Effect of pH on the physicochemical characteristics and the surface chemical composition of camel and bovine whey protein's powders.
Adsorption
Animals
Calorimetry
Camelus
Cattle
Chromatography, High Pressure Liquid
Crystallization
Hydrogen-Ion Concentration
Lactoglobulins
/ chemistry
Lactose
/ chemistry
Mass Spectrometry
Powders
/ chemistry
Protein Denaturation
Surface Properties
Transition Temperature
Water
/ chemistry
Whey Proteins
/ chemistry
Camel whey proteins
Glass transition temperature
LC–MS
X-ray Photoelectron spectroscopy
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
15 Dec 2020
15 Dec 2020
Historique:
received:
17
02
2020
revised:
04
07
2020
accepted:
05
07
2020
pubmed:
20
7
2020
medline:
21
10
2020
entrez:
20
7
2020
Statut:
ppublish
Résumé
This study investigated the effect of pH on the denaturation extent, the surface chemical composition, the water sorption isotherm and the glass transition temperature of camel and bovine whey protein's powders. The LC-MS analysis indicated that the β-Lactoglobulin was the most denatured protein in bovine whey powders regardless the pH value, while this protein was totally absent in camel whey. The α-Lactalbumin was relatively heat stable after drying and predominated the powder surface (X-ray photoelectron spectroscopy results) in both camel and bovine whey powders regardless the pH (neutral (6.7) or acidic (4.3 and 4.6)). Analysis of the water sorption isotherms indicated that decreasing the pH induced the increase of the water activity of lactose crystallization for camel and bovine whey powders. Finally, decreasing the pH led to the decrease of the glass transition temperature of camel and bovine whey powder (at 0.13, 0.23, and 0.33 of water activity).
Identifiants
pubmed: 32683259
pii: S0308-8146(20)31376-5
doi: 10.1016/j.foodchem.2020.127514
pii:
doi:
Substances chimiques
Lactoglobulins
0
Powders
0
Whey Proteins
0
Water
059QF0KO0R
Lactose
J2B2A4N98G
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
127514Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.