Your browser doesn't support javascript.
loading
The interplay of muscle and pea proteins in low-salt gels: An insight into in situ structure formation in hybrid meat alternatives.
Nie, Yunqing; Xiong, Youling L; Jiang, Jiang.
Afiliación
  • Nie Y; State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
  • Xiong YL; State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA. Electronic address: ylxiong@uky.edu.
  • Jiang J; State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: jiangjiang@jiangnan.edu.cn.
Food Chem ; 455: 139870, 2024 Oct 15.
Article en En | MEDLINE | ID: mdl-38850985
ABSTRACT
The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 â†’ 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T2 from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Guisantes / Geles / Proteínas Musculares Límite: Animals Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Guisantes / Geles / Proteínas Musculares Límite: Animals Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido