title: Peptide Fractions Obtained from Rice By-Products by Means of an Environment-Friendly Process Show In Vitro Health-Related Bioactivities.
abstract: Recently, the isolation of new health-related bioactive molecules derived from agro-food industrial by-products by means of environment-friendly extraction processes has become of particular interest. In the present study, a protein by-product from the rice starch industry was hydrolysed with five commercial proteolytic enzymes, avoiding the use of solvents or chemicals. The digestion processes were optimised, and the digestates were separated in fractions with four different molecular weight ranges by using a cross-flow membrane filtration technique. Total hydrolysates and fractions were tested in vitro for a wide range of biological activities. For the first time rice-derived peptides were assayed for anti-tyrosinase, anti-inflammatory, cytotoxicity and irritation capacities. Antioxidant and anti-hypertensive activities were also evaluated. Protamex, Alcalase and Neutrase treatments produced peptide fractions with valuable bioactivities without resulting cytotoxic or irritant. Highest levels of bioactivity were detected in Protamex-derived samples, followed by samples treated with Alcalase. Based on the present results, a future direct exploitation of isolated peptide fractions in the nutraceutical, functional food and cosmetic industrial fields may be foreseen.
authors.affiliation: Department of Biological Geological and Environmental Sciences, University of Bologna, Bologna, Italy.
authors.forename: Maura
authors.initials: M
authors.lastname: Ferri
authors.affiliation: Fraunhofer Institute for Environmental, Safety, and Energy Technology UMSICHT, Oberhausen, Germany.
authors.forename: Jürgen
authors.initials: J
authors.lastname: Graen-Heedfeld
authors.affiliation: Fraunhofer Institute for Environmental, Safety, and Energy Technology UMSICHT, Oberhausen, Germany.
authors.forename: Karlheinz
authors.initials: K
authors.lastname: Bretz
authors.affiliation: Cell Culture Laboratory, Sterlab, Vallauris, France.
authors.forename: Fabien
authors.initials: F
authors.lastname: Guillon
authors.affiliation: Department of Chemistry "G. Ciamician", University of Bologna, Bologna, Italy.
authors.forename: Elisa
authors.initials: E
authors.lastname: Michelini
authors.affiliation: Department of Chemistry "G. Ciamician", University of Bologna, Bologna, Italy.
authors.forename: Maria Maddalena
authors.initials: MM
authors.lastname: Calabretta
authors.affiliation: Carminia snc, Bologna, Italy.
authors.forename: Matteo
authors.initials: M
authors.lastname: Lamborghini
authors.affiliation: Department of Biological Geological and Environmental Sciences, University of Bologna, Bologna, Italy.
authors.forename: Nicolò
authors.initials: N
authors.lastname: Gruarin
authors.affiliation: Department of Chemistry "G. Ciamician", University of Bologna, Bologna, Italy.
authors.forename: Aldo
authors.initials: A
authors.lastname: Roda
authors.affiliation: Fraunhofer Institute for Environmental, Safety, and Energy Technology UMSICHT, Oberhausen, Germany.
authors.forename: Axel
authors.initials: A
authors.lastname: Kraft
authors.affiliation: Department of Biological Geological and Environmental Sciences, University of Bologna, Bologna, Italy.
authors.forename: Annalisa
authors.identifier: http://orcid.org/0000-0002-3541-4030
authors.initials: A
authors.lastname: Tassoni
mesh_terms: D012275:Oryza / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011492:Protein Hydrolysates / Q000378:metabolism*; D013381:Subtilisins
chemical_list: D010455:Peptides; D011492:Protein Hydrolysates; D010447:Peptide Hydrolases; D013381:Subtilisins