TY - JOUR
T1 - In vitro protein digestibility of RuBisCO from alfalfa obtained from different processing histories
T2 - Insights from free N-terminal and mass spectrometry study
AU - Tanambell, Hart
AU - Danielsen, Marianne
AU - Gulbrandsen Devold, Tove
AU - Møller, Anders Hauer
AU - Dalsgaard, Trine Kastrup
PY - 2024/2
Y1 - 2024/2
N2 - 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.
AB - 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.
KW - Alfalfa
KW - Alternative protein
KW - In vitro protein digestion
KW - Peptidomics
KW - Protein refinement
KW - RuBisCO
KW - Plant Proteins/metabolism
KW - Amino Acid Sequence
KW - Ribulose-Bisphosphate Carboxylase/chemistry
KW - Medicago sativa/metabolism
UR - http://www.scopus.com/inward/record.url?scp=85171615050&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2023.137301
DO - 10.1016/j.foodchem.2023.137301
M3 - Journal article
C2 - 37734151
SN - 0308-8146
VL - 434
JO - Food Chemistry
JF - Food Chemistry
M1 - 137301
ER -