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Supelco

Astec® CHIRALDEX™ G-TA Capillary GC Column

L × I.D. 30 m × 0.25 mm, df 0.12 μm

Synonym(s):

GC column, chiral, gamma-dextran

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About This Item

UNSPSC Code:
41115710
NACRES:
SB.54

material

fused silica

description

GC capillary column

packaging

pkg of 1 ea

parameter

-10-180 °C temperature (isothermal or programmed)

Beta value

500

df

0.12 μm

technique(s)

gas chromatography (GC): suitable

L × I.D.

30 m × 0.25 mm

matrix active group

non-bonded; 2,6-di-O-pentyl-3-trifluoroacetyl derivative of γ-cyclodextrin phase

application(s)

agriculture
chemicals and industrial polymers
cleaning products
clinical
cosmetics
environmental
flavors and fragrances
food and beverages
forensics and toxicology
life science and biopharma
personal care
pharmaceutical (small molecule)

column type

capillary chiral

separation technique

chiral

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General description

Astec® CHIRALDEX G-TA is the first choice in the Group 1 CSPs (Surface Interactions, Complex Derivatives). This phase has been shown to be the most broadly-selective phase for the pharmaceutical industry, especially for the analysis of chiral intermediates and drug studies in various stages of clinical trials. Separations occur without the inclusion mechanism and are typically faster and more efficient than most chiral stationary phases. G-TA has also been used to separate parent drug enantiomers and their metabolites. G-TA has its highest selectivity for oxygen-containing analytes like alcohols, diols and polyols as the free alcohol and as an acyl derivative; amines as acyl derivatives; amino alcohols, halogens (Cl>Br>F), amino acids, hydroxy acids, lactones, furans and pyrans. It is also highly selective for halogenated compounds.

Application

Astec® CHIRALDEX™ G-TA (2,6-di-O-pentyl-3-trifluoroacetyl-γ-cyclodextrin) derivatized cyclodextrin chiral stationary phase may be used in capillary gas chromatography for separation of four isomers from 7 racemic sulfinate esters. It was used in an experimental study done for cloning and characterization of three epoxide hydrolases identified by analyzing open reading frames (ORFs) of a marine bacterium, Erythrobacter litoralis HTCC2594. It was also used in HPLC and GC analyses of the conversion of epoxides during enantioselectivity of epoxide hydrolase from Agrobacterium radiobacter (EchA) using error-prone PCR and DNA shuffling.

Chem/Phys Resistance

Temp. Limits:
  • -10 °C to 180 °C isothermal and programmed

Other Notes

We offer a variety of chromatography accessories including analytical syringes

Legal Information

Astec is a registered trademark of Merck KGaA, Darmstadt, Germany
CHIRALDEX is a trademark of Sigma-Aldrich Co. LLC

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Certificates of Analysis (COA)

Lot/Batch Number
290339-04
290339-03
290339-02
290339-01
290506-04

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Bert van Loo et al.
Chemistry & biology, 11(7), 981-990 (2004-07-24)
The enantioselectivity of epoxide hydrolase from Agrobacterium radiobacter (EchA) was improved using error-prone PCR and DNA shuffling. An agar plate assay was used to screen the mutant libraries for activity. Screening for improved enantioselectivity was subsequently done by spectrophotometric progress
Jung-Hee Woo et al.
Applied microbiology and biotechnology, 76(2), 365-375 (2007-06-02)
Previously, we reported that ten strains belonging to Erythrobacter showed epoxide hydrolase (EHase) activities toward various epoxide substrates. Three genes encoding putative EHases were identified by analyzing open reading frames of Erythrobacter litoralis HTCC2594. Despite low similarities to reported EHases
Asymmetric ring opening of meso-epoxides with B-halobis(2-isocaranyl)boranes 2-dIcr2BX
Roy, Chandra D., Brown, Herbert C.
Tetrahedron Asymmetry, 17 (13), 1931-1936 (2006)
Kinetic resolutions concentrate the minor enantiomer and aid measurement of high enantiomeric purity.
Caron, Gaetan; Tseng, George W.M.; Kazlauskas, R.J.
Tetrahedron Asymmetry, 5 (1), 83-92 (1994)
Hugo L van Beek et al.
FEBS open bio, 4, 168-174 (2014-03-22)
Enzyme stability is an important parameter in biocatalytic applications, and there is a strong need for efficient methods to generate robust enzymes. We investigated whether stabilizing disulfide bonds can be computationally designed based on a model structure. In our approach
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