Recovery of soluble proteins from migratory locust (Locusta migratoria) and characterisation of their compositional and techno-functional properties

Edible insects emerged as an alternative source of high-quality proteins. Therefore, the effect of an extraction procedure for the recovery of migratory locust (Locusta migratoria) protein concentrate (MLPC) on the compositional characteristics and techno-functional properties was studied. The influ...

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Veröffentlicht in:Food research international 2018-04, Vol.106, p.271-279
Hauptverfasser: Purschke, Benedict, Tanzmeister, Helene, Meinlschmidt, Pia, Baumgartner, Sabine, Lauter, Kathrin, Jäger, Henry
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Sprache:eng
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Zusammenfassung:Edible insects emerged as an alternative source of high-quality proteins. Therefore, the effect of an extraction procedure for the recovery of migratory locust (Locusta migratoria) protein concentrate (MLPC) on the compositional characteristics and techno-functional properties was studied. The influence of pH value (2−10) and salt concentration (0, 1 and 3% w/v) on techno-functional properties was evaluated. Proteins were identified and characterized by RP-HPLC, SDS-PAGE and LC-MS/MS. The initial crude protein content of the whole locusts (65.9% on dry base) could be enhanced to 82.3% (MLPC). Solubility profiles of MLPC showed maximum solubility at pH9 (100%). Promising functionality comparable to egg white protein in terms of emulsifying activity at pH5, foamability at pH3 and 3% NaCl, and foam stability at pH9 were found. Consequently, MLPC offers a nutritious protein source with good functional properties at certain conditions, which could be used as food ingredient in a variety of food systems. [Display omitted] •Composition of L. migratoria protein was studied using HPLC, SDS-PAGE and LC-MS/MS.•LC-MS/MS analysis revealed high amounts of 3 unreviewed tubulin α/β fragments.•Migratory protein were rich in alanine, leucine and glutamine/glutamic acid.•A protein concentrate (82%db protein) with high protein solubility was prepared.•Functionality (emulsification and foamability) were comparable to egg white protein.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2017.12.067