Comparative study on molecular and higher-order structures of legume seed protein isolates: Lentil, mungbean and yellow pea. (15th June 2023)
- Record Type:
- Journal Article
- Title:
- Comparative study on molecular and higher-order structures of legume seed protein isolates: Lentil, mungbean and yellow pea. (15th June 2023)
- Main Title:
- Comparative study on molecular and higher-order structures of legume seed protein isolates: Lentil, mungbean and yellow pea
- Authors:
- Shrestha, Smriti
van 't Hag, Leonie
Haritos, Victoria
Dhital, Sushil - Abstract:
- Highlights: Globulin proteins' composition varied among legume seed protein. Lentils and pea globulin comprised of both legumin-like and vicilin-like. Mungbean globulins richer in vicilin-like protein. Globulin protein composition regulate the thermal stability. Protein secondary structure influenced by thermal processing. Abstract: 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 TransformHighlights: Globulin proteins' composition varied among legume seed protein. Lentils and pea globulin comprised of both legumin-like and vicilin-like. Mungbean globulins richer in vicilin-like protein. Globulin protein composition regulate the thermal stability. Protein secondary structure influenced by thermal processing. Abstract: 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. … (more)
- Is Part Of:
- Food chemistry. Volume 411(2023)
- Journal:
- Food chemistry
- Issue:
- Volume 411(2023)
- Issue Display:
- Volume 411, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 411
- Issue:
- 2023
- Issue Sort Value:
- 2023-0411-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-06-15
- Subjects:
- Globulin protein -- Secondary structure -- Thermal denaturation
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2023.135464 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25657.xml