Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities
The formation of advanced glycation end products (AGEs) is a pivotal factor in the development of various age-related and diabetes associated pathophysiologies, including but not limeted to arthritis, Alzheimer’s disease, atherosclerosis and cataracts. Consequently, the prospect of inhibiting AGE fo...
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Sakarya University
2024-12-01
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| Series: | Sakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi |
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| Online Access: | https://dergipark.org.tr/en/download/article-file/3976826 |
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| author | Ebru Kocadağ Kocazorbaz |
| author_facet | Ebru Kocadağ Kocazorbaz |
| author_sort | Ebru Kocadağ Kocazorbaz |
| collection | DOAJ |
| description | The formation of advanced glycation end products (AGEs) is a pivotal factor in the development of various age-related and diabetes associated pathophysiologies, including but not limeted to arthritis, Alzheimer’s disease, atherosclerosis and cataracts. Consequently, the prospect of inhibiting AGE formation emerges as a viable strategy to prevent or halt the advancement of diabetic complications. In the scientific literature, there is still a reluctance to produce bioactive peptides demonstrating antiglycation activity from breast milk. The breast milk protein was hydrolysed using trypsin for 240 min. The antiglycation, metal chelating activity, lipid peroxidation activity, and antioxidant activity of the peptides in the hydrolysates obtained after hydrolysis of human milk with trypsin enzyme were performed. The peptide diversity obtained after hydrolysis was determined by RP-HPLC. The breast milk hydrolysate was demonstrated significant antiglycation activity (IC50: 312.8 ± 12.1 µg/mL), antioxidant activity (61.8±4.58 mM AAE/µg peptide) , metal chelation activity (24.4%/μg peptide). The hydrolysate effectively inhibited lipid peroxidation (30.5±0.12%) compared to Trolox (51.2±0.3%). These findings highlight the potential of breast milk protein hydrolysates as a source of bioactive peptides with diverse health benefits. The present study offers valuable insights into utilizing human milk peptides as novel functional food components. |
| format | Article |
| id | doaj-art-693ebb889a314cbc9a75b3ddc447c856 |
| institution | DOAJ |
| issn | 2147-835X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Sakarya University |
| record_format | Article |
| series | Sakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi |
| spelling | doaj-art-693ebb889a314cbc9a75b3ddc447c8562025-08-20T03:16:32ZengSakarya UniversitySakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi2147-835X2024-12-012861178118710.16984/saufenbilder.149476928Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation ActivitiesEbru Kocadağ Kocazorbaz0https://orcid.org/0000-0001-5611-5235Ege üniversitesiThe formation of advanced glycation end products (AGEs) is a pivotal factor in the development of various age-related and diabetes associated pathophysiologies, including but not limeted to arthritis, Alzheimer’s disease, atherosclerosis and cataracts. Consequently, the prospect of inhibiting AGE formation emerges as a viable strategy to prevent or halt the advancement of diabetic complications. In the scientific literature, there is still a reluctance to produce bioactive peptides demonstrating antiglycation activity from breast milk. The breast milk protein was hydrolysed using trypsin for 240 min. The antiglycation, metal chelating activity, lipid peroxidation activity, and antioxidant activity of the peptides in the hydrolysates obtained after hydrolysis of human milk with trypsin enzyme were performed. The peptide diversity obtained after hydrolysis was determined by RP-HPLC. The breast milk hydrolysate was demonstrated significant antiglycation activity (IC50: 312.8 ± 12.1 µg/mL), antioxidant activity (61.8±4.58 mM AAE/µg peptide) , metal chelation activity (24.4%/μg peptide). The hydrolysate effectively inhibited lipid peroxidation (30.5±0.12%) compared to Trolox (51.2±0.3%). These findings highlight the potential of breast milk protein hydrolysates as a source of bioactive peptides with diverse health benefits. The present study offers valuable insights into utilizing human milk peptides as novel functional food components.https://dergipark.org.tr/en/download/article-file/3976826human milkbioactive peptidealzheimer’s diseaseantiglycation activitylipid peroxidation |
| spellingShingle | Ebru Kocadağ Kocazorbaz Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities Sakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi human milk bioactive peptide alzheimer’s disease antiglycation activity lipid peroxidation |
| title | Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities |
| title_full | Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities |
| title_fullStr | Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities |
| title_full_unstemmed | Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities |
| title_short | Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities |
| title_sort | exploring the functional potential of breast milk protein hydrolysates antiglycation antioxidant metal chelation and lipid peroxidation activities |
| topic | human milk bioactive peptide alzheimer’s disease antiglycation activity lipid peroxidation |
| url | https://dergipark.org.tr/en/download/article-file/3976826 |
| work_keys_str_mv | AT ebrukocadagkocazorbaz exploringthefunctionalpotentialofbreastmilkproteinhydrolysatesantiglycationantioxidantmetalchelationandlipidperoxidationactivities |