Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate
Yeast protein hydrolysate may be considered as a good source of bioactive peptides. Yeast hydrolysate was prepared by two different physical-enzymatic and autolysis treatments to identify the most active angiotensin I-converting enzyme (ACE) inhibitory and antioxidant peptides. The most active hydro...
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| Format: | Article |
| Language: | English |
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Elsevier
2015-12-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S175646461500448X |
| _version_ | 1818690713408241664 |
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| author | Mahta Mirzaei Saeed Mirdamadi Mohamad Reza Ehsani Mahmoud Aminlari Ebrahim Hosseini |
| author_facet | Mahta Mirzaei Saeed Mirdamadi Mohamad Reza Ehsani Mahmoud Aminlari Ebrahim Hosseini |
| author_sort | Mahta Mirzaei |
| collection | DOAJ |
| description | Yeast protein hydrolysate may be considered as a good source of bioactive peptides. Yeast hydrolysate was prepared by two different physical-enzymatic and autolysis treatments to identify the most active angiotensin I-converting enzyme (ACE) inhibitory and antioxidant peptides. The most active hydrolysate was obtained after sonication-trypsin hydrolysis. The hydrolysate was subjected to fractionation by ultrafiltration. Fraction with molecular weight of <3 kDa exhibited the highest activity. Reverse phase high performance liquid chromatography (RP-HPLC) resolved this fraction into five fractions, one of which (fraction F3) with amino acid sequence of Tyr-Gly-Lys-Pro-Val-Ala-Val-Pro-Ala-Arg (MW:1057.45 Da) exhibited ACE inhibitory (IC50 = 0.42 ± 0.02 mg/ml) and antioxidant activities (26.25 ± 0.13 µM TE/µg protein). Taken together, the results of this study show that S. cerevisiae proteins contain specific peptides in their sequences which can be released by enzymatic hydrolysis. These peptides have excellent bioactive properties that can potentially replace the antioxidant and antihypertensive agents with chemical origin. |
| first_indexed | 2024-12-17T12:30:22Z |
| format | Article |
| id | doaj.art-495a0f56e94444e7a0169d58c9bd2c46 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-17T12:30:22Z |
| publishDate | 2015-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-495a0f56e94444e7a0169d58c9bd2c462022-12-21T21:48:36ZengElsevierJournal of Functional Foods1756-46462015-12-0119259268Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysateMahta Mirzaei0Saeed Mirdamadi1Mohamad Reza Ehsani2Mahmoud Aminlari3Ebrahim Hosseini4Department of Food Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, IranDepartment of Biotechnology, Iranian Research Organization for Science & Technology (IROST), Tehran, Iran; Corresponding author. Department of Biotechnology, Iranian Research Organization for Science & Technology, Ehsani Rad St., Enqelab St., Parsa Sq., Ahmadabad Mostoufi Rd., Azadegan Highway, 3353 5111, Tehran, Iran. Tel.: +98 09121076460; fax: +982156275510.Department of Food Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, Iran; Corresponding author. Department of Food Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, Iran. Tel.: +98 09123308508; fax: +982144865464.Department of Biochemistry, School of Veterinary Medicine, Shiraz University, Shiraz, IranDepartment of Food Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, IranYeast protein hydrolysate may be considered as a good source of bioactive peptides. Yeast hydrolysate was prepared by two different physical-enzymatic and autolysis treatments to identify the most active angiotensin I-converting enzyme (ACE) inhibitory and antioxidant peptides. The most active hydrolysate was obtained after sonication-trypsin hydrolysis. The hydrolysate was subjected to fractionation by ultrafiltration. Fraction with molecular weight of <3 kDa exhibited the highest activity. Reverse phase high performance liquid chromatography (RP-HPLC) resolved this fraction into five fractions, one of which (fraction F3) with amino acid sequence of Tyr-Gly-Lys-Pro-Val-Ala-Val-Pro-Ala-Arg (MW:1057.45 Da) exhibited ACE inhibitory (IC50 = 0.42 ± 0.02 mg/ml) and antioxidant activities (26.25 ± 0.13 µM TE/µg protein). Taken together, the results of this study show that S. cerevisiae proteins contain specific peptides in their sequences which can be released by enzymatic hydrolysis. These peptides have excellent bioactive properties that can potentially replace the antioxidant and antihypertensive agents with chemical origin.http://www.sciencedirect.com/science/article/pii/S175646461500448XSaccharomyces cerevisiaeAntioxidant activityACE-inhibitoryProtein hydrolysatePeptide |
| spellingShingle | Mahta Mirzaei Saeed Mirdamadi Mohamad Reza Ehsani Mahmoud Aminlari Ebrahim Hosseini Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate Journal of Functional Foods Saccharomyces cerevisiae Antioxidant activity ACE-inhibitory Protein hydrolysate Peptide |
| title | Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate |
| title_full | Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate |
| title_fullStr | Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate |
| title_full_unstemmed | Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate |
| title_short | Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate |
| title_sort | purification and identification of antioxidant and ace inhibitory peptide from saccharomyces cerevisiae protein hydrolysate |
| topic | Saccharomyces cerevisiae Antioxidant activity ACE-inhibitory Protein hydrolysate Peptide |
| url | http://www.sciencedirect.com/science/article/pii/S175646461500448X |
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