Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Obtained from Alcalase Protein Hydrolysate Fractions of Hemp ( Cannabis sativa L.) Bran.

Autor: Samaei SP; Department of Agricultural and Food Sciences, Alma Mater Studiorum, University of Bologna, Piazza Goidanich 60, 47521 Cesena, Italy., Martini S; Department of Life Sciences (DSV), University of Modena and Reggio Emilia, Via Amendola 2, 42122 Reggio Emilia, Italy., Tagliazucchi D; Department of Life Sciences (DSV), University of Modena and Reggio Emilia, Via Amendola 2, 42122 Reggio Emilia, Italy., Gianotti A; Department of Agricultural and Food Sciences, Alma Mater Studiorum, University of Bologna, Piazza Goidanich 60, 47521 Cesena, Italy.; CIRI (Interdepartmental Centre of Agri-Food Industrial Research), Alma Mater Studiorum, University of Bologna, Via Quinto Bucci 336, 47521 Cesena (FC), Italy., Babini E; Department of Agricultural and Food Sciences, Alma Mater Studiorum, University of Bologna, Piazza Goidanich 60, 47521 Cesena, Italy.; CIRI (Interdepartmental Centre of Agri-Food Industrial Research), Alma Mater Studiorum, University of Bologna, Via Quinto Bucci 336, 47521 Cesena (FC), Italy.
Jazyk: angličtina
Zdroj: Journal of agricultural and food chemistry [J Agric Food Chem] 2021 Aug 18; Vol. 69 (32), pp. 9220-9228. Date of Electronic Publication: 2021 Aug 05.
DOI: 10.1021/acs.jafc.1c01487
Abstrakt: Proteins from hemp bran (HPB), a byproduct of the hemp seed food-processing chain, were chemically extracted, hydrolyzed by Alcalase, and separated by membrane ultrafiltration into four fractions (MW <1, 1-3, 3-5, and >5 kDa). The antioxidant and antihypertensive properties of the initial extract and the fractions were evaluated by in vitro assays for their ability to scavenge radical species, bind with metal ions, reduce ferric ions, and inhibit angiotensin-converting enzyme (ACE) activity. Bioactive peptides were identified by high-resolution mass spectrometry and sequence comparison with BIOPEP and BioPep DB databases. The hydrolysate was strongly antioxidant and ACE-inhibiting; the most bioactive peptides were further concentrated by ultrafiltration. Of the 239 peptides identified, 47 (12 antioxidant and 35 ACE-inhibitory) exhibited structural features correlated with the specific bioactivity. These results highlight the promise of hydrolysate and size-based HPB fractions as natural functional ingredients for the food or pharmaceutical industry.
Databáze: MEDLINE