• 제목/요약/키워드: enzyme inhibitory activity

검색결과 1,011건 처리시간 0.032초

Rapid Identification of the ${\alpha}$-Glucosidase Inhibitory Compounds from Geranium thunbergii Sieb. et Zucc. by HPLC-micro-fractionation and HPLC-UV-$MS^n$

  • 최세진
    • 한국약용작물학회:학술대회논문집
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    • 한국약용작물학회 2010년도 심포지엄 및 추계학술발표회
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    • pp.430-430
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    • 2010
  • In this study ethanol extracts of aerial part of Geranium thunbergii Sieb. et Zucc. was investigated for their ability to inhibit a-glucosidase, and thus was fractionated using two organic solvents, including dichloromethane, ethyl acetate. The ethyl acetate-soluble fraction, which manifested potent enzyme inhibitory properties, was then followed by tracking down the active compound by combining HPLC micro-fractionation to an enzyme assay in 96-well plate. The ${\alpha}$-glucosidase inhibitory activity profile showed that two peaks exhibited potent inhibitory activity, and then the structural analyses of the two peaks were carried out by HPLC-UV-MS. The main ${\alpha}$-glucosidase inhibitory compounds in the ethyl acetate-soluble fractions of ethanol extracts of Geranium thunbergii Sieb. et Zucc. were tentatively identified as geraniin and kaempferol-7-rhamnoside.

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The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

  • Kim, Sung-Rae;Byun, Hee-Guk
    • Fisheries and Aquatic Sciences
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    • 제15권3호
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    • pp.183-190
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    • 2012
  • The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

ACE-inhibitory Effect and Physicochemical Characteristics of Yogurt Beverage Fortified with Whey Protein Hydrolysates

  • Lim, Sung-Min;Lee, Na-Kyoung;Park, Keun-Kyu;Yoon, Yoh-Chang;Paik, Hyun-Dong
    • 한국축산식품학회지
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    • 제31권6호
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    • pp.886-892
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    • 2011
  • This study investigated the ACE-inhibitory effect of yogurt beverage fortified with hydrolysates as well as the suitability of hydrolysates as a nutraceutical additive to yogurt beverage. Three whey protein hydrolysates hydrolyzed by alcalase, protamex, and trypsin were each added to yogurt beverage at concentrations of 1.25, 2.5, and 5 mg/mL. Yogurt beverage fortified with 2.5 mg/mL of hydrolysates had 61-69% ACE-inhibitory activity, whereas yogurt beverage fortified with 5 mg/mL of hydrolysates showed 74% ACE-inhibitory activity. There were no significant differences in ACE-inhibitory activity between the alcalase or protamex hydrolysates during storage; however, trypsin hydrolysate exhibited significant differences. On the other hand, physicochemical characteristics such as pH (3.47-3.77), titratable acidity (0.81-0.84%), colority, viable cell count, and sensory qualities were not significantly different among the tested yogurt beverage samples during storage. These results showed that yogurt beverage fortified with whey protein hydrolysates maintained antihypertensive activity and underwent no unfavorable changes in physicochemical characteristics regardless of enzyme type.

내산성 Protease에 관한 연구 제2보 조해제에 의한 영향 및 각종기질에 대한 작용성에 대하여 (Studies on the Acid stable Protease from Penicillium sp. Part II. Effect of inhibitor on the proteolytic activity of acid Protease and the Milk clotting activity.)

  • 김상열
    • 한국미생물·생명공학회지
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    • 제1권2호
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    • pp.99-104
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    • 1973
  • A study on the active center of the acid protease from Penicillium sp. was conducted, and also the milk clotting activity of acid prorease was measured. 1. PCMB failed to influence the proteolytic activity of acid protease, indicating that a reactive sulfhydryl group is not required for the enzymatic activity. 2. $\varepsilon$-amino caproic acid did not show any inhibitory effect on tile proteolytic activity of acid protease. 3. Also 2, 4-dinitro phenol did not show any inhibitory effect on the enzyme activity. 4. Acid protease from Penicillium sp. showed a strong milk clotting activity in the presence of Ca ion. 5. This enzyme had a strong proteolytic activity on various substrate, such as casein, denatured hemoglobin, ovalbumin, denatured bovine muscle protein, denatured percine muscle protein and denatured chicken muscle protein.

