Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities
Tryptic WPHs with considerable residual whey protein content intact were developed from two sheep/goat WPCs (65% and 80% protein) without pH control. Pasteurization was used to avoid denaturation. Changes in non-protein nitrogen (DH_TCASN), free amino groups (DH_TNBS), and major whey proteins were u...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-07-01
|
| Series: | Foods |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2304-8158/11/14/2103 |
| _version_ | 1797406336534708224 |
|---|---|
| author | Lambros Sakkas Eleni Lekaki Golfo Moatsou |
| author_facet | Lambros Sakkas Eleni Lekaki Golfo Moatsou |
| author_sort | Lambros Sakkas |
| collection | DOAJ |
| description | Tryptic WPHs with considerable residual whey protein content intact were developed from two sheep/goat WPCs (65% and 80% protein) without pH control. Pasteurization was used to avoid denaturation. Changes in non-protein nitrogen (DH_TCASN), free amino groups (DH_TNBS), and major whey proteins were used to investigate the degree and extent of hydrolysis. Antihypertensive potential (ACE-IA), radical scavenging (DPPH-RSA), and iron chelation (Fe-CA) were assessed. No statistically significant changes in pH (5.84–6.29) were observed during hydrolysis and storage. At the start of hydrolysis, DH_TCASN was ≅11% for both substrates whereas DH_TNBS was >10% and >5% for WP65 and WP80, respectively. After one-hour hydrolysis, DH_TCASN was ≅17% for both substrates and DH_TNBS was ≅15% and ≅11% for WP65 and WP80, respectively. The β-lactoglobulin, α-lactalbumin, and caseinomacropeptide of WP65 were hydrolyzed by 14 ± 1.3%, 73.9 ± 2.6% and 37 ± 2.6%. The respective values for WP80 were 14.9 ± 1.7%, 79.9 ± 1%, and 32.7 ± 4.8%. ACE-IA of the hydrolysates of both substrates was much higher (>80%) than that of controls (<10%). Hydrolysis, substrate type, and storage did not affect the DPPH-RSA (45–54%). Fe-CA of the WP65 and WP80 hydrolysates were ≅40% and ≅20%, respectively; a similar outcome was found in the respective controls. Refrigerated storage for 17 h did not affect the degree of hydrolysis and biofunctional activities. |
| first_indexed | 2024-03-09T03:24:54Z |
| format | Article |
| id | doaj.art-e386cd643f8e4792828a2a59d9eed82a |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T03:24:54Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-e386cd643f8e4792828a2a59d9eed82a2023-12-03T15:03:37ZengMDPI AGFoods2304-81582022-07-011114210310.3390/foods11142103Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant ActivitiesLambros Sakkas0Eleni Lekaki1Golfo Moatsou2Laboratory of Dairy Research, Department of Food Science and Human Nutrition, Agricultural University of Athens, Iera Odos 75, 11855 Athens, GreeceLaboratory of Dairy Research, Department of Food Science and Human Nutrition, Agricultural University of Athens, Iera Odos 75, 11855 Athens, GreeceLaboratory of Dairy Research, Department of Food Science and Human Nutrition, Agricultural University of Athens, Iera Odos 75, 11855 Athens, GreeceTryptic WPHs with considerable residual whey protein content intact were developed from two sheep/goat WPCs (65% and 80% protein) without pH control. Pasteurization was used to avoid denaturation. Changes in non-protein nitrogen (DH_TCASN), free amino groups (DH_TNBS), and major whey proteins were used to investigate the degree and extent of hydrolysis. Antihypertensive potential (ACE-IA), radical scavenging (DPPH-RSA), and iron chelation (Fe-CA) were assessed. No statistically significant changes in pH (5.84–6.29) were observed during hydrolysis and storage. At the start of hydrolysis, DH_TCASN was ≅11% for both substrates whereas DH_TNBS was >10% and >5% for WP65 and WP80, respectively. After one-hour hydrolysis, DH_TCASN was ≅17% for both substrates and DH_TNBS was ≅15% and ≅11% for WP65 and WP80, respectively. The β-lactoglobulin, α-lactalbumin, and caseinomacropeptide of WP65 were hydrolyzed by 14 ± 1.3%, 73.9 ± 2.6% and 37 ± 2.6%. The respective values for WP80 were 14.9 ± 1.7%, 79.9 ± 1%, and 32.7 ± 4.8%. ACE-IA of the hydrolysates of both substrates was much higher (>80%) than that of controls (<10%). Hydrolysis, substrate type, and storage did not affect the DPPH-RSA (45–54%). Fe-CA of the WP65 and WP80 hydrolysates were ≅40% and ≅20%, respectively; a similar outcome was found in the respective controls. Refrigerated storage for 17 h did not affect the degree of hydrolysis and biofunctional activities.https://www.mdpi.com/2304-8158/11/14/2103WPHsheep/goat whey WPCtrypsin hydrolysisdegree of hydrolysisACE inhibitory activityDPPH radical scavenging activity |
| spellingShingle | Lambros Sakkas Eleni Lekaki Golfo Moatsou Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities Foods WPH sheep/goat whey WPC trypsin hydrolysis degree of hydrolysis ACE inhibitory activity DPPH radical scavenging activity |
| title | Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities |
| title_full | Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities |
| title_fullStr | Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities |
| title_full_unstemmed | Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities |
| title_short | Whey Protein Hydrolysates of Sheep/Goat Origin Produced by the Action of Trypsin without pH Control: Degree of Hydrolysis, Antihypertensive Potential and Antioxidant Activities |
| title_sort | whey protein hydrolysates of sheep goat origin produced by the action of trypsin without ph control degree of hydrolysis antihypertensive potential and antioxidant activities |
| topic | WPH sheep/goat whey WPC trypsin hydrolysis degree of hydrolysis ACE inhibitory activity DPPH radical scavenging activity |
| url | https://www.mdpi.com/2304-8158/11/14/2103 |
| work_keys_str_mv | AT lambrossakkas wheyproteinhydrolysatesofsheepgoatoriginproducedbytheactionoftrypsinwithoutphcontroldegreeofhydrolysisantihypertensivepotentialandantioxidantactivities AT elenilekaki wheyproteinhydrolysatesofsheepgoatoriginproducedbytheactionoftrypsinwithoutphcontroldegreeofhydrolysisantihypertensivepotentialandantioxidantactivities AT golfomoatsou wheyproteinhydrolysatesofsheepgoatoriginproducedbytheactionoftrypsinwithoutphcontroldegreeofhydrolysisantihypertensivepotentialandantioxidantactivities |