Pseudo-Biospecific Affinity Ligand Chromatography

Vijayalakshmi, M. A.

doi:10.1007/978-1-4899-1872-7_18

Cited by 9 publications

(2 citation statements)

References 30 publications

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“…As an alternative, pseudo affinity ligands [80] and ion exchange groups [81] having well defined chemical structure have been designed to capture proteins. There are basically three classes of such ligands-amino acids, metal chelates and triazine dyes [82]. These ligands possess relatively low specificity but have higher physical and chemical stability, are easy to elute, have low cost and high bonding capacity.…”

Section: Mnps As Pre-concentration and Capture Probementioning

confidence: 99%

Magnetic Particles-Based Analytical Platforms for Food Safety Monitoring

et al. 2019

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Magnetic nanoparticles (MNPs) have attracted growing interest as versatile materials for the development of analytical detection and separation platforms for food safety monitoring. This review discusses recent advances in the synthesis, functionalization and applications of MNPs in bioanalysis. A special emphasis is given to the use of MNPs as an immobilization support for biomolecules and as a target capture and pre-concentration to increase selectivity and sensitivity of analytical platforms for the monitoring of food contaminants. General principles and examples of MNP-based platforms for separation, amplification and detection of analytes of interest in food, including organic and inorganic constituents are discussed.

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Section: Mnps As Pre-concentration and Capture Probementioning

confidence: 99%

Magnetic Particles-Based Analytical Platforms for Food Safety Monitoring

et al. 2019

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“…The cryogel functionalization via the glutaraldehyde method transforms epoxy groups on the surface of the monolith into activated aldehyde groups, which can react with the amine groups of binding molecules. [ 10 ] Among the binding agents, amino acids stand out due to their biocompatibility, [ 12 ] stability, low cost, [ 13 ] ease to obtain and manipulate.…”

Section: Introductionmentioning

confidence: 99%

Performance of pseudo‐specific cryogel in lysozyme purification from chicken egg white

et al. 2022

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The application of cryogels for biomolecule purification has expanded due to their adsorption efficiency and operational advantages. In this study, polyacrylamide cryogels functionalized with L-phenylalanine (cryogel-Phe) via the glutaraldehyde method were designed for lysozyme adsorption. Cryogel functionalization was confirmed by Fourier-transform infrared spectroscopy and Kjeldahl analysis, indicating the immobilization of 458.65 mg phenylalanine g cryogel À1 . Cryogel-Phe showed high porosity (0.95) and a Young's modulus of 526.71 kPa. Thermogravimetric analysis indicated that thermal degradation occurred above 200 C. Differential scanning calorimetry and X-ray diffraction confirmed that the cryogel material was amorphous. In addition, the column presented a hydraulic permeability of 4.15 Â 10 À13 m 2 , axial dispersion ranging from 10 À7 to 10 À6 m 2 s À1 , and a height equivalent to a theoretical plate ranging from 0.10 to 0.21 cm. The highest adsorption of lysozyme (67.65 mg g À1 ) was obtained using sodium thiocyanate saline solution (0.025 mol L À1 , pH 5.0). The ability of the cryogel-Phe column to capture and purify lysozyme was confirmed by high enzymatic activity (1294.17 U ml À1 ), purity (87.92%), purification factor (11.49), and sulphate-polyacrylamide electrophoresis gel (SDS-PAGE) electrophoresis gel.

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Preparation of Affinity Chromatography Monolith in Miniaturized Format and Application for Protein Separation

Tetala

2022

Methods in Molecular Biology

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Pseudo-Biospecific Affinity Ligand Chromatography

Cited by 9 publications

References 30 publications

Magnetic Particles-Based Analytical Platforms for Food Safety Monitoring

Magnetic Particles-Based Analytical Platforms for Food Safety Monitoring

Performance of pseudo‐specific cryogel in lysozyme purification from chicken egg white

Preparation of Affinity Chromatography Monolith in Miniaturized Format and Application for Protein Separation

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