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The Relationship between Physiological Activity and Cell Number in Dolsan Leaf Mustard Kimchi (Brassica juncea)

  • Park, You-Young;Yoo, Eun-Jeong;Lim, Hyun-Soo;Kang, Dong-Soo;Naoyuki Nishizawa;Park, Myeong-Rak
    • Preventive Nutrition and Food Science
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    • 제6권2호
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    • pp.117-121
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    • 2001
  • Changes in antioxidative activity and Angiotensin converting enzyme(ACE) inhibitory activity in juice prepared from Dolsan leaf mustard kimchi (DLMK) ar various fermentation temperatures were investigated. Antioxidative activity of juice from optimally ripened DLMK at 20 and 3$0^{\circ}C$ showed 80 and 83%, respectively. Juice from 10-day fermented DLMK at 3$0^{\circ}C$ showed 62% inhibitory activity against the ACE. In the juice fermented DLMK at 2$0^{\circ}C$~3$0^{\circ}C$, physiological activity was higher than that of the 4~1$0^{\circ}C$. In particular, optimally ripened DLMK at 3$0^{\circ}C$ showed the highest physiological activity. The physiological activity in DLMK juice at the fermentation period increased significantly with an increase in the growth of microbes. Consequently, a maximum physiological activity was shown at the maximum cell number. These results suggest that the microorganisms in DLMK juice would play an important role in the physiological activity.

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식물성 한약의 Tyrosinase 활성 저해 효과 검색 (1) (Screening of Tyrosinase Inhibitory Activity of Plant Oriental Medicines (1))

  • 황형칠;박종철;강민구;강옥화;권동렬
    • 생약학회지
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    • 제46권1호
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    • pp.84-92
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    • 2015
  • Tyrosinase is a key enzyme to control the biosynthesis of melanin pigments and has two enzyme activities, namely of 1-tyrosine hydroxylase and of 1-dopa oxidase. Thus, tyrosinase is regarded as a target in skin-whitening and therapeutic intervention of local hyperpigmentation diseases. We have tested tyrosinase inhibitory activity on the water extracts of 50 species oriental medicinal plant. Among them, five medicinal plants, Linderae Radix, Clematidis Radix, Cinnamomi Cortex Spissus, Fritillariae Thunbergii Bulbus and Bulbus Fritillariae Cirrhosae were investigated strong inhibition effect. Five medicinal plants were fractionated using organic solvents (methylene chloride, ethyl acetate, n-butanol, water). Cinnamomi Cortex Spissus (ethyl acetate fraction) was investigated strong inhibition effect. Tyrosinase inhibitory activity below $IC_{50}\;40{\mu}g/ml$ is confirmed in five herbal plants that are Linderae Radix, Clematidis Radix, Cinnamomi Cortex Spissus, Fritillariae Thunbergii Bulbus and Bulbus Fritillariae Cirrhosae. Tyrosinase inhibitory levels ($IC_{50}\;{\mu}g/ml$) of each plants were 15.56, 35.02, 25.14, 15.20 and 39.77. We also investigate the effect of effective plant's fraction. in dose of $100{\mu}g/ml$, Cinnamomi Cortex Spissus (P-36) EtOAc fraction significant inhibitory effect over 50%. Clematidis Radix (P-35) and Cinnamomi Cortex Spissus (P-36) MC fraction inhibit tyrosinase each 36.60% and 43.21%. inhibitory rates of Fritillariae Thunbergii Bulbus (P-40) EtOAc and $H_2O$ fraction are 31.40% and 31.51%. Bulbus Fritillariae Cirrhosae (P-45) BuOH fraction regulate tyrosinase activity to 37.71%. We examined tyrosinase inhibitory activity of natural products and these results suggest that several herbs have potential as a new whitening material.

대조 추출물분획이 치은 섬유아세포의 생물학적 활성화에 미치는 영향 (EFFECT OF ZIZYPHI FRUCTUS EXTRACT ON THE BIOLOGICAL ACTIVITY OF GINGIVAL FIBROBLAST)

