title: Antioxidant and ACE-inhibitory activities of hemp (Cannabis sativa L.) protein hydrolysates produced by the proteases AFP, HT, Pro-G, actinidin and zingibain.
abstract: Hemp protein isolates (HPIs) were hydrolysed by proteases (AFP, HT, ProG, actinidin and zingibain). The enzymatic hydrolysis of HPIs was evaluated through the degree of hydrolysis and SDS-PAGE profiles. The bioactive properties of the resultant hydrolysates (HPHs) were accessed through ORAC, DPPḢ scavenging and ACE-inhibitory activities. The physical properties of the resultant HPHs were evaluated for their particle sizes, zeta potential and surface hydrophobicity. HT had the highest rate of caseinolytic activity at the lowest concentration (0.1 mg mL(-1)) compared to other proteases that required concentration of 100 mg mL(-1) to achieve their maximum rate of caseinolytic activity. This led to the highest degree of hydrolysis of HPIs by HT in the SDS-PAGE profiles. Among all proteases and substrates, HT resulted in the highest bioactivities (ORAC, DPPḢ scavenging and ACE-inhibitory activities) generated from alkali extracted HPI in the shortest time (2 h) compared to the other protease preparations.
authors.affiliation: Department of Food Science, University of Otago, PO Box 56, Dunedin 9054, New Zealand. Electronic address: tehsuesiang@yahoo.com.
authors.forename: Sue-Siang
authors.initials: SS
authors.lastname: Teh
authors.affiliation: Department of Food Science, University of Otago, PO Box 56, Dunedin 9054, New Zealand.
authors.forename: Alaa El-Din A
authors.initials: AEA
authors.lastname: Bekhit
authors.affiliation: Department of Biochemistry, University of Otago, PO Box 56, Dunedin 9054, New Zealand.
authors.forename: Alan
authors.initials: A
authors.lastname: Carne
authors.affiliation: Department of Food Science, University of Otago, PO Box 56, Dunedin 9054, New Zealand.
authors.forename: John
authors.initials: J
authors.lastname: Birch
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000975:Antioxidants / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001713:Biphenyl Compounds / Q000737:chemistry; D002188:Cannabis / Q000737:chemistry*; D003546:Cysteine Endopeptidases / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D010316:Particle Size; D010447:Peptide Hydrolases / Q000737:chemistry*; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry; D010851:Picrates / Q000737:chemistry; D011492:Protein Hydrolysates / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D013499:Surface Properties
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D001713:Biphenyl Compounds; D010851:Picrates; D011492:Protein Hydrolysates; C004931:1,1-diphenyl-2-picrylhydrazyl; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A; D003546:Cysteine Endopeptidases; C018745:actinidain
keywords: ACE-inhibitory; Hemp protein isolates; ORAC; Proteases