Your browser doesn't support javascript.
loading
Comparative study on molecular and higher-order structures of legume seed protein isolates: Lentil, mungbean and yellow pea.
Shrestha, Smriti; van 't Hag, Leonie; Haritos, Victoria; Dhital, Sushil.
Afiliación
  • Shrestha S; Department of Chemical and Biological Engineering, Monash University, Clayton, VIC 3800, Australia.
  • van 't Hag L; Department of Chemical and Biological Engineering, Monash University, Clayton, VIC 3800, Australia. Electronic address: leonie.vanthag@monash.edu.
  • Haritos V; Department of Chemical and Biological Engineering, Monash University, Clayton, VIC 3800, Australia.
  • Dhital S; Department of Chemical and Biological Engineering, Monash University, Clayton, VIC 3800, Australia. Electronic address: sushil.dhital@monash.edu.
Food Chem ; 411: 135464, 2023 Jun 15.
Article en En | MEDLINE | ID: mdl-36669335
Lentils and mungbean proteins are under-researched compared to pea and soybean. Lentils (green, red and black-lentils), mungbean and yellow pea protein isolates were obtained by alkaline extraction (pH 9)-isoelectric precipitation (pH 4.5) and investigated for molecular and higher-order structures using complementary and novel approaches. These extracted isolates showed comparable protein content but significantly greater nitrogen solubility index (NSI > 85 %) than commercial pea and soy protein isolates (NSI < 60 %). Based on molecular weight estimations from sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis, the soluble proteins of lentils and yellow pea were identified as legumin-like and vicilin-like, while mungbean was dominated by vicilin-like proteins. The soluble extracts were confirmed to be in native structural condition by size exclusion chromatography and nano-differential scanning calorimetry, unlike commercial extracts. Further differences in secondary structure were evident on circular dichroism spectra of the soluble extracts and deconvolution of the Amide I region (1700-1600 cm-1) from Fourier Transform Infrared of the total protein.
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: Lens (Planta) / Vigna / Fabaceae Idioma: En Revista: Food Chem Año: 2023 Tipo del documento: Article País de afiliación: Australia 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: Lens (Planta) / Vigna / Fabaceae Idioma: En Revista: Food Chem Año: 2023 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Reino Unido