http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
혐기성조건에서 Lactobacillus rhamnosus BHN-LAB 76에 의한 배당체 이소플라본의 비배당체 이소플라본으로의 생물전환
김병혁,장종옥,이준형,박예은,김중규,윤여초,정수진,권기석,이중복 한국식품저장유통학회 2019 한국식품저장유통학회지 Vol.26 No.2
Isoflavones exhibit an estrogenic activity and have been reported extensively for their potential role in preventing chronic diseases, such as cancer, osteoporosis, and postmenopausal syndrome. Pueraria is a medicinally important leguminous plant producing several glycoside isoflavones, such as daidzin, daidzein, genistin, and puerarin. However, daidzin and genistin mainly exist as nonabsorbable and biologically inactive glycosides. The bioavailability of glucosides is increased by hydrolysis of the sugar moiety using β-glucosidase. Furthermore, intestinal microorganisms can enhance the biological activity of these isoflavones through biotransformation. Lactic acid bacteria (LAB) are typical probiotic microorganisms used in fermented foods, as feed additives, and in pharmaceuticals. Therefore, we isolated Lactobacillus rhamnosus BHN-LAB 76 from Korean traditional fermented food and assessed its isoflavone-transforming activity in the production of daidzein using HPLC. The Pueraria lobata extract was fermented with L. rhamnosus BHN-LAB 76 for 72 h at 37℃ under anaerobic conditions. L. rhamnosus BHN-LAB 76 could convert about 25% of daidzin to daidzein. These results confirmed the potential of L. rhamnosus BHN-LAB 76 as a probiotic culture, which can be utilized in the manufacture of fermented and functional foods.
Flavonoids Biotransformation by Human Gut Bacterium Dorea sp. MRG-IFC3 Cell-Free Extract
Mi Huynh Thi Ngoc,Kim Heji,Lee Jong Suk,Eser Bekir Engin,Han Jaehong 한국미생물·생명공학회 2024 Journal of microbiology and biotechnology Vol.34 No.6
Human gut bacterium Dorea sp. MRG-IFC3 is unique in that it is capable of metabolizing puerarin, an isoflavone C-glycoside, whereas it shows broad substrate glycosidase activity for the various flavonoid O-glycosides. To address the question on the substrate specificity, as well as biochemical characteristics, cell-free biotransformation of flavonoid glycosides was performed under various conditions. The results showed that there are two different enzyme systems responsible for the metabolism of flavonoid C-glycosides and O-glycosides in the MRG-IFC3 strain. The system responsible for the conversion of puerarin was inducible and comprised of two enzymes. One enzyme oxidizes puerarin to 3”-oxo-puerarin and the other enzyme converts 3”-oxo-puearin to daidzein. The second enzyme was only active toward 3”-oxo-puerarin. The activity of puerarin conversion to daidzein was enhanced in the presence of Mn2+ and NAD+ . It was concluded that the puerarin C-deglycosylation by Dorea sp. MRG-IFC3 possibly adopts the same biochemical mechanism as the strain PUE, a species of Dorea longicatena.
Isoflavone glycosides from the flowers of Pueraria thunbergiana
Jung, Won-Tae,Moon, Jeon-Ok,Park, Hee-Juhn,Oh, Sei-Ryang,Park, Jong-Hee,Lee, Hyeong-Kyu,Lee, Kyung-Tae WHO COLLABORATING CENTRE FOR TRADITIONAL MEDICINE 1999 東西醫學硏究所 論文集 Vol.1999 No.-
Two new isoflavone glycosides together with glycitein, tectoridin and glycitin, were isohted from the flowers of Pueraria thun-bergiana. These structures were determined as 4',7-dihydroxy-6-methoxyisoflavone 7-O-β-D-xylopyranosyl-(1->6)-β-D-gluco-pyranosie And 4',5,7-trihdroxy-6-methoxyisoflavone 7-O-β-D-xylopyranosyl-(1->6)-β-D-glucopyranoside.