  • 양창호;이용무;조기영;배기환;정종평
    • Journal of Periodontal and Implant Science
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    • 제24권1호
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    • pp.144-154
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    • 1994
  • Final goal of periodontal treatment is to reconstruct the destructed periodontal tissue as well as to remove the necrotic pathologic elements. The purpose of this study is to investigate on the effect of Zizyphi extract to the inhibitory ability on collagenolytic activity of P gingivalis, biologic activity of gingival fibroblasts, and on the collagen and protein synthesis of gingival fibroblasts. Gingival fibroblast from giniva of first bicuspids from patient for orthodontic treatment were used and cultured. For the measurement of inhibitory ability of collagenolytic activity, crude enzyme was extracted and used on the basis of modified Ono's method. On the inhibition of collagenolytic enzyme from herbal extracts, collagenokit CLN-100 were used. The cellular activity of gingival fibroblast, were studied using MTT solution and measured optical density on 570mm by ELISA reader. To measure the effects on the ability of whole protein and collagen synthesis, cell membrane was destructed with ultrasonic grinder after culturing, centrifuged and counted by liquid scintilation counter. The inhibitory effects on producing of $IL-l{\beta}$ by monocyte, after promotion of producing $IL-l{\beta}$ by LPS, were compared with the mixture of herbal extracts and other drugs using thymocyte stimulation assay. About inhibitory effects of $PGF_2$. by gingival fibroblasts, herbal extract was compared with the addition of the other control groups using enzyme imunoassay. On the inhibition of collagenolytic activity by P. gingivalis, benzene extracts showed the most efficient inhibitory effects among the $19{\mu}g/ml$ of the compared extracts and 40.5% by Tetracycline. On the cellular activity promoting effects, compared extracts showed a bit of more effects than PDGF of $100{\mu}g/ml$ concentration and IGF of $20{\mu}g/ml$ concentration. All of the PDGF, IGF, Zizyphi Fructus extract should increase in collagen synthesis, but especially 70% ethylalcohol extracts of Zizyphi Fructus showed comparably high effects among the compared extracts. Effects on whole protein synthesis were slightly increased on every extract but especially 70% ethylalcohol extract showed significantly effective than any other estract. On the inhibitory effects of Zizyphi Fructus $IL-l{\beta}$ production by monocyte, compared extracts showed 70% of highly inhibitory effect than that of 60% inhibition effects on controlled group and each extracts showed no significant difference. In $PGF_2$ production inhibitroy effect of Zizyphi Fructus gingival fibroblasts, Herbal extracts showed 70% of inhibition comparing with tat of 90.2% of controlled group, but each extracts showed similar effects excluding the $H_2O$ extracts. These results suggested that Zizyphi Fructus might be useful medicine for inhibition of inflammatory mediator including $IL-l{\beta}$ and $PGF_2$.

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Storage Stability of the Synthetic Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Separated from Beef Sarcoplasmic Protein Extracts at Different pH, Temperature, and Gastric Digestion

  • Jang, Ae-Ra;Jo, Cheo-Run;Lee, Moo-Ha
    • Food Science and Biotechnology
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    • 제16권4호
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    • pp.572-575
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    • 2007
  • The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

3D-QSAR of Angiotensin-Converting Enzyme Inhibitors: Functional Group Interaction Energy Descriptors for Quantitative Structure-Activity Relationships Study of ACE Inhibitors

  • Kim, Sang-Uk;Chi, Myung-Whan;Yoon, Chang-No;Sung, Ha-Chin
    • BMB Reports
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    • 제31권5호
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    • pp.459-467
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    • 1998
  • A new set of functional group interaction energy descriptors relevant to the ACE (Angiotensin-Converting Enzyme) inhibitory peptide, QSAR (Quantitative Structure Activity Relationships), is presented. The functional group interaction energies approximate the charged interactions and distances between functional groups in molecules. The effective energies of the computationally derived geometries are useful parameters for deriving 3D-QSAR models, especially in the absence of experimentally known active site conformation. ACE is a regulatory zinc protease in the renin-angiotensin system. Therapeutic inhibition of this enzyme has proven to be a very effective treatment for the management of hypertension. The non bond interaction energy values among functional groups of six-feature of ACE inhibitory peptides were used as descriptor terms and analyzed for multivariate correlation with ACE inhibition activity. The functional group interaction energy descriptors used in the regression analysis were obtained by a series of inhibitor structures derived from molecular mechanics and semi-empirical calculations. The descriptors calculated using electrostatic and steric fields from the precisely defined functional group were sufficient to explain the biological activity of inhibitor. Application of the descriptors to the inhibition of ACE indicates that the derived QSAR has good predicting ability and provides insight into the mechanism of enzyme inhibition. The method, functional group interaction energy analysis, is expected to be applicable to predict enzyme inhibitory activity of the rationally designed inhibitors.

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헤이즐넛 첨가에 따른 청국장의 품질 특성 변화 (Changes in the Quality Characteristics of Cheonggukjang prepared with Hazelnut)

  • 김종덕;이영현;이난희;김대현;최웅규
    • 한국식품영양학회지
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    • 제31권6호
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    • pp.926-932
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    • 2018
  • This research was conducted to investigate the changes in quality characteristics of cheonggukjang fermented with the addition of hazelnut (10, 20, 30 and 40%) including; water content, pH, hydrophilic and lipophilic substances, color, viscosity and angiotensin converting enzyme inhibition activity. There was no significant change in pH with the addition of hazelnut. The water content significantly decreased with the addition of hazelnut. Hazelnut was also found to brighten the color of cheonggukjang. L-value and b-value increased with the addition of cheonggjuang. There was an insignificant change in the a-value. There was a slight decrease in the content of hydrophilic with addition of hazelnuts. Where there was more than 20% addition of hazelnut to soybean, the viscous substance content in cheonggukjang decreased significantly. Angiotensin converting enzyme inhibitory activity increased proportionally to the amount of hazelnut added. It was identified that the addition of 40% of hazelnut made its angiotensin converting enzyme inhibitory activity 10% point higher than that of control. These results suggests that the addition of hazelnut makes it possible to produce cheongkukjang of excellent angiotensin converting enzyme inhibitory activity.