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Bae, Hyoung-Cchurl,Choi, Jong-Woo,Nam, Myoung-Soo Korean Society for Food Science of Animal Resource 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius CNU27 possessed a high level of ${\alpha}$-galactosidase activity. Purified ${\alpha}$-galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher than that in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum temperature and pH for the enzyme were $40^{\circ}C$ and 6.0, respectively. The enzyme was stable between 25 and $50^{\circ}C$. However, ${\alpha}$-galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30% of the original activity by addition of $Cu^{2+}$ and $Hg^{2+}$, respectively. Other metal compounds did not affect the enzyme activity significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysis was measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at $40^{\circ}C$.
Properties of β-Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27
Bae, Hyoung-Churl,Renchinkhand, Gereltuya,Nam, Myoung-Soo Korean Society for Food Science of Animal Resource 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius Nam27 with a high ${\beta}$-galactosidase activity was selected for enzymatic characterization. For purification, cell pellet was disrupted by Bead Beater, by DEAE-Sepharose and Mono-Q chromatography. The specific activity of the purified enzyme was 5,312 units/mg. The molecular weight of native monomeric ${\beta}$-galactosidase was estimated to be 30,000 dalton (monomer) by the SDS-PAGE. The optimum temperature and optimum pH were $50^{\circ}C$ and 5.0, respectively. This enzyme was stable between 35 and $55^{\circ}C$. ${\beta}$-galactosidase activity was lost rapidly above pH 7.0. But ${\beta}$-galactosidase was more stable at pH 4.0 (acidic conditions). And ${\beta}$-galactosidase activity was lost rapidly above $65^{\circ}C$ after 10 min incubation. $Ca^{2+}$ and $Zn^{2+}$ metal ions enhanced ${\beta}$-galactosidase activity by 164.09% and 127.37% while $Cu^{2+}$, $Fe^{3+}$ and $Mn^{2+}$ lowered ${\beta}$-galactosidase activity by 58.29%,85.10% and 77.66% respectively. Other metal ions didn't affect ${\beta}$-galactosidase activity significantly.
Properties of β-Galactosidase fromLactobacillus salivarius subsp. salivarius Nam27
Hyoung Churl Bae,Gereltuya Renchinkhand,Myoung Soo Nam 한국축산식품학회 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius Nam27 with a high β-galactosidase activity was selected for enzymatic charac-The specific activity of the purified enzyme was 5,312 units/mg. The molecular weight of native monomeric β-galactosi-dase was estimated to be 30,000 dalton (monomer) by the SDS-PAGE. The optimum temperature and optimum pH were50°C and 5.0, respectively. This enzyme was stable between 35 and 55°C. β-Galactosidase activity was lost rapidly abovepH 7.0. But β-galactosidase was more stable at pH 4.0 (acidic conditions). And β-galactosidase activity was lost rapidlyabove 65°C after 10 min incubation. Ca2+ and Zn2+ metal ions enhanced βwhile Cu2+, Fe3+ and Mn2+ lowered β-galactosidase activity by 58.29%, 85.10% and 77.66%, respectively. Other metal ionsdidn’t affect β-galactosidase activity significantly.
Hyoung Cchurl Bae,Jong Woo Choi,Myoung Soo Nam 한국축산식품학회 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius CNU27 posessed a high level of α-galactosidase activity. Purified α-galactosi-dase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchangechromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher thanthat in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum tempera-ture and pH for the enzyme were 40oC and 6.0, respectively. The enzyme was stable between 25 and 50oC. However, α-galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30%of the original activity by addition of Cu2+ and Hg2+significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysiswas measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at 40oC.
