Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis
| Autor: | S Ahmed Nacer, Justine Mouecoucou, Luc Mejean, C. Villaume, Christian Sanchez |
|---|---|
| Přispěvatelé: | Unité de Recherches Animal et Fonctionnalités des Produits Animaux (URAFPA), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Laboratoire de Physico-chimie et Génie Alimentaires, Institut National Polytechnique de Lorraine (INPL), Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Physico-chimie et Génie Alimentaires (LPGA), ProdInra, Migration |
| Rok vydání: | 2003 |
| Předmět: |
Whey protein
animal structures food.ingredient Pectin 030309 nutrition & dietetics PEPSIN ENZYMATIC ACTIVITY Static Electricity Lactoglobulins macromolecular substances Polysaccharide Methylation complex mixtures 03 medical and health sciences Hydrolysis 0404 agricultural biotechnology food PECTIN N RELEASE Pepsin Nephelometry and Turbidimetry [SDV.IDA]Life Sciences [q-bio]/Food engineering Beta-lactoglobulin chemistry.chemical_classification 0303 health sciences Chromatography biology digestive oral and skin physiology food and beverages PEPSIN 04 agricultural and veterinary sciences General Chemistry Hydrogen-Ion Concentration [SDV.IDA] Life Sciences [q-bio]/Food engineering β-LACTOGLOBULIN 040401 food science Pepsin A In vitro Enzyme chemistry Biochemistry TURBIDITY biology.protein Pectins General Agricultural and Biological Sciences |
| Zdroj: | Journal of Agricultural and Food Chemistry Journal of Agricultural and Food Chemistry, American Chemical Society, 2004, 52 (2), pp.355-360. ⟨10.1021/jf034584a⟩ |
| ISSN: | 1520-5118 0021-8561 |
| Popis: | International audience; This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of â-lactoglobulin (â-lg). Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of â-lg-pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. â-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of â-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity. |
| Databáze: | OpenAIRE |
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