Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves
In this study, white mulberry (WM; Morus alba L.) and its leaf (WML) were hydrolyzed using enzymes at different preheating temperatures (50, 60, 70, 80, and 90 °C) with distilled water at a ratio of 1:10 (w/v). Pepsin, trypsin, chymotrypsin, and alcalase were employed for enzymatic hydrolysis, aimin...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024-06-01
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| Series: | Food Chemistry Advances |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2772753X23004185 |
| _version_ | 1797372006048464896 |
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| author | Fatma Tuba Kirac Didem Sahingil Ali Adnan Hayaloglu |
| author_facet | Fatma Tuba Kirac Didem Sahingil Ali Adnan Hayaloglu |
| author_sort | Fatma Tuba Kirac |
| collection | DOAJ |
| description | In this study, white mulberry (WM; Morus alba L.) and its leaf (WML) were hydrolyzed using enzymes at different preheating temperatures (50, 60, 70, 80, and 90 °C) with distilled water at a ratio of 1:10 (w/v). Pepsin, trypsin, chymotrypsin, and alcalase were employed for enzymatic hydrolysis, aiming to investigate the impact of heat treatment and enzymatic hydrolysis on bioactive properties; in particular, angiotensin-converting enzyme-inhibitory (ACE-i) and antioxidant activities. The highest hydrolysis efficiency was observed when using pepsin. The smaller peptides with <3 kDa had better ACE-i and antioxidant activities in both WM and WML samples. Regarding antioxidant activity, the highest level was identified at a preheating temperature of 90 °C in the WM sample, and at preheating temperatures of 50 °C and without heating in the WML samples. In conclusion, heat treatment and enzymatic hydrolysis were found to be a positive impact on ACE-i and antioxidant activities under various conditions. Moreover, the proteins derived from WM and WML were rich in the sources of potential ACE-i and antioxidant peptides. |
| first_indexed | 2024-03-08T18:29:11Z |
| format | Article |
| id | doaj.art-d3f97a85a9c043c3ab396e6ed72d6409 |
| institution | Directory Open Access Journal |
| issn | 2772-753X |
| language | English |
| last_indexed | 2024-03-08T18:29:11Z |
| publishDate | 2024-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry Advances |
| spelling | doaj.art-d3f97a85a9c043c3ab396e6ed72d64092023-12-30T04:45:26ZengElsevierFood Chemistry Advances2772-753X2024-06-014100597Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leavesFatma Tuba Kirac0Didem Sahingil1Ali Adnan Hayaloglu2Department of Food Engineering, Bursa Technical University, Bursa, 16310, Turkey; Department of Food Engineering, Inonu University, Malatya, 44280, Turkey; Corresponding author.Department of Food Engineering, Inonu University, Malatya, 44280, TurkeyDepartment of Food Engineering, Inonu University, Malatya, 44280, TurkeyIn this study, white mulberry (WM; Morus alba L.) and its leaf (WML) were hydrolyzed using enzymes at different preheating temperatures (50, 60, 70, 80, and 90 °C) with distilled water at a ratio of 1:10 (w/v). Pepsin, trypsin, chymotrypsin, and alcalase were employed for enzymatic hydrolysis, aiming to investigate the impact of heat treatment and enzymatic hydrolysis on bioactive properties; in particular, angiotensin-converting enzyme-inhibitory (ACE-i) and antioxidant activities. The highest hydrolysis efficiency was observed when using pepsin. The smaller peptides with <3 kDa had better ACE-i and antioxidant activities in both WM and WML samples. Regarding antioxidant activity, the highest level was identified at a preheating temperature of 90 °C in the WM sample, and at preheating temperatures of 50 °C and without heating in the WML samples. In conclusion, heat treatment and enzymatic hydrolysis were found to be a positive impact on ACE-i and antioxidant activities under various conditions. Moreover, the proteins derived from WM and WML were rich in the sources of potential ACE-i and antioxidant peptides.http://www.sciencedirect.com/science/article/pii/S2772753X23004185White mulberry (Morus Alba)ACE-i activityBioactive peptidesAntioxidantPlant protein |
| spellingShingle | Fatma Tuba Kirac Didem Sahingil Ali Adnan Hayaloglu Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves Food Chemistry Advances White mulberry (Morus Alba) ACE-i activity Bioactive peptides Antioxidant Plant protein |
| title | Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves |
| title_full | Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves |
| title_fullStr | Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves |
| title_full_unstemmed | Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves |
| title_short | Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves |
| title_sort | isolation and characterization of a new potential source of bioactive peptides white mulberry morus alba fruits and its leaves |
| topic | White mulberry (Morus Alba) ACE-i activity Bioactive peptides Antioxidant Plant protein |
| url | http://www.sciencedirect.com/science/article/pii/S2772753X23004185 |
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