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An original use of size exclusion-HPLC for predicting the performances of batch ultrafiltration implemented to enrich a complex protein hydrolysate in a targeted bioactive peptide

Abstract : This article reports an original strategy for predicting the performances of UF aimed at enriching a hydrolysate in a targeted peptide. This strategy is based on classical equations from UF global mass balance that requires both the retention rate and the initial concentration of every hydrolysate peptide. The main difficulty lies in the assessment of this information for hydrolysates are commonly composed of a hundred or more different peptides. The originality of this work is to overcome this using a simple hydrolysate SE-HPLC analysis. In this methodology, every point of the chromatogram is meant to be a 'virtual peptide' having both RR and concentration defined from retention time and absorbance. The strategy was applied to predict the enrichment of a complex hydrolysate in a bioactive peptide (VW). Modelled and experimental values of VW enrichment and extraction yield had no relative errors higher than 10%, which validated the method in this case.
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https://hal.archives-ouvertes.fr/hal-00777705
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Submitted on : Thursday, January 17, 2013 - 6:32:29 PM
Last modification on : Thursday, April 9, 2020 - 1:42:10 AM

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Romain Kapel, F. Klingenberg, Xavier Framboisier, Pascal Dhulster, Ivan Marc. An original use of size exclusion-HPLC for predicting the performances of batch ultrafiltration implemented to enrich a complex protein hydrolysate in a targeted bioactive peptide. Journal of Membrane Science, Elsevier, 2011, 383 (1-2), pp.26-34. ⟨10.1016/j.memsci.2011.08.025⟩. ⟨hal-00777705⟩

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