• 약학회지
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• 제46권6호
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• pp.387-391
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• 2002

In vitro $\beta$-lactamase inhibitory activity of 6-exomethylene sulbactam compounds (CH-120, 130, 140, 145, 150, 155) was compared with clavulanic acid, sulbactam and tazobactam. The inhibitory activity of CH-140 was stronger than sulbactam and clavulanic acid against Type II, III, IV, TEM enzymes and stronger than tazobactam against Type IV enzyme. The inhibitory activity of CH-145 was stronger than sulbactam and clavulanic acid against Type I, II, III, IV, TEM enzymes and stronger than tazobactam against Type III, IV enzymes. The in vitro antimicrobial activity of CH-140 and CH-145 combined with piperacillin and ceftriaxone was compared with the sulbactam and tazobactam against $\beta$-lactamase producing 31 strains. But, synergistic activity of CH-140 and CH-145 was inferior to tazobactam.

• 한국축산식품학회지
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• 제43권1호
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• pp.46-60
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• 2023

Slaughterhouse blood is a by-product of animal slaughter that can be a good source of animal protein. This research purposed to examine the functional qualities of the blood plasma from Hanwoo cattle, black goat, and their hydrolysates. Part of the plasma was hydrolyzed with proteolytic enzymes (Bacillus protease, papain, thermolysin, elastase, and α-chymotrypsin) to yield bioactive peptides under optimum conditions. The levels of hydrolysates were evaluated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis. The antioxidant, metal-chelating, and angiotensin I-converting enzyme (ACE) inhibitory properties of intact blood plasma and selected hydrolysates were investigated. Accordingly, two plasma hydrolysates by protease (pH 6.5/55℃/3 h) and thermolysin (pH 7.5/37℃/3-6 h) were selected for analysis of their functional properties. In the oil model system, only goat blood plasma had lower levels of thiobarbituric acid reactive substances than the control. The diphenyl picrylhydrazyl radical scavenging activity was higher in cattle and goat plasma than in proteolytic hydrolysates. Ironchelating activities increased after proteolytic degradation except for protease-treated cattle blood. Copper-chelating activity was excellent in all test samples except for the original bovine plasma. As for ACE inhibition, only non-hydrolyzed goat plasma and its hydrolysates by thermolysin showed ACE inhibitory activity (9.86±5.03% and 21.77±3.74%). In conclusion, goat plasma without hydrolyzation and its hydrolysates can be a good source of bioactive compounds with functional characteristics, whereas cattle plasma has a relatively low value. Further studies on the molecular structure of these compounds are needed with more suitable enzyme combinations.

• 생명과학회지
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• 제20권5호
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• pp.768-774
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• 2010

전통발효주 막걸리의 기능성을 증명하기 위하여 S사막걸리로부터 구입한 막걸리 침전물의 여러 가지 생리활성에 대하여 조사하였다. 우선 막걸리 침전물 열수 추출물의 항산화 효과를 측정하기 위해 DPPH radical 소거능과 SOD 유사활성을 측정하였다. 그 결과 DPPH법을 통해 측정한 막걸리 침전물 열수 추출물의 radical 소거능은 10 mg/ml에서 48.0%으로 나타났으며, 농도가 증가함에 따라 유의적으로 증가하는 경향을 나타내었다. 또한 SOD 유사활성은 10 mg/ml 농도에서 98.7%로 비교적 높은 SOD 유사활성을 보였다. 항고혈압 활성 측정 실험에서는 현재 시판되고 있는 항고혈압제인 captopril은 0.1 mg/ml에서 93.4%의 ACE 억제효과가 나타났고, 막걸리 침전물 열수 추출물 10 mg/ml에서는 74.0%의 높은 저해 활성을 나타내었다. 따라서, 막걸리 침전물 열수 추출물은 인체에 부작용이 적은 천연 항고혈압소재로서 이용가능성이 높은 것으로 사료된다. 아질산염 소거능 측정 실험에서는 positive control인 Vit. C1 mg/ml의 경우 pH 1.2와 3.0에서는 74~64%, pH 6.0에서는 45%의 소거능을 보인반면, 막걸리 침전물 열수 추출물의 경우 pH 1.2와 3.0에서는 51~42%, pH 6.0에서는 28%의 소거능을 나타내었다. 막걸리 침전물 열수 추출물의 숙취해소 효능은 ADH와 ALDH 활성증진에 막걸리 침전물 열수 추출물이 미치는 영향을 조사함으로써 증명하고자 하였다. 그 결과, 알콜과 acetaldehyde 분해능은 높게 나타났다. 이상의 결과들은 막걸리 침전물의 우수한 기능성으로서의 이용 가능성에 대한 기초자료로 그 가치가 기대된다.

• Journal of Animal Science and Technology
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• 제47권1호
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVI)
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• pp.566-569
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• 2005

tyrosinase 저해 활성 실험 결과 1.2%(w/v) 이상의 농도에서 70% 이상의 저해를 나타내 색소침착에 대한 기능성 화장품 원료로 사용이 가능할 것으로 보이며, ACE 저해 활성 실험에서 1.5% 농도에서 60% 가량의 저해활성을 보여 혈관 변형 치료 및 예방에 효과가 있을 것으로 기대된다. UV 흡수능에서는 UV-B, UV-C의 영역에서 흡수 경향을 나타내며 자외선 차단제의 원료로 사용이 가능할 것으로 기대되며, 또한 bead 형성능을 가지고 있어 약물전달체로서 이용 가능성이 기대된다.

