The Size-Exclusion Chromatographic Behavior of Synthetic Water-Soluble Polymers on Diol Bonded Phase Supports

Herman, David; Field, Larry R.; Abbott, Seth R.

doi:10.1093/chromsci/19.9.470

Cited by 50 publications

(16 citation statements)

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“…The epoxyactivated silica (epoxy−silica) was prepared according to previously established protocols. 37 The SP-100-15-P Daiso silica gel (pore size of 100 Å, 5 g) was calcined at 200 °C under vacuum for 24 h. The freshly activated dry silica was then suspended in dry toluene (80 mL) and degassed by sonication under vacuum for 30 min. A 10-fold theoretical excess of GLYMO was added, and the mixture was heated to reflux for 4 h. The amount of GLYMO added to the reaction mixture was calculated 38 based on the specific surface area of silica (452 m 2 / g) (based on the information provided by the supplier of bare silica (Daiso Chemical Co. Ltd., Japan)) and the wetting area of GLYMO (330 m 2 /g).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR

et al. 2016

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Solid-state magic-angle spinning (MAS) NMR spectroscopy was employed to investigate structural detail in an enzyme, human carbonic anhydrase II (hCA II) in uniformly 15 N and selectively (15 N leucine) enriched states, covalently immobilized on epoxyfunctionalized silica. The immobilized hCA II retained 71% of its specific enzymatic activity when compared to the free enzyme in solution. Based on the one-and two-dimensional 1 H, 13 C, 15 N and 29 Si MAS NMR spectra, chemical shift assignments could be obtained from the silica support, covalent linker and the immobilized enzyme. The successful covalent immobilization of the enzyme on epoxy-silica was confirmed by the appearance of signals from the aromatic and carbonyl groups in the immobilized enzyme in addition to signals from the modified support. Most notably, our MAS NMR results suggest that the covalent immobilization of the hCA II on epoxy-silica does not significantly affect the structural integrity of the protein.

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Section: ■ Materials and Methodsmentioning

confidence: 99%

High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR

et al. 2016

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“…294 Size-exclusion chromatography on diol-bonded Si-gel was also observed for synthetic polymers in reversed-phase mode. 295 For low molecular weight aromatic analytes, dipolar interactions determined the chromatographic behavior on diol-bonded Sigel by normal-phase chromatography. 296 The antibiotic Sch 58761 (61) was isolated from cultures of Micromonospora carbonaceae using normal-phase chromatography with a diolbonded Si-gel column.…”

Section: Ion-exchange Chromatographymentioning

confidence: 99%

The isolation of water-soluble natural products – challenges, strategies and perspectives

et al. 2022

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“…A large number ofracemic drugs have been resolved into their enantiomers on chiral stationary phases based on, for example, immobilized bovine [6], human serum albumin [7], cq-acidglycoprotein [8], ~-chymotrypsin [9], ovomucoid [ 10] or cellulase [ 11]. The protein has been immobilized on several modified silica surfaces via aldehyde [12], tresyl [9] and epoxide functions [ 13], for example. In this paper we discuss the use of an enzyme, amyloglucosidase, as a chiral selector.…”

Section: Introductionmentioning

confidence: 99%

Use of immobilized amyloglucosidase as chiral selector in chromatography. Immobilization and performance in liquid chromatography

et al. 1999

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SummaryThe enzyme amyloglucosidase was immobilized on oxidized DIOL silica and used to separate enantiomers of amino alcohols. The influence of pore size on enantioselectivity was studied and an optimum in the separation factors was found using 500 A DIOL silica as the starting material. About twice the amount of the protein could be immobilized on the 500 .~ DIOL silica material as on the 300 and 1000 ]~ materials. The immobilization procedure was easy to reproduce and no significant difference in the chromatographic behavior was observed between two amyloglucosidase columns produced in-house. The effect of solute structure on enantioselective retention was studied using a set of 10 closely related amino alcohols. High separation factors (~ > 2) were obtained and the efficiency of the amyloglucosidase columns was greater than 25 000 plates/m based on the last eluted enantiomer.

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The Size-Exclusion Chromatographic Behavior of Synthetic Water-Soluble Polymers on Diol Bonded Phase Supports

Cited by 50 publications

References 0 publications

High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR

High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR

The isolation of water-soluble natural products – challenges, strategies and perspectives

Use of immobilized amyloglucosidase as chiral selector in chromatography. Immobilization and performance in liquid chromatography

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