malignant tumors. However, the molecular mechanisms underlying the direct anti-proliferative activity of IFN-${\gamma}$ are poorly understood. In the present study, we examined the in vitro antitumor activity of IFN-${\gamma}$ on two human non-small-cell lung carcinoma (NSCLC) cell lines, H322M and H226. Our findings indicated that IFN-${\gamma}$ treatment caused a time-dependent reduction in cell viability and induced apoptosis through a FADD-mediated caspase-8/tBid/mitochondria-dependent pathway in both cell lines. Notably, we also postulated that IFN-${\gamma}$ increased indoleamine 2,3-dioxygenase (IDO) expression and enzymatic activity in H322M and H226 cells. In addition, inhibition of IDO activity by the IDO inhibitor 1-MT or tryptophan significantly reduced IFN-${\gamma}$-induced apoptosis and death receptor 5 (DR5) expression, which suggests that IDO enzymatic activity plays an important role in the anti-NSCLC cancer effect of IFN-${\gamma}$. These results provide new mechanistic insights into interferon-${\gamma}$ antitumor activity and further support IFN-${\gamma}$ as a potential therapeutic adjuvant for the treatment of NCSLC.

엿기름의 효소활성과 관련한 보리의 품질특성 (Quality Characteristics of Barley Varieties Related to Enzymatic Activity in Malt)

  • 이영택;서세정;장학길
    • 한국식품과학회지
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    • 제31권6호
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    • pp.1421-1426
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    • 1999
  • 엿기름의 품질 요소인 당화력(DP)은 보리품종에 따라 큰 차이를 나타내 $139{\sim}220^{\circ}L$의 범위에 있었다. 당화력은 ${\alpha}-amylase$ 보다 ${\beta}-amylase$와 높은 상관관계가 있어 엿기름의 ${\beta}-amylase$ 활성이 매우 중요한 인자였으며, 엿기름 첨가에 따른 amylograph 전분기질 점도 감소는 ${\alpha}-amylase$와 관련이 있는 것으로 확인되었다. 보리품종들의 품질요소들을 분석하여 엿기름 당화력과의 상관관계를 조사한 결과 엿기름의 당화력은 원맥의 품질인자와 상관관계가 별로 높지 않았으나 중량이 낮은 품종이나 덜 풍만한 품종에서 당화력이 높은 경향을 보여주었다. 보리원맥이 지니고 있는 ${\beta}-amylase$ 활성은 엿기름의 당화력과 상관관계가 있는 것으로 평가되었으며 엿기름의 당화력을 예측할 수 있는 잠재적인 당화력으로서 엿기름 제조에 매우 유용한 품질인자인 것으로 판단되었다.

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Identification of ${\gamma}-Glutamylamine$ Cyclotransferase, as the Preform Enzyme at the Dormant Stage, From Soybean (Glycine max) Seeds

  • Kang, Hyeog;Park, Sung-Joon;Cho, Young-Dong
    • BMB Reports
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    • 제30권6호
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    • pp.438-442
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    • 1997
  • ${\gamma}-Glutamylamine$ cyclotransferase was purified to homogeneity from soybean (Glycine max) seeds. To our knowledge, it is the first purification of the enzyme from plant origins. The molecular weight of the enzyme estimated by Sephacryl S-300 gel filtration and SDS-PAGE was 27,000, indicating that the enzyme is a monomer. The optimal pH for activity was 8.6. The Km value for ${\gamma}-glutamyldansylcadaverine$ was 11 ${\mu}M$. The enzymatic activity was substantially inhibited by the addition of p-chloromercuribenzoate and partially inhibited by the $Cu^{2+}$ ion. However, neither other modification reagents nor other divalent metal ions affected the enzymatic activity. The comparison between the enzymatic activities of seed extracts treated with cycloheximide and control extracts, and the detection of the same single protein band by western blot analysis at the dormant stage without inhibition with distilled water indicate that ${\gamma}-Glutamylamine$ cyclotransferase is already present at the dormant stage and gradually activated during germination in soybean seeds.

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