This study aims to obtain a valuable mixture of short-chain peptides from hempseed as a new ingredient for developing nutraceutical and functional foods useful for preventing metabolic syndrome that represents the major cause of death globally.A dedicated analytical platform based on a purification step by size exclusion chromatography or ultrafil-tration membrane and high-resolution mass spectrometry was developed to isolate and comprehensively char-acterize short-chain peptides leading to the identification of more than 500 short-chain peptides. Our results indicated that the short-chain peptide mixture was about three times more active than the medium-chain peptide mixture and total hydrolysate with respect to measured inhibition of the angiotensin-converting enzyme. The short-chain peptide mixture was also two times more active as a dipeptidyl peptidase IV, and twofold more active on the cholesterol metabolism pathway through the modulation of low-density lipoprotein receptor.
Isolation and functional characterization of hemp seed protein-derived short- and medium-chain peptide mixtures with multifunctional properties for metabolic syndrome prevention / A. Cerrato, C. Lammi, A.L. Capriotti, C. Bollati, C. Cavaliere, C.M. Montone, M. Bartolomei, G. Boschin, J. Li, S. Piovesana, A. Arnoldi, A. Lagan(`a). - In: FOOD RESEARCH INTERNATIONAL. - ISSN 0963-9969. - 163:(2023 Jan), pp. 112219.1-112219.11. [10.1016/j.foodres.2022.112219]
Isolation and functional characterization of hemp seed protein-derived short- and medium-chain peptide mixtures with multifunctional properties for metabolic syndrome prevention
C. Lammi
Secondo
;C. Bollati;M. Bartolomei;G. Boschin;J. Li;A. ArnoldiPenultimo
;
2023
Abstract
This study aims to obtain a valuable mixture of short-chain peptides from hempseed as a new ingredient for developing nutraceutical and functional foods useful for preventing metabolic syndrome that represents the major cause of death globally.A dedicated analytical platform based on a purification step by size exclusion chromatography or ultrafil-tration membrane and high-resolution mass spectrometry was developed to isolate and comprehensively char-acterize short-chain peptides leading to the identification of more than 500 short-chain peptides. Our results indicated that the short-chain peptide mixture was about three times more active than the medium-chain peptide mixture and total hydrolysate with respect to measured inhibition of the angiotensin-converting enzyme. The short-chain peptide mixture was also two times more active as a dipeptidyl peptidase IV, and twofold more active on the cholesterol metabolism pathway through the modulation of low-density lipoprotein receptor.File | Dimensione | Formato | |
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