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Updated: May 9, 2026
Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
In vitro protein digestibility of RuBisCO from alfalfa obtained from different processing histories: Insights from
Hartono Tanambell1, Marianne Danielsen2, Tove Gulbrandsen Devold3
1Department of Food Science, Faculty of Technical Sciences, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CiFOOD Aarhus University Centre for Innovative Food Research, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark.
Abstract:
Ribulose-1,5-bisphosphate-carboxylase/oxygenase (RuBisCO) from alfalfa is a potentially climate-friendly alternative protein with a promising amino acid composition. The balance between yield and purity is a challenge for alternative plant proteins, partly due to the naturally occurring antinutrients. Therefore, measuring the in vitro protein digestibility (IVPD) of RuBisCO with various purity levels is of interest. It was hypothesized that the digestibility of RuBisCO from alfalfa might vary with different processing histories and levels of refinement. To test this hypothesis, RuBisCO from alfalfa with 4 different processing histories were subjected to the INFOGEST IVPD protocol and measurement of free N-terminals and peptidomics. The result showed that the digestibility of RuBisCO was high regardless of the processing history and purity, as demonstrated by 77-99% sequence coverage in the gastric phase. In intestinal phase, increase of free N-terminals and lower sequence coverage (< 10%) indicated that the proteins were hydrolyzed to smaller peptides.
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