Enhancement of myofibrillar protein gelation by plant proteins for improved surimi gel characteristics: Mechanisms and performanceShow others and affiliations
2024 (English)In: Lebensmittel-Wissenschaft + Technologie, ISSN 0023-6438, E-ISSN 1096-1127, Vol. 198, article id 116045Article in journal (Refereed) Published
Abstract [en]
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.
Place, publisher, year, edition, pages
Elsevier BV , 2024. Vol. 198, article id 116045
Keywords [en]
Gel property, Gelation, Pea protein, Soy isolate protein, Surimi gel, Wheat gluten
National Category
Circular Food Process Technologies Food Biotechnology Biochemistry Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-345743DOI: 10.1016/j.lwt.2024.116045ISI: 001299460400001Scopus ID: 2-s2.0-85190070143OAI: oai:DiVA.org:kth-345743DiVA, id: diva2:1852519
Note
QC 20240424
2024-04-182024-04-182025-02-20Bibliographically approved