김혜경,배형철,남명수 충남대학교 농업과학연구소 2003 농업과학연구 Vol.30 No.1
오디의 건강 효과와 유산균 배양시 발효촉진 효과를 기대한 새로운 요구르트 개발의 일환으로, 환원 탈지유에 건조방법에 따른 오디의 첨가와 오디 첨가수준을 달리 한 요구르트 제조시 pH, 산도, 유산균수의 변화, 오디요구르트의 저장성 및 관능검사를 수행한 결과는 다음과 같다. 1. 생오디, 동결건조오디, 열풍건조오디는 보통 요구르트에 비하여 pH 저하와 산 생성의 증가가 빨라 발효촉진 효과를 보였으며, 처리구 간에는 동결건조오디나 열풍건조 오디에 비하여 생오디에서 그 효과가 두드러짐을 알 수 있었다. 2. 생오디의 첨가수준이 높을수록 pH 저하와 산생성의 증가가 빨라 발효촉진의 효과를 보였으며, 유산균수도 첨가수준이 높을수록 증가하였다. 3. 생오디 요구르트는 대조군에 비하여 유리당중의 fructose가 증가되었다. 4. 생오디 요구르트에서 lactic acid 함량은 대조군에 비하여 오디의 첨가량이 많을수록 더욱 증가되었다. 5. 생오디 요구르트의 관능검사 결과 외관(color), 맛(taste) 및 전체적인 기호도(overall acceptability)에서 유의적 차이를 보였으며, 향기(oder)와 조직감(texture)에서도 0.3%, 0.6% 처리구에 비하여 0.9%처리구가 좋은 결과를 보여 오디첨가요구르트의 제조 가능성을 보여주었다. 6. 생오디 요구르트의 저장실험 결과, 5℃에서 15일간 저장시 0.9% 오디첨가요구르트는 pH 4.04, 산도 1.082로 나타났고, 유산균수는 1.9×10^9cfu/ml로 우리나라의 호상 요구르트 총 유산균수 기준치 1.0×10^8cfu/ml를 초과하여 제품으로서의 우수성을 확인 할 수 있었다. This experiment was carried out to examine the fermentation properties of yogurt added fresh mulberry, freeze dried-mulberry and heated air dried-mulberry at concentrations of 0%, 0.3%, 0.6% and 0.9%. Lactic acid bacteria was used mixed starter culture(Str.salivarius ssp. thermophilus and Lac. delbrueckii ssp. bulgaricus). We obtained excellent results from the yogurt added fresh mulberry. In yogurt added 0.9% fresh-mulberry, lactic acid contents and titratable acidity were higher than those of 0%, 0.3%, 0.6% fresh-mulberry added. Also, sensory scores of color, taste and overall acceptability of the yogurt with 0.9% fresh mulberry was higher than those of any other groups.
Characteristics of Gouda Cheese Supplemented with Chili Pepper Extract Microcapsules
Yoo Kyeong Kim,Myoung Soo Nam,Hyoung Churl Bae1 한국축산식품학회 2017 한국축산식품학회지 Vol.37 No.6
In this study, the physicochemical and sensory properties of Gouda cheese supplemented with microcapsules of chili pepper extract were evaluated. Microcapsules of pepper extract were prepared by coacervation technique using gum acacia-gelatin wall and chili pepper oil core. Changes in pH, lactic acid bacteria (LAB) population, and free amino acid (FAA) content after supplementation of Gouda cheese with chili pepper capsules were monitored during ripening. Texture and sensory characteristics of the Gouda cheese ripened for 6 months were evaluated. The supplementation of pepper extract microcapsules (0.5% or 1%, w/w) did not influence the pH values and LAB content of the Gouda cheese (p<0.05) during the ripening period. While the content of total FAA increased with the ripening process in all the cheese groups (p<0.05), no significant difference (p<0.05) in the content of total FAA was observed among the sample groups at each time point. The addition of pepper extract microcapsules (1%, w/w) to Gouda cheese significantly decreased hardness (p<0.05) and negatively affected sensory attributes in terms of taste and texture (p<0.05). The results demonstrated that supplementation with 0.5% pepper extract microcapsules could provide additional bioactive ingredients, along with maintenance of the quality of Gouda cheese.
토끼에서 Etofenprox와 Spinosad 합제의 국소자극성 시험
황윤환,김명석,송인배,박병권,양승호,임용현,송치용,안성한,남현수,임정교,정상일,명노일,윤효인 忠南大學校 獸醫科大學 附設 動物醫科學硏究所 2008 動物醫科學硏究誌 Vol.15 No.1
This study was performed to evaluation the skin and eye irritation of etofenprox 8% and spinosad 4% combination in male New Zealand White rabbits. In skin irritation test, the combination of etofenprox and spinosad did not showed any change of body weight but caused slight skin irritation with the P.I.I. (primary irritation index) value 0.25. The etofenprox and spinosad combination showed severe eye irritation 1 h, 24 h, 48 h, and 72 h after ocular treatment, having the A.O.I. (acute ocular irritation) value of 37.3. Therefore, these result indicated that the combination of etofenprox and spinosad might be irritant formulation on eye and skin.
