14144-06-0Relevant academic research and scientific papers
Isolation and characterization of dioscin-α-l-rhamnosidase from bovine liver
Qian, Siriguleng,Wang, Hongying,Zhang, Chunzhi,Yu, Hongshan
, p. 31 - 35 (2013)
A novel dioscin-α-l-rhamnosidase was isolated and purified from fresh bovine liver. The activity of the enzyme was tested using diosgenyl-2,4-di-O- α-l-rhamnopyranosyl-β-d-glucopyranoside as a substrate. It was cleaved by the enzyme to two compounds, rhamnoses and diosgenyl-O-β-d- glucopyranoside. The optimal conditions for enzyme activity were that temperature was at 42 C, pH was at 7, reaction time was at 4 h, and the substrate concentration was at 2%. Furthermore, metal ions such as Fe 3+, Cu2+, Zn2+, Ca2+ and Mg 2+ showed different effects on the enzyme activity. Mg2+ acted as an activator whereas Cu2+, Fe3+, and Zn 2+ acted as strong inhibitors in a wide range of concentrations from 0 to 200 mM. It was interesting that Ca2+ played a role as an inhibitor when its concentration was at 10 mM and acted as an activator at the other concentrations for the enzyme. Moreover, the molecular weight of enzyme was determined as 75 kDa.
STRUCTURE CHARACTERIZATION OF HAEMOSTATIC DIOSGENIN GLYCOSIDES FROM PARIS POLYPHYLLA
Ma, James C. N.,Lau, F. W.
, p. 1561 - 1566 (1985)
Key Word Index - Paris polyphylla; Liliaceae; polyphyllin D; pariphyllin; yunnan paiyao; haemostatic and cytotoxic diosgenin glycosides. - From Paris polyphylla var. chinensis Hare (Liliaceae), four diosgenin glycosides with haemostatic effects were isolated.The structure of the major component was elucidated by chemical and spectroscopic methods as 3-(Rha -> 2Glu)>-Ara -> 4Glu)>-β-D-glucopyranosyl)-25(R)-spirost-5-en-3β-ol.This saponin was found to be identical to three previously reported compounds to which other structures were originally assigned, namely the major component from P. polyphylla Smith, the major cytotoxic component of yunnan paiyao, and polyphyllin D from P. polyphylla grown in the Himalaya region.
The microbiological transformation of steroidal saponins by Curvularia lunata
Feng, Bing,Ma, Bai-Ping,Kang, Li-Ping,Xiong, Cheng-Qi,Wang, Sheng-Qi
, p. 11758 - 11763 (2005)
The microbiological transformation of polyphyllin I (compound I), polyphyllin III (compound II), polyphyllin V (compound III) and polyphyllin VI (compound IV) by Curvularia lunata into their corresponding subsaponins, for example, diosgenin-3-O-α-l-arabinofuranosyl (1→4)-β-d- glucopyranoside (compound V), diosgenin-3-O-α-l-rhamnopyranosyl (1→4)-β-d-glucopyranoside (compound VI), diosgenin-3-O-β-d- glucopyranoside (compound VII) and pennogenin-3-O-β-d-glucopyranoside (compound VIII), were studied in this paper. Curvularia lunata is able to hydrolyze terminal rhamnosyls that are linked by 1→2 C- bond to sugar residues of steroidal saponins at C-3 position with high activity and regioselectivity.
A biocatalytic synthesis of diosgenyl-β-d-glucopyranoside by the use of four recombinant enzymes in one pot
Dong, Qing,Ouyang, Li-Ming,Yu, Hui-Lei,Xu, Jian-He,Lin, Guo-Qiang
, p. 1603 - 1605 (2010)
A system for the one-pot synthesis of diosgenyl-β-d-glucopyranoside (trillin) using multiple recombinant enzymes is developed. The enzymes maltodextrin phosphorylase (E1), glucose-1-phosphate thymidylyltransferase (E2), inorganic pyrophosphatase (E3), and solanidine glucosyltransferase (E4) involved in the work have been cloned and expressed in Escherichia coli. Under the optimized reaction conditions, the yield of trillin reached 28% (ca. 15.8 mg/l). The recovery yield of trillin after purification was 89%.
Small molecular weight PEGylation of diosgenin in an in vivo animal study for diabetic auditory impairment treatment
Kim, Dong-Hwan,Hong, Bin Na,Le, Hoa Thi,Hong, Ha Na,Lim, Choon Woo,Park, Keun Ha,Kim, Tae Woo,Kang, Tong Ho
, p. 4609 - 4612 (2012)
Diosgenin was modified to control its in vivo bioavailability by conjugating a hydrophilic unit, tetraethylene glycol. The diosgenin- tetraethylene glycol conjugate (TE) was orally administered in streptozotocin induced diabetic mice for this auditory protection study. The bioactivity improvement of TE for in vivo diabetic auditory impairment treatment was clearly observed in three different auditory tests and compared with that of diosgenin. The improvement in in vivo efficacy suggests that the small molecular weight PEGylation of diosgenin is a synthetically robust and systematically applicable strategy to reform the poor pharmacokinetics of a hydrophobic aglycone.
The substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata
Feng, Bing,Kang, Li-ping,Ma, Bai-ping,Quan, Bo,Zhou, Wen-bin,Wang, Yong-ze,Zhao, Yu,Liu, Yi-xun,Wang, Sheng-qi
, p. 6796 - 6812 (2007)
In previous work, we studied and reported that an enzyme from Curvularia lunata 3.4381 had the novel specificity to hydrolyze the terminal rhamnosyl at C-3 position of steroidal saponin and obtained four transformed products; the enzyme was purified and ascertained as glucoamylase (EC 3.2.1.3 GA). In this work, the enzyme exhibiting steroidal saponin-rhamnosidase activity was systematically studied on 21?steroidal saponins and 6 ginsenosides. The results showed that the α-1,2-linked end-rhamnosyl residues at C-3 position of steroidal saponins could be hydrolyzed to corresponding secondary steroidal saponins, among which 18 compounds were isolated and identified, including 3 new secondary compounds. For the furostanosides having glucosyl residues at the C-26 position, hydrolysis occurred first at end-rhamnosyl at C-3 position to produce secondary furostanosides. The reaction of hydrolyzing glucosyl at C-26 position depended considerably on longer reaction times yielding the corresponding secondary spirostanosides (without rhamnosyl and glucosyl residues). The enzyme had the strict specificity for the terminal α-1,2-linked rhamnosyl residues of linear chain, or the terminal α-1,2-linked rhamnosyl residues with branched chain of 1,4-linked glycosyl residues of sugar chain at C-3 position of steroidal saponins, it was not specific for different aglycones, different glycons, and the number of glycon of sugar chain of steroidal saponin. The end-rhamnosyl of ginsenosides and p-nitrophenyl-α-l-rhamnopyranoside (pNPR) could not be hydrolyzed by the enzyme from C. lunata.
Pathways of biotransformation of zingiberen newsaponin from Dioscorea zingiberensis C. H. Wright to diosgenin
Huang, Hongzhi,Zhao, Min,Lu, Li,Tan, Dawei,Zhou, Wenbin,Xiong, Chengqi,Zhao, Yang,Song, Xinbo,Yu, Liyan,Ma, Baiping
, p. 1 - 7 (2013)
A new steroidal saponin-β-glucosidase from Aspergillus flavus that specifically hydrolyzed the terminal β-d-glucosyl group at the C-3 position of zingiberen newsaponin, deltonin and trillin from Dioscorea zingiberensis C. H. Wright (DZW) was purified, and characterized. The optimal temperature and pH for the new steroidal saponin-β-glucosidase was 50 C and pH 5.0. The steroidal saponin-β-glucosidase was stable at 30-60 C, and retained more than 80% activity. Further, the purified protein was analyzed by ESI-Q-TOF proteomic analyzer. The results indicated that this enzyme is a β-glucosidase of the type glycosidase hydrolase 3 (GH3). Using a combination of the steroidal saponin-β-glucosidase and steroidal saponin-α-1,2-rhamnosidase from Curvularia lunata obtained previously in our lab, the saponins zingieren newsaponin and deltonin could be converted to diosgenin. The pathways of converting zingiberen newsaponin and deltonin into diosgenin by the two key enzymes were elucidated in this study.
Purification and characterization of dioscin-α-L-rhamnosidase from pig liver
Qian, Srguleng,Yu, Hongshan,Zhang, Chunzhi,Lu, Mingchun,Wang, Hongying,Jin, Fengxie
, p. 911 - 914 (2005)
Dioscin-α-L-rhamnosidase was isolated, purified and partially characterized from pig liver. The maximum activity was reached at pH 7, 42°C, 24 h, and 2% of substrate concentration. Fe3+ and Cu 2+ inhibited the enzyme; the ion Ca2+ activated it. Mg2+ was an inhibitor at 100 mM, but it was an activator at 200 mM. Zn2+ could be a weak activator of the enzyme. The molecular weight of dioscin-α-L-rhamnosidase was about 47 kDa as determined by the method of SDS-polyacrylamide gel electrophoresis.
STEROIDAL SAPONINS FROM THE BULBS OF TRITELEIA LACTEA AND THEIR INHIBITORY ACTIVITY ON CYCLIC AMP PHOSPHODIESTERASE
Mimaki, Yoshihiro,Nakamura, Osamu,sashida, Yutaka,Nikaido, Tamotsu,Ohmoto, taichi
, p. 1279 - 1286 (1995)
The chemical compounds in the bulbs of Triteleia lactea have been analysed as a part of our systematic study of plants of the subfamily Allioideae in Liliaceae.Thirteen steroidal saponins, seven of which appeared to be new compounds, were isolated.The structures of the new saponins were elucidated on the basis of the spectroscopic analysis, including two-dimensional NMR techniques, and hydrolysis.Inhibitory activity of the isolated saponins on cyclic AMP phosphodiesterase was evaluated to identify new compounds with medicinal potential. - Key words: triteleia lactea; Allioideae; Liliaceae; bulbs; steroidal saponins; spirostanol saponins; cyclic AMP phosphodiesterase inhibition.
N-Pentenyl-Type Glycosides for Catalytic Glycosylation and Their Application in Single-Catalyst One-Pot Oligosaccharide Assemblies
Zu, Yujia,Cai, Chenglin,Sheng, Jingyuan,Cheng, Lili,Feng, Yingle,Zhang, Shengyong,Zhang, Qi,Chai, Yonghai
supporting information, p. 8270 - 8274 (2019/10/14)
We have developed a new type of n-pentenyl-type glycosides that can be activated by catalytic amounts of promoter, Hg(NTf2)2 or PPh3AuCl/AgNTf2, at room temperature. The mild activation conditions and outstanding stability of common protection/deprotection manipulations enable the enynyl donors to have broad applications in constructing various glycosidic bonds. Furthermore, under the Hg(NTf2)2-catalyzed conditions, the sequential activation of different types of donors was achieved, based on which a gentiotetrasaccharide was synthesized via the newly developed single-catalyst one-pot strategy.