대두 이소플라본 당전이 반응 산물의 콜레스테롤 생합성 저해 효과
유랑국(Lang Kuk Yoo),최승준(Seung Jun Choi),문태화(Tae Wha Moon),심재훈(Jae-Hoon Shim) 한국식품영양과학회 2016 한국식품영양과학회지 Vol.45 No.2
HMG-CoA reductase는 체내 콜레스테롤 생합성에 있어서 속도제한단계(율속) 효소이다. 본 연구는 HMG-CoA reductase에 대한 이소플라본 배당체의 저해 효과를 연구하였다. 100 μM의 농도에서 genistein-7-O-triglucoside(G2-genistin)는 HMG-CoA reductase 활성을 약 18% 정도 저해하였으나, daidzein-7-O-triglucoside는 저해 효과를 갖지 않았다. 시리아햄스터 HMG-CoA reductase의 반응속도 실험에서 G2-genistin은 농도에 관계없이 Vmax의 저해정도가 일정하였으며, 이것은 G2-genistin이 HMG-CoA reductase의 경쟁적 저해제로 작용함을 시사하고 HMGCoA reductase의 활성을 직접적으로 저해함으로써 혈중콜레스테롤 함량을 감소시킬 수 있음을 예상할 수 있다. Hydroxy-3-methylglutaryl-CoA reductase (HMG-CoA reductase) is the rate-limiting enzyme in biosynthesis of cholesterol in animals. In this study, inhibitory effects of isoflavone glycosides on HMG-CoA reductase were investigated. At sample concentration of 100 μM, genistein-7-O-triglucoside (G2-genistin) inhibited HMG-CoA reductase activity by approximately 18%, whereas daidzein-7-O-triglucoside had no inhibitory effect. In the kinetic experiments with Syrian hamster HMG-CoA reductase, G2-genistin showed inhibitory efficacy with an invariable Vmax value, suggesting that G2-genistin works as a competitive inhibitor of HMG-CoA reductase and has potential for hypocholesterolemic action through direct regulation of HMG-CoA reductase.
A New Isoflavone Glycoside from the Stem Bark of Sophora japonica
Hyun Young Park,Soo Hee Kim,Gi Beom Kim,Jae Young Sim,임순성,Myong Jo Kim,Wanjoo Chun,Yong Soo Kwon 대한약학회 2010 Archives of Pharmacal Research Vol.33 No.8
A new isoflavone glycoside, 6-methoxy-7-hydroxy-4’-O-β-D-glucosyl isoflavone, glycitein-4’-O-β-D-glucoside (10), along with nine known flavonoids, were isolated from the stem bark of Sophora japonica. The structures of these compounds were determined by analysis of spectroscopic data (1D -, 2D - NMR and HRMS). The inhibitory effects of all the isolated compounds on aldose reductase were evaluated in vitro. Among these compounds, daidzein (1), puerol A (4), and paratensein-7-O-glucoside (9) exhibited potent inhibitory effects, with IC50 values of 3.2, 6.4, and 1.9 μM, respectively.
Shenglin Hu,Dongmei Wang,Jiong Hong 한국생물공학회 2018 Biotechnology and Bioprocess Engineering Vol.23 No.1
In this study, a simple, inexpensive and fast β-glucosidase immobilization system was constructed and evaluated in isoflavone glycosides hydrolysis. A β-glucosidase gene from Thermoascus aurantiacus IFO9748 was recombinantly expressed in Pichia pastoris KM71H and immobilized on regenerated amorphous cellulose (RAC) by fused cellulose binding module 3. Through simple mixing cellulose and crude enzyme for 15 min under room temperature, 96.04% β-glucosidase was immobilized onto RAC. The optimum temperature for β-glucosidase activity was increased by 5ºC after immobilization. The half-life (t½) of heat inactivation of immobilized enzyme at 60oC was improved over 8 folds. After 30 rounds recycled at 40oC, 96.9% daidzin and 98.9% genistin could still be hydrolyzed. A continuous hydrolysis system was also constructed, and at the flow rate of 0.2 mL/min after 30 h hydrolysis, 95.6% genistin and 90.2% daidzin can still be hydrolyzed. Combined the simple and high efficient enzyme immobilization procedure and inexpensive cellulose, this scalable and practical system may have broad prospects for industrial utilization.