Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance

Three commonly used plant proteins, soy isolate protein (SPI), wheat gluten (WG) and pea protein (PP), were incorporated into surimi gels, and their effects on myofibrillar protein gelation and resultant surimi gel properties have been investigated. Results revealed that addition of any of these pla...

Full description

Bibliographic Details
Published in:LWT
Main Author: Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
Format: Article
Language:English
Published: Academic Press 2024
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85190070143&doi=10.1016%2fj.lwt.2024.116045&partnerID=40&md5=4f0ca5353793395f2af9bac807c28e65
id 2-s2.0-85190070143
spelling 2-s2.0-85190070143
Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
2024
LWT
198

10.1016/j.lwt.2024.116045
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85190070143&doi=10.1016%2fj.lwt.2024.116045&partnerID=40&md5=4f0ca5353793395f2af9bac807c28e65
Three commonly used plant proteins, soy isolate protein (SPI), wheat gluten (WG) and pea protein (PP), were incorporated into surimi gels, and their effects on myofibrillar protein gelation and resultant surimi gel properties have been investigated. Results revealed that addition of any of these plant proteins at 5 g/100 g surimi enhanced the surimi gelation, among which SPI addition resulted in smoother, denser and whiter surimi gels (whiteness of 61.49) with superior textural attributes (hardness of 1994 g), water-holding capacity (85.67%) and structural integrity. Such improvements were attributed to the uniform distribution of SPI solution between adjacent surimi protein molecules, not only aiding in maintaining the matrix's continuity but bridging the interaction between the proteins. SPI with a higher content of charged amino acids (47.17%) exhibited a better ability to interact with the charged N- and C- terminals of surimi proteins. This interaction promoted the complete unfolding of surimi proteins, facilitated the conversion of α-helix to β structures, exposing hydrophobic ends and sulfhydryl groups, and consequently enhanced the formation of hydrophobic interactions and disulfide bonds during gelation. This study demonstrated that plant proteins, especially SPI, are effective gel-reinforcing additives in surimi gels, offering insights for developing plant protein-rich surimi products. © 2024 The Authors
Academic Press
236438
English
Article
All Open Access; Gold Open Access
author Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
spellingShingle Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
author_facet Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
author_sort Zhao Y.; Wei K.; Chen J.; Wei G.; Li J.; Zheng B.; Song Y.; Gao P.; Zhou R.
title Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
title_short Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
title_full Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
title_fullStr Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
title_full_unstemmed Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
title_sort Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performance
publishDate 2024
container_title LWT
container_volume 198
container_issue
doi_str_mv 10.1016/j.lwt.2024.116045
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-85190070143&doi=10.1016%2fj.lwt.2024.116045&partnerID=40&md5=4f0ca5353793395f2af9bac807c28e65
description Three commonly used plant proteins, soy isolate protein (SPI), wheat gluten (WG) and pea protein (PP), were incorporated into surimi gels, and their effects on myofibrillar protein gelation and resultant surimi gel properties have been investigated. Results revealed that addition of any of these plant proteins at 5 g/100 g surimi enhanced the surimi gelation, among which SPI addition resulted in smoother, denser and whiter surimi gels (whiteness of 61.49) with superior textural attributes (hardness of 1994 g), water-holding capacity (85.67%) and structural integrity. Such improvements were attributed to the uniform distribution of SPI solution between adjacent surimi protein molecules, not only aiding in maintaining the matrix's continuity but bridging the interaction between the proteins. SPI with a higher content of charged amino acids (47.17%) exhibited a better ability to interact with the charged N- and C- terminals of surimi proteins. This interaction promoted the complete unfolding of surimi proteins, facilitated the conversion of α-helix to β structures, exposing hydrophobic ends and sulfhydryl groups, and consequently enhanced the formation of hydrophobic interactions and disulfide bonds during gelation. This study demonstrated that plant proteins, especially SPI, are effective gel-reinforcing additives in surimi gels, offering insights for developing plant protein-rich surimi products. © 2024 The Authors
publisher Academic Press
issn 236438
language English
format Article
accesstype All Open Access; Gold Open Access
record_format scopus
collection Scopus
_version_ 1809677769166028800