Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 498310
Title Recovery of protein from green leaves : Overview of crucial steps for utilisation
Author(s) Tamayo Tenorio, Angelica; Gieteling, Jarno; Jong, Govardus A.H. De; Boom, Remko M.; Goot, Atze J. Van Der
Source Food Chemistry 203 (2016). - ISSN 0308-8146 - p. 402 - 408.
DOI https://doi.org/10.1016/j.foodchem.2016.02.092
Department(s) Food Process Engineering
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) Dry matter composition - Leaf biorefinery - Membrane proteins - Protein extraction
Abstract

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.

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