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Sökning: id:"swepub:oai:DiVA.org:kth-345743" > Enhancement of myof...

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

Zhao, Yadong, 1985- (författare)
KTH,Fiber- och polymerteknologi,School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Wei, Kun (författare)
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Chen, Junliang (författare)
College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, Henan, China, Henan
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Wei, Ganping (författare)
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Li, Jiajia (författare)
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Zheng, Bin (författare)
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Song, Yan (författare)
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
Gao, Pingping (författare)
Faculty of Applied Sciences, Universiti Teknologi MARA, Kota Samarahan 94300, Sarawak, Malaysia, Sarawak
Zhou, Rusen (författare)
School of Chemical and Biomolecular Engineering, University of Sydney, Sydney 2006, Australia
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 (creator_code:org_t)
Elsevier BV, 2024
2024
Engelska.
Ingår i: Lebensmittel-Wissenschaft + Technologie. - : Elsevier BV. - 0023-6438 .- 1096-1127. ; 198
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • 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.

Ämnesord

TEKNIK OCH TEKNOLOGIER  -- Annan teknik -- Livsmedelsteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Other Engineering and Technologies -- Food Engineering (hsv//eng)
NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

Gel property
Gelation
Pea protein
Soy isolate protein
Surimi gel
Wheat gluten

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