| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5133191 | Food Chemistry | 2017 | 10 Pages |
â¢No protein subunits in globulin and prolamin fractions.â¢No peaks appeared in RP-HPLC chromatograms of globulin for either species.â¢Two predominant peaks in the RP-HPLC profiles of all protein fractions.â¢Highest antioxidant activity (AA) of hydrolyzed protein fractions in glutelin-2.â¢Optimum ACE and AA values of separated peptides (RP-HPLC) in glutein-2 and albumin.
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 4Â h via pepsin hydrolysis in globulin fraction of Nigella damascena. Highest antioxidant activities of hydrolyzed protein fractions were found in glutelin-2 for both species.
