Molecular characterization and bio-functional property determination using SDS-PAGE and RP-HPLC of protein fractions from two Nigella species.
This study aimed to investigate the molecular and bio-functional properties of protein fractions from Nigella damascena and Nigella arvensis, including the albumin, globulin, glutein-1, glutein-2 and prolamin fractions. Protein subunits were not observed in globulin and prolamin fractions. No peaks appeared in RP-HPLC chromatograms of globulin for either species. Two predominant peaks were observed in the RP-HPLC profiles of all protein fractions. Proteins separated by RP-HPLC have potential inhibitory and antioxidant activities in all fractions. Optimum ACE-inhibitory and antioxidant activities of proteins separated by RP-HPLC were observed in glutein-2 and albumin, respectively, for both species. For pepsin and combined pepsin-trypsin hydrolyses, the highest degree of hydrolysis (DH) was obtained in glutein-2 fraction of Nigella arvensis. Highest ACE-inhibitory activity of hydrolyzed protein fractions was found at 4h via pepsin hydrolysis in globulin fraction of Nigella damascena. Highest antioxidant activities of hydrolyzed protein fractions were found in glutelin-2 for both species.
["Alu'datt|Muhammad H|MH|", 'Rababah|Taha|T|', 'Alhamad|Mohammad N|MN|', "Alodat|Moh'd|M|", 'Al-Mahasneh|Majdi A|MA|', 'Gammoh|Sana|S|', 'Ereifej|Khalil|K|', 'Almajwal|Ali|A|', 'Kubow|Stan|S|']
D000975:Antioxidants D002851:Chromatography, High Pressure Liquid D056148:Chromatography, Reverse-Phase D004591:Electrophoresis, Polyacrylamide Gel D006868:Hydrolysis D031844:Nigella D010940:Plant Proteins
Molecular Protein fractions Fractionation Nigella species Antioxidant activity Angiotensin converting enzyme RP-HPLC fractionation