Breakthrough performance of stacks of dye-cellulosic fabric in affinity chromatography of lysozyme

Tejeda-Mansir, Armando; Rm, Montesinos; Magaña-Plaza, I.; Guzmán, Roberto

doi:10.1007/s00449-002-0302-0

Cited by 7 publications

(4 citation statements)

References 25 publications

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“…The maximum capacities of all the Protein A ligand materials MP-AA (High Sub), MP-AA (Low Sub) and Toyopearl-AA are in the range of 37 -45 mg per mL. This is compatible with the static capacity normally observed in commercial and experimental affinity adsorbents [38]. Toyopearl epoxy which is a commercial epoxy-activated support was utilised as a control to confirm Protein A binding to a model solid support.…”

Section: Adsorbent Characteristicssupporting

confidence: 93%

A megaporous material harbouring a peptide ligand for affinity IgG purification

et al. 2017

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Common limitations of Protein A affinity chromatography include high adsorbent costs, ligand instability and possible ligand leakage. In this study, a short peptide with affinity for IgG was synthesized chemically and subsequently immobilized on a megaporous support. The support was prepared utilising the cryogel technique while the peptide-ligand was covalently immobilised via thiol-epoxy click chemistry. The cryogel support was chemically grafted to increase the number of reaction sites. This adsorbent was designated as "MP-Pep". Adsorption isotherms were employed to evaluate protein binding capacity. A maximum static binding capacity within the range of 30-60 mg/mL was observed for hIgG. This parameter compares well with other commercial and non-commercial adsorbents, as reported in the literature. As a control material, a Protein A grafted megaporous cryogel was synthesized. Dynamic binding capacity values were obtained by breakthrough analysis. The peptide cryogel showed a dynamic capacity value 9.0 mg/mL in comparison to 9.7 mg/mL in the case of the Protein A based adsorbent. The ratio of dynamic binding capacity to static binding capacity was 20%, indicating suboptimal product capture. However, the advantage of MP-Pep lies in its cost-effective preparations while maintaining a reasonable binding capacity for the targeted product. The presence of cooperative effects during protein binding could also represent an advantage during the processing of a feedstock containing a product in high concentration.

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Section: Adsorbent Characteristicssupporting

confidence: 93%

A megaporous material harbouring a peptide ligand for affinity IgG purification

et al. 2017

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“…The adsorption capacities are high compared with published data in literature. TejedaMansir et al [35] investigated adsorption of LZ on dye cellulosics. Their Langmuir isotherm values were q m = 2.0 mg/ml and K d = 5.9 × 10 −2 mg/ml.…”

Section: Mixed Matrix Membrane Adsorbers Characterizationmentioning

confidence: 99%

Enzyme capturing and concentration with mixed matrix membrane adsorbers

Saiful

Borneman

Weßling

2006

Journal of Membrane Science

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“…of fabric 100% cotton, style no. 400 M, were washed by boiling for 1 h in 5% soap solution (Tejeda-Mansir et al 2003). After eliminating the soap by washing it extensively with distilled water, the cotton fabric pieces were treated with phosphoric acid (85% w/v) (Wood 1988).…”

Section: Purification and Immobilization Of Ad-cbd Recombinant Proteimentioning

confidence: 99%

One-step Purification and Immobilization in Cellulose of the GroEL Apical Domain Fused to a Carbohydrate-binding Module and its use in Protein Refolding

et al. 2006

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The apical domain of the chaperonin, GroEL, fused to the carbohydrate binding module type II, CBD(Cex), of Cellulomonas fimi, was expressed in Escherichia coli. The recombinant protein, soluble or from inclusion bodies, was directly purified and immobilized in microcrystalline cellulose particles or cellulose fabric membranes. Assisted refolding of rhodanese by the immobilized mini-chaperone showed a two-fold improvement as compared to a control. Using chromatographic refolding, 35% of rhodanese activity was recovered in only 5 min (mean residence time) as compared to 17% for spontaneous refolding. This mini-chaperone immobilized in cellulose could be a cost-efficient method to refold recombinant proteins expressed as inclusion bodies.

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Breakthrough performance of stacks of dye-cellulosic fabric in affinity chromatography of lysozyme

Cited by 7 publications

References 25 publications

A megaporous material harbouring a peptide ligand for affinity IgG purification

A megaporous material harbouring a peptide ligand for affinity IgG purification

Enzyme capturing and concentration with mixed matrix membrane adsorbers

One-step Purification and Immobilization in Cellulose of the GroEL Apical Domain Fused to a Carbohydrate-binding Module and its use in Protein Refolding

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