• Preventive Nutrition and Food Science
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• 제19권4호
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• pp.274-280
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• 2014

The purpose of this study was to investigate the biological activities of cultivated Angelica gigas Nakai (CAG) and wild Angelica gigas Nakai (WAG) extracts prepared by extraction with water, 30% ethanol, 60% ethanol, or 90% ethanol. The electron donating ability of the WAG extracts was higher than that of the CAG extracts and 0.1% and 1.0% solutions of the comparative substance, L-ascorbic acid. The superoxide dismutase-like activity of the CAG extracts was higher than that of WAG extracts. Superoxide dismutase-like activity was highest (33.95%) in the CAG water extract. The total polyphenol content was highest in the 60% ethanol extracts of WAG. The nitrite scavenging ability of the CAG and WAG extracts was highest at a pH of 1.2. The tyrosinase inhibitory effect was highest (43.72%) in the water extract of WAG. The angiotensin converting enzyme inhibitory activity was highest (83.84%) in the 60% ethanol extract of WAG. The results of the present study will be useful for understanding the antioxidant and angiotensin-converting enzyme inhibitory activities of Angelica gigas Nakai extracts.

• 한국축산식품학회지
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• 제31권5호
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• pp.663-667
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• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

• 한국미생물·생명공학회지
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• 제23권1호
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• pp.53-59
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• 1995

A protease isolated and purified 51 fold from the culture filtrate of a soil bacterium, Bacillus sp. KUN-17, which was appeared to be a monomeric protein with molecular weight of 38, 000 daltons, was suggested to be involved in the serine (-alkaline) protease (E.C 3.4.21.14) since its activity was selectively inhibited by phenylmethylsulfonyl fluoride (PMSF) and required 40$\circ$C and pH 10.5 for optimal condition. The half-life of the enzyme activity was 1 hr at 55$\circ$C, and the activity was maintained even under high concentrations of SDS or urea. The enzyme was indicated to perform random proteolysis from the fact that most of the chromogenic substrates employed were hydrolyzed by the enzyme. The affinity of the enzyme for natural proteins was approximately 10-times higher than ester compounds, and both substrates showed mutual inhibitory effect competitively for the enzyme activity.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2022년도 추계학술대회
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• pp.312-312
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• 2022

Peanut hull as by-product has been discarded during peanut processing. However, peanut hull contains plenty of polyphenols that shows various physiological activities. The objectives of this study were to investigate anti-inflammatory and enzyme inhibitory activities of polyphenols from 'Sinpalkwang' peanut (Arachis hypogaea L.) hull. Compounds were isolated from methanol extracts of peanut hull by preparative-high performance liquid chromatography after identifying and quantifying polyphenols using Ultra performance liquid chromatography (UPLC) and UPLC-Quadrupole time-of-flight-mass spectrometry profiling. The structures of compounds were elucidated by one-dimensional [¹H, ¹³C] nuclear magnetic resonance (NMR) and two-dimensional NMR (correlated spectroscopy, heteronuclear single quantum coherence and heteronuclear multiple bond correlation). Three compounds were identified as 5,7-dihydroxy-4H-chromen-4-one (peak 2), luteolin (peak 4) and eriodictyol (peak 5). Significant differences in inflammatory mediator such as nitric oxide (NO), interleukin-6 (IL-6) and interleukin-1β (IL-lβ) in lipopolysaccharide stimulated Raw 264.7 macrophages and in enzyme (xanthine oxidase [XO] and α-glucosidase [AG]) inhibitory activities were observed between three compounds (p < 0.05). Peak 5 treated Raw 264.7 macrophages showed lower content of NO (16.4 uM), IL-6 (7.0 ng/mL), and IL-1β (60.6 pg/mL) than peak 2 (NO: 28.3 uM, IL-6: 11.3 ng/mL, IL-1β: 66.9 pg/mL) and peak 4 (NO: 24.7 uM, IL-6: 9.3 ng/mL, IL-1β: 62.6 pg/mL). Peak 5 showed higher XO inhibitory activity (84.7%) and higher AG inhibitory activity (52.4%) than peak 2 (XO inhibitory activity: 45.4%, AG inhibitory activity: 21.6%) and peak 4 (XO inhibitory activity: 37.9%, AG inhibitory activity: 37.5%) at concentration of 0.5mg/mL. This study suggests that peanut hull could be a potential source of anti-inflammatory and physiological materials while creating new use of discarded peanut hull as by-products concomitantly.

• Journal of Nutrition and Health
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• 제53권3호
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• pp.244-254
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• 2020

본 연구는 선씀바귀의 항산화 및 탄수화물 소화효소 억제 효과를 평가하여 제 2형 당뇨환자에게 중요한 항산화제 및 혈당 상승 억제제로서의 가능성을 타진하고자 하였다. 선씀바귀 추출물의 총 폴리페놀, 플라보노이드 함량과 in vitro 항산화 활성 및 소화효소 저해 활성을 조사한 결과 ISE가 ISW보다 총페놀과 플라보노이드 함량이 높았고 항산화 활성 및 소화효소 저해 활성 또한 높았다. ISE의 계통분획물 중에 에틸아세테이트 분획물과 부탄올 분획물의 소화효소 저해 활성이 가장 우수하고, 추출물의 항산화활성과 탄수화물 소화효소 억제효과가 총 페놀 및 플라보노이드함량과 높은 상관성을 가지는 것으로 볼 때, ISW에 비해 상대적으로 높은 ISE의 항산화 및 소화효소 저해 활성은 페놀 화합물, 특히 플라보노이드 화합물 때문임을 알 수 있었다. 따라서 ISE와 에틸아세테이트 그리고 부탄올 분획물은 우수한 항당뇨 기능성 소재라고 판단된다.