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14144-06-0

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14144-06-0 Usage

Definition

ChEBI: A sterol 3-beta-D-glucoside having diosgenin as the sterol component.

Check Digit Verification of cas no

The CAS Registry Mumber 14144-06-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,1,4 and 4 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 14144-06:
(7*1)+(6*4)+(5*1)+(4*4)+(3*4)+(2*0)+(1*6)=70
70 % 10 = 0
So 14144-06-0 is a valid CAS Registry Number.
InChI:InChI=1/C33H52O8/c1-17-7-12-33(38-16-17)18(2)26-24(41-33)14-23-21-6-5-19-13-20(8-10-31(19,3)22(21)9-11-32(23,26)4)39-30-29(37)28(36)27(35)25(15-34)40-30/h5,17-18,20-30,34-37H,6-16H2,1-4H3/t17-,18+,20+,21-,22+,23+,24+,25-,26+,27-,28+,29-,30-,31+,32+,33-/m1/s1

14144-06-0SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017

1.Identification

1.1 GHS Product identifier

Product name Trillin

1.2 Other means of identification

Product number -
Other names Melongoside B

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:14144-06-0 SDS

14144-06-0Relevant articles and documents

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.

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.

Glucosylation and galactosylation of diosgenin and solasodine by soluble glycosyltransferase(s) from Solanum melongena leaves

Paczkowski,Wojciechowski

, p. 1429 - 1434 (1994)

-

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%.

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.

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.

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.

STEROID SAPONINS WITH ANTI-CANCER ACTIVITY

-

, (2018/09/08)

The present invention relates to a new class of steroid saponins that have interesting biological activity. In particular the present invention relates to a class of steroid saponins in which the sugar moiety has been selectively functionalised to introdu

Solasodine-3-O-β-D-glucopyranoside kills Candida albicans by disrupting the intracellular vacuole

Chang, Wenqiang,Li, Ying,Zhang, Ming,Zheng, Sha,Li, Yan,Lou, Hongxiang

, p. 139 - 146 (2017/06/05)

The increasing incidence of fungal infections and emergence of drug resistance underlie the constant search for new antifungal agents and exploration of their modes of action. The present study aimed to investigate the antifungal mechanisms of solasodine-3-O-β-D-glucopyranoside (SG) isolated from the medicinal plant Solanum nigrum L. In vitro, SG displayed potent fungicidal activity against both azole-sensitive and azole-resistant Candida albicans strains in Spider medium with its MICs of 32 μg/ml. Analysis of structure and bioactivity revealed that both the glucosyl residue and NH group were required for SG activity. Quantum dot (QD) assays demonstrated that the glucosyl moiety was critical for SG uptake into Candida cells, as further confirmed by glucose rescue experiments. Measurement of the fluorescence intensity of 2′,7'-dichlorofluorescin diacetate (DCFHDA) by flow cytometry indicated that SG even at 64 μg/ml just caused a moderate increase of reactive oxygen species (ROS) generation by 58% in C. albicans cells. Observation of vacuole staining by confocal microscopy demonstrated that SG alkalized the intracellular vacuole of C. albicans and caused hyper-permeability of the vacuole membrane, resulting in cell death. These results support the potential application of SG in fighting fungal infections and reveal a novel fungicidal mechanism.

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