To characterize the high-value protein content and to discover new bioactive peptides, present in edible organisms, as silkworm pupae, semiquantitative analytical approach has been applied. The combination of appropriate protein extraction methods, semiquantitative high-resolution mass spectrometry analyses of peptides, in silico bioactivity and gene ontology analyses, allowed protein profiling of silkworm pupae (778 gene products) and the characterization of bioactive peptides. The semiquantitative analysis, based on the measurement of the emPAI, revealed the presence of high-abundance class of proteins, such as larval storage protein (LSP) class. This class of proteins, beside its nutrient reservoir activity, is of great pharmaceutical interest for their efficacy in cardiovascular diseases. Potential allergens were also characterized and quantified, such as arginine kinase, thiol peroxiredoxin, and Bom m 9. This powerful bioanalytical approach proved the potential industrial applications of Bombyx mori pupae, as source of high-value proteins in a green and "circular" economy perspective.

Silkworm pupae as source of high-value edible proteins and of bioactive peptides / A.A. Altomare, G. Baron, G. Aldini, M. Carini, A. D'Amato. - In: FOOD SCIENCE & NUTRITION. - ISSN 2048-7177. - 8:6(2020 Jun), pp. 2652-2661. [10.1002/fsn3.1546]

Silkworm pupae as source of high-value edible proteins and of bioactive peptides

A.A. Altomare
Primo
;
G. Baron
Secondo
;
G. Aldini;M. Carini
Penultimo
;
A. D'Amato
Ultimo
2020

Abstract

To characterize the high-value protein content and to discover new bioactive peptides, present in edible organisms, as silkworm pupae, semiquantitative analytical approach has been applied. The combination of appropriate protein extraction methods, semiquantitative high-resolution mass spectrometry analyses of peptides, in silico bioactivity and gene ontology analyses, allowed protein profiling of silkworm pupae (778 gene products) and the characterization of bioactive peptides. The semiquantitative analysis, based on the measurement of the emPAI, revealed the presence of high-abundance class of proteins, such as larval storage protein (LSP) class. This class of proteins, beside its nutrient reservoir activity, is of great pharmaceutical interest for their efficacy in cardiovascular diseases. Potential allergens were also characterized and quantified, such as arginine kinase, thiol peroxiredoxin, and Bom m 9. This powerful bioanalytical approach proved the potential industrial applications of Bombyx mori pupae, as source of high-value proteins in a green and "circular" economy perspective.
Bombyx mori; bioactive peptides; high‐resolution mass spectrometry; protein profiling; semiquantitative analyses
Settore CHIM/08 - Chimica Farmaceutica
giu-2020
19-mag-2020
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/953001
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