Extraction, gelation and microstructure of Bambara groundnut vicilins

C.F. Diedericks, Linda de Koning, Victoria A. Jideani, P. Venema, E. van der Linden

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Nowadays there is a growing interest in exploiting new sources of plant proteins as functional ingredients in food products. In recent years, Bambara groundnut (Vigna subterranea (L.) Verdc.) [BGN] has been explored as such a potential plant protein source, as a means of value-addition to this leguminous crop. To elucidate on the macroscopic functionality of BGN protein isolates, the focus of our study was on the extraction and characterisation of the vicilin protein fraction as the known major storage protein present in legume seeds. BGN vicilin had a high protein content (91%) and formed the largest component in relation to the other protein fractions. Together with molecular weight profiles obtained with gel electrophoresis and size-exclusion chromatography coupled with light scattering, the purity of vicilin and its presence as the predominant protein fraction in BGN black-eye seeds were confirmed. The isoelectric point (pH 5.3), solubility profile (highest solubility 86% at NaCl concentrations above 200 mM) and thermal denaturation temperature (92 °C) of BGN vicilin correspond to the range reported for other legume vicilins. Furthermore, the gelation behaviour of BGN vicilin gels was investigated using dynamic oscillatory measurements. These data were further analysed with scaling models, which revealed that fractal scaling was best suited for description of the BGN vicilin gel networks. The gel microstructures were visualised with confocal laser scanning and scanning electron microscopy.
LanguageEnglish
Article number105226
JournalFood Hydrocolloids
Volume97
Early online date18 Jul 2019
DOIs
Publication statusE-pub ahead of print - 18 Jul 2019

Fingerprint

Vigna subterranea
vicilin
Gelation
gelation
microstructure
Proteins
Microstructure
Gels
plant source protein
Plant Proteins
gels
Fabaceae
Solubility
Seed
solubility
Seeds
legumes
Fractals
Denaturation
Size exclusion chromatography

Keywords

  • Bambara groundnut
  • Vicilin
  • Plant protein
  • Fractal dimension
  • Scaling

Cite this

@article{4b1cd2856c3b45efa60999520d69b361,
title = "Extraction, gelation and microstructure of Bambara groundnut vicilins",
abstract = "Nowadays there is a growing interest in exploiting new sources of plant proteins as functional ingredients in food products. In recent years, Bambara groundnut (Vigna subterranea (L.) Verdc.) [BGN] has been explored as such a potential plant protein source, as a means of value-addition to this leguminous crop. To elucidate on the macroscopic functionality of BGN protein isolates, the focus of our study was on the extraction and characterisation of the vicilin protein fraction as the known major storage protein present in legume seeds. BGN vicilin had a high protein content (91{\%}) and formed the largest component in relation to the other protein fractions. Together with molecular weight profiles obtained with gel electrophoresis and size-exclusion chromatography coupled with light scattering, the purity of vicilin and its presence as the predominant protein fraction in BGN black-eye seeds were confirmed. The isoelectric point (pH 5.3), solubility profile (highest solubility 86{\%} at NaCl concentrations above 200 mM) and thermal denaturation temperature (92 °C) of BGN vicilin correspond to the range reported for other legume vicilins. Furthermore, the gelation behaviour of BGN vicilin gels was investigated using dynamic oscillatory measurements. These data were further analysed with scaling models, which revealed that fractal scaling was best suited for description of the BGN vicilin gel networks. The gel microstructures were visualised with confocal laser scanning and scanning electron microscopy.",
keywords = "Bambara groundnut, Vicilin, Plant protein, Fractal dimension, Scaling",
author = "C.F. Diedericks and {de Koning}, Linda and Jideani, {Victoria A.} and P. Venema and {van der Linden}, E.",
year = "2019",
month = "7",
day = "18",
doi = "10.1016/j.foodhyd.2019.105226",
language = "English",
volume = "97",
journal = "Food Hydrocolloids",
issn = "0268-005X",
publisher = "Elsevier",

}

Extraction, gelation and microstructure of Bambara groundnut vicilins. / Diedericks, C.F.; de Koning, Linda; Jideani, Victoria A.; Venema, P.; van der Linden, E.

In: Food Hydrocolloids, Vol. 97, 105226, 12.2019.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Extraction, gelation and microstructure of Bambara groundnut vicilins

AU - Diedericks, C.F.

AU - de Koning, Linda

AU - Jideani, Victoria A.

AU - Venema, P.

AU - van der Linden, E.

PY - 2019/7/18

Y1 - 2019/7/18

N2 - Nowadays there is a growing interest in exploiting new sources of plant proteins as functional ingredients in food products. In recent years, Bambara groundnut (Vigna subterranea (L.) Verdc.) [BGN] has been explored as such a potential plant protein source, as a means of value-addition to this leguminous crop. To elucidate on the macroscopic functionality of BGN protein isolates, the focus of our study was on the extraction and characterisation of the vicilin protein fraction as the known major storage protein present in legume seeds. BGN vicilin had a high protein content (91%) and formed the largest component in relation to the other protein fractions. Together with molecular weight profiles obtained with gel electrophoresis and size-exclusion chromatography coupled with light scattering, the purity of vicilin and its presence as the predominant protein fraction in BGN black-eye seeds were confirmed. The isoelectric point (pH 5.3), solubility profile (highest solubility 86% at NaCl concentrations above 200 mM) and thermal denaturation temperature (92 °C) of BGN vicilin correspond to the range reported for other legume vicilins. Furthermore, the gelation behaviour of BGN vicilin gels was investigated using dynamic oscillatory measurements. These data were further analysed with scaling models, which revealed that fractal scaling was best suited for description of the BGN vicilin gel networks. The gel microstructures were visualised with confocal laser scanning and scanning electron microscopy.

AB - Nowadays there is a growing interest in exploiting new sources of plant proteins as functional ingredients in food products. In recent years, Bambara groundnut (Vigna subterranea (L.) Verdc.) [BGN] has been explored as such a potential plant protein source, as a means of value-addition to this leguminous crop. To elucidate on the macroscopic functionality of BGN protein isolates, the focus of our study was on the extraction and characterisation of the vicilin protein fraction as the known major storage protein present in legume seeds. BGN vicilin had a high protein content (91%) and formed the largest component in relation to the other protein fractions. Together with molecular weight profiles obtained with gel electrophoresis and size-exclusion chromatography coupled with light scattering, the purity of vicilin and its presence as the predominant protein fraction in BGN black-eye seeds were confirmed. The isoelectric point (pH 5.3), solubility profile (highest solubility 86% at NaCl concentrations above 200 mM) and thermal denaturation temperature (92 °C) of BGN vicilin correspond to the range reported for other legume vicilins. Furthermore, the gelation behaviour of BGN vicilin gels was investigated using dynamic oscillatory measurements. These data were further analysed with scaling models, which revealed that fractal scaling was best suited for description of the BGN vicilin gel networks. The gel microstructures were visualised with confocal laser scanning and scanning electron microscopy.

KW - Bambara groundnut

KW - Vicilin

KW - Plant protein

KW - Fractal dimension

KW - Scaling

U2 - 10.1016/j.foodhyd.2019.105226

DO - 10.1016/j.foodhyd.2019.105226

M3 - Article

VL - 97

JO - Food Hydrocolloids

T2 - Food Hydrocolloids

JF - Food Hydrocolloids

SN - 0268-005X

M1 - 105226

ER -