Complex coacervation of pea albumin-pectin and ovalbumin-pectin assessed by isothermal titration calorimeter and turbidimetry.
coacervates
complexation
pea protein
pectin
thermodynamic parameters
water soluble fractions
Journal
Journal of the science of food and agriculture
ISSN: 1097-0010
Titre abrégé: J Sci Food Agric
Pays: England
ID NLM: 0376334
Informations de publication
Date de publication:
Feb 2021
Feb 2021
Historique:
received:
13
01
2020
revised:
17
07
2020
accepted:
13
08
2020
pubmed:
14
8
2020
medline:
30
3
2021
entrez:
14
8
2020
Statut:
ppublish
Résumé
This study investigates the complexation of a pea albumin-rich fraction and ovalbumin with pectin of different degrees of esterification (DE) and blockiness (DB) as a function of pH and biopolymer mixing ratio by turbidimetric titration and isothermal titration calorimetry (ITC). Turbidimetric analysis found maximum complexation occurred at a mixing ratio of 4:1 for pea albumin with high methoxy pectin, 8:1 for pea albumin with low methoxy pectin, and 8:1 for ovalbumin with low methoxy pectin. In the case of ovalbumin with high methoxy pectin, interactions were very weak. The pectin with high levels of esterification and blockiness displayed greater interactions with the pea albumin in both turbidimetry and ITC. However, low methoxy pectin imparted better interactions with ovalbumin and displayed higher optical density values than high methoxy pectin. The current study indicated that the different thermodynamic parameters of PA-pectin complexes can be tuned by controlling the structural characteristics (DB, DE, and d-galacturonic acid) of the pectin. © 2020 Society of Chemical Industry.
Sections du résumé
BACKGROUND
BACKGROUND
This study investigates the complexation of a pea albumin-rich fraction and ovalbumin with pectin of different degrees of esterification (DE) and blockiness (DB) as a function of pH and biopolymer mixing ratio by turbidimetric titration and isothermal titration calorimetry (ITC).
RESULTS
RESULTS
Turbidimetric analysis found maximum complexation occurred at a mixing ratio of 4:1 for pea albumin with high methoxy pectin, 8:1 for pea albumin with low methoxy pectin, and 8:1 for ovalbumin with low methoxy pectin. In the case of ovalbumin with high methoxy pectin, interactions were very weak. The pectin with high levels of esterification and blockiness displayed greater interactions with the pea albumin in both turbidimetry and ITC. However, low methoxy pectin imparted better interactions with ovalbumin and displayed higher optical density values than high methoxy pectin.
CONCLUSIONS
CONCLUSIONS
The current study indicated that the different thermodynamic parameters of PA-pectin complexes can be tuned by controlling the structural characteristics (DB, DE, and d-galacturonic acid) of the pectin. © 2020 Society of Chemical Industry.
Substances chimiques
Albumins
0
Biopolymers
0
Plant Proteins
0
Pectins
89NA02M4RX
Ovalbumin
9006-59-1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1209-1217Subventions
Organisme : Natural Sciences and Engineering Research Council of Canada
ID : 2014-05661
Informations de copyright
© 2020 Society of Chemical Industry.
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