TY - JOUR
T1 - Recovery of protein from green leaves
T2 - Overview of crucial steps for utilisation
AU - Tamayo Tenorio, Angelica
AU - Gieteling, Jarno
AU - De Jong, Govardus A.H.
AU - Boom, Remko M.
AU - Van Der Goot, Atze J.
PY - 2016
Y1 - 2016
N2 - Plant leaves are a major potential source of novel food proteins. Till now, leaf protein extraction methods mainly focus on the extraction of soluble proteins, like rubisco protein, leaving more than half of all protein unextracted. Here, we report on the total protein extraction from sugar beet leaves (Beta vulgaris L.) by a traditional thermal extraction method consisting of mechanical pressing, heating to 50 °C and centrifugation. The resulting streams (i.e. supernatant, green-protein pellet and fibrous pulp) were characterised in terms of composition, physical structure and processing options. The protein distributed almost equally over the supernatant, pellet and pulp. This shows that thermal precipitation is an unselective process with respect to fractionation between soluble (rubisco) and insoluble (other) proteins. About 6% of the total protein could be extracted as pure rubisco (90% purity) from the supernatant. Surfactants commonly used for protein solubilisation could hardly re-dissolve the precipitated proteins in the pellet phase, which suggested that irreversible association was induced between the co-precipitated proteins and cell debris. Thus, the extraction of this protein will require prevention of their co-precipitation, and should take place in the original juice solution.
AB - Plant leaves are a major potential source of novel food proteins. Till now, leaf protein extraction methods mainly focus on the extraction of soluble proteins, like rubisco protein, leaving more than half of all protein unextracted. Here, we report on the total protein extraction from sugar beet leaves (Beta vulgaris L.) by a traditional thermal extraction method consisting of mechanical pressing, heating to 50 °C and centrifugation. The resulting streams (i.e. supernatant, green-protein pellet and fibrous pulp) were characterised in terms of composition, physical structure and processing options. The protein distributed almost equally over the supernatant, pellet and pulp. This shows that thermal precipitation is an unselective process with respect to fractionation between soluble (rubisco) and insoluble (other) proteins. About 6% of the total protein could be extracted as pure rubisco (90% purity) from the supernatant. Surfactants commonly used for protein solubilisation could hardly re-dissolve the precipitated proteins in the pellet phase, which suggested that irreversible association was induced between the co-precipitated proteins and cell debris. Thus, the extraction of this protein will require prevention of their co-precipitation, and should take place in the original juice solution.
KW - Dry matter composition
KW - Leaf biorefinery
KW - Membrane proteins
KW - Protein extraction
U2 - 10.1016/j.foodchem.2016.02.092
DO - 10.1016/j.foodchem.2016.02.092
M3 - Article
AN - SCOPUS:84958825042
SN - 0308-8146
VL - 203
SP - 402
EP - 408
JO - Food Chemistry
JF - Food Chemistry
ER -