In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties
Hydrolysates were produced using Alcalase (AH), chymotrypsin (CH), pepsin (PH), and trypsin (TH), and also fluted pumpkin leaf protein isolate (FLI) as a substrate. AH had the lowest degree of hydrolysis (16.37%) but exhibited overall superior antioxidant and enzyme inhibitory properties. Therefore,...
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Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences
2020-12-01
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| Series: | Polish Journal of Food and Nutrition Sciences |
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| Online Access: | http://www.journalssystem.com/pjfns/In-vitro-characterization-of-fluted-pumpkin-leaf-protein-hydrolysates-and-ultrafiltration,130401,0,2.html |
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| author | Akinsola Albert Famuwagun Adeola Monisola Alashi Saka Olasunkanmi Gbadamosi Kehinde Adekunbi Taiwo Joseph Durodoluwa Oyedele Odunayo Clement Adebooye Rotimi Emmanuel Aluko |
| author_facet | Akinsola Albert Famuwagun Adeola Monisola Alashi Saka Olasunkanmi Gbadamosi Kehinde Adekunbi Taiwo Joseph Durodoluwa Oyedele Odunayo Clement Adebooye Rotimi Emmanuel Aluko |
| author_sort | Akinsola Albert Famuwagun |
| collection | DOAJ |
| description | Hydrolysates were produced using Alcalase (AH), chymotrypsin (CH), pepsin (PH), and trypsin (TH), and also fluted pumpkin leaf protein isolate (FLI) as a substrate. AH had the lowest degree of hydrolysis (16.37%) but exhibited overall superior antioxidant and enzyme inhibitory properties. Therefore, it was fractionated by membrane ultrafiltration to give 10 kDa peptide fractions. Gel permeation chromatography showed that the molecular weight of the FLI was 19.77 kDa and that of the hydrolysates was below 7.5 kDa. The hydrolysate peptides had a high content of hydrophobic amino acids but low levels of sulfur-containing amino acids, when compared to protein of FLI. Peptide sequence analysis showed that the hydrolysates consisted of dipeptides, tripeptides, and tetrapeptides with molecular weights below 500 Da. The hydrolysates were also stronger inhibitors of linoleic acid oxidation, α-amylase, α-glucosidase, and angiotensin converting enzyme (ACE) than FLI. Among the fractions, the <1 and 1-3 kDa were the most effective free radical scavengers and metal chelators in addition to their strong inhibitory activities against α-amylase, α-glucosidase, and ACE. We conclude that the AH and low molecular weight peptide fraction (<3 kDa) could find applications in formulating foods with various bioactive properties. |
| format | Article |
| id | doaj-art-8a4979faffbc46ce9699c14864bf1c08 |
| institution | Kabale University |
| issn | 2083-6007 |
| language | English |
| publishDate | 2020-12-01 |
| publisher | Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences |
| record_format | Article |
| series | Polish Journal of Food and Nutrition Sciences |
| spelling | doaj-art-8a4979faffbc46ce9699c14864bf1c082025-02-02T03:21:15ZengInstitute of Animal Reproduction and Food Research of the Polish Academy of SciencesPolish Journal of Food and Nutrition Sciences2083-60072020-12-0170442944310.31883/pjfns/130401130401In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory PropertiesAkinsola Albert Famuwagun0Adeola Monisola Alashi1Saka Olasunkanmi Gbadamosi2Kehinde Adekunbi Taiwo3Joseph Durodoluwa Oyedele4Odunayo Clement Adebooye5Rotimi Emmanuel Aluko6Department of Food and Human Nutritional Sciences, University of Manitoba, R3T 2N2 Winnipeg, CanadaDepartment of Food and Human Nutritional Sciences, University of Manitoba, R3T 2N2 Winnipeg, CanadaDepartment of Food Science & Technology, Obafemi Awolowo University, 220002 Ile-Ife, NigeriaDepartment of Food Science & Technology, Obafemi Awolowo University, 220002 Ile-Ife, NigeriaDepartment of Soil and Land Resources Management, Faculty of Agriculture, Obafemi Awolowo University, 220002 Ile-Ife, NigeriaDepartment of Agronomy, Faculty of Agriculture, Obafemi Awolowo University, 220002 Ile-Ife, NigeriaDepartment of Food and Human Nutritional Sciences, University of Manitoba, R3T 2N2 Winnipeg, CanadaHydrolysates were produced using Alcalase (AH), chymotrypsin (CH), pepsin (PH