Time evolution of exposed hydrophobicity of water-soluble proteins during their depolymerisation by endo-proteases

• Autores: Enrique Sentandreu, J.M. Sendra, José Vicente Carbonell
• Localización: Food science and technology international = Ciencia y tecnología de alimentos internacional, ISSN-e 1532-1738, ISSN 1082-0132, Vol. 10, Nº 6, 2004, págs. 399-408
• Idioma: inglés
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• Resumen

  • During the depolymerisation of a water-soluble protein by an endo-protease, the exposed hydrophobicity of the substrate, that is the hydrophobicity that is accessible to hydrophobic probes, changes with the progress of the reaction. This work describes the depolymerisation of bovine serum albumin, a-casein and B-lactoglobulin using the proteases Alcalase, Flavourzyme, a-chymotrypsin, mercuripapain and trypsin. Time evolution of substrate hydrophobicity was monitored by a fiow-injection analysis (FIA) system with fluorescence detection and an aqueous eluant containing p-toluidinylnaphthalene-6-sulfonate (2,6-TNS) as the fluorescent probe. In all cases, the time evolution of the substrate hydrophobicity was fitted using a derived mathematical function containing two adjustable rate constants and two constant parameters. This methodology allowed the determination of protease activities, as well as online monitoring of the depolymerisation process, when using water-soluble proteins as substrate.