신장에서 노화에 따른 Sirtuin1-NFE2-related Factor 2 Signaling의 변화
배명남 ( Myoung Nam Bae ),최민석 ( Min Seok Choi ),음상훈 ( Sang-hoon Eum ),김은님 ( Eun Nim Kim ),임지희 ( Ji Hee Lim ),김민영 ( Min Young Kim ),반태현 ( Tae Hyun Ban ),장인애 ( In-ae Jang ),윤혜은 ( Hye Eun Yoon ),박철휘 ( Cheol 대한내과학회 2017 대한내과학회지 Vol.92 No.1
목적: 노화에 따른 변화는 산화스트레스가 주요 역할을 하며 SIRT1과 Nrf2가 관여하여 조절하는 것으로 알려져 있다. 이에 본 연구에서는 항산화 효소와 SIRT1-Nrf2의 관계에 의한 신장의 변화를 관찰하였다. 방법: 본 실험에서는 2, 12, 24개월의 C57BL/6 수컷 마우스를 이용하여 신장 기능, 조직학적 변화, 산화스트레스 및 SIRT1-Nrf2 신호전달 변화를 관찰하였다. 결과: 24개월군에서 알부민뇨가 증가되었으며, 크레아티닌 청소율은 12개월군에 비해 24개월군에서 감소되었다. 조직학적 변화에서 사구체 혈관 간세포질과 세뇨관 간질 섬유화가 24개월군에서 증가되었다. 또한, 24개월군에서 산화스트레스 지표인 3-Nitrotyrosine 면역조직화학 발현과 세포사멸이 증가되었다. 24시간 소변내 8-isoprostane과 8-hy-droxy-deoxyguanosine 농도는 노화에 따라 증가하였다. 반면에 SIRT1과 핵내 Nrf2 단백질 발현은 24개월군에서 감소되었다. 항산화 효소 heme oxygenase-1과 NADPH quinone oxi-doreductase1의 발현이 24개월군에서 감소되었으며 또 다른 항산화 효소로 알려진 superoxide dismutase 2도 감소되었다. 결론: SIRT1의 발현이 노화에 따라 감소됨을 증명하였으며 이 결과는 Nrf2를 포함한 SIRT1의 하위분자들의 발현에 관여하여 산화스트레스를 유도하였다. 이러한 신호 전달체계의 약물학적 조절은 신장 노화와 관련된 변화를 감소시킬 수 있을 것이다. Background/Aims: Renal aging-related changes are characterized by oxidative stress. SIRT1 regulates cellular conditions by activating Nrf2. The present study investigated the processes of renal changes by antioxidant enzymes and the relationship between SIRT1 and Nrf2. Methods: We used male 2-, 12-, and 24-month-old C57BL/6 mice. We measured renal function, histological changes, oxidative stress, and expression of SIRT1-Nrf2 signaling in the kidneys. Results: 24-month-old mice exhibited increased albuminuria and serum creatinine. Creatinine clearance was decreased in 24-month-old mice compared with 12-month-old mice. There were increases in mesangial volume and tubulointerstitial fibrosis in 24-month-old mice. Moreover, oxidative stress marker, 3-Nitrotyrosine, expression and apoptosis were increased in 24-month-old mice. The 24 h urinary 8-isoprostane and 8-hydroxy-deoxyguanosine excretion increased with aging. The levels of expression of SIRT1 and nuclear Nrf2 were decreased in 24-month-old mice. The antioxidant enzymes HO-1 and NQO-1 were down-regulated in 24-month-old mice. Another antioxidant enzyme, SOD2, was decreased in 24-month-old mice. Conclusions: Our results demonstrated that SIRT1 was down-regulated with aging, and this may be related to changes in the expression of target molecules including Nrf2. As a result, oxidative stress was induced. The pharmacological targeting of these signaling molecules may reduce the pathological changes associated with aging in the kidney. (Korean J Med 2017;92:53-61)