Structural features of myofibrillar fish protein interacting with phosphatidylcholine liposomes.
Infrared spectroscopy
Liposome
Muscle protein
Protein structure
Journal
Food research international (Ottawa, Ont.)
ISSN: 1873-7145
Titre abrégé: Food Res Int
Pays: Canada
ID NLM: 9210143
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
05
06
2020
revised:
20
08
2020
accepted:
06
09
2020
entrez:
25
11
2020
pubmed:
26
11
2020
medline:
15
5
2021
Statut:
ppublish
Résumé
The interactions between liposomes and fish myofibrillar protein (surimi ground salted protein, SURP) were evaluated. Liposomes prepared with ultrapure phosphatidylcholine (UPC) or partially purified phosphatidylcholine (PPC) were dispersed at different weight ratio on SURP. Changes in protein stability and structure were evaluated using FTIR, intrinsic fluorescence and free sulfhydryl groups, and changes in liposome properties were studied by dynamic light scattering and electron microscopy. PPC promoted denaturation and aggregation of SURP, reflected in secondary structure loss, exposure of tyrosine residues and increment of free sulfhydryl. UPC produced partial unfolding and changes in the secondary structure of SURP from α-helical to β-strand. Liposome size increased by about 40% and showed modified surface charge after SURP exposure, indicating the formation of protein corona. Surface charge and composition of liposomes influence SURP stability and could exert different effects on the myofibrillar protein network, which is important for liposome applications in surimi products.
Identifiants
pubmed: 33233262
pii: S0963-9969(20)30712-2
doi: 10.1016/j.foodres.2020.109687
pii:
doi:
Substances chimiques
Fish Proteins
0
Lecithins
0
Liposomes
0
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
109687Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.