TY - JOUR
T1 - Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics
T2 - Mechanisms and performance
AU - Zhao, Yadong
AU - Wei, Kun
AU - Chen, Junliang
AU - Wei, Ganping
AU - Li, Jiajia
AU - Zheng, Bin
AU - Song, Yan
AU - Gao, Pingping
AU - Zhou, Rusen
N1 - Publisher Copyright:
© 2024 The Authors
PY - 2024/4/15
Y1 - 2024/4/15
N2 - 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.
AB - 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.
KW - Gel property
KW - Gelation
KW - Pea protein
KW - Soy isolate protein
KW - Surimi gel
KW - Wheat gluten
UR - https://www.scopus.com/pages/publications/85190070143
U2 - 10.1016/j.lwt.2024.116045
DO - 10.1016/j.lwt.2024.116045
M3 - 文章
AN - SCOPUS:85190070143
SN - 0023-6438
VL - 198
JO - LWT
JF - LWT
M1 - 116045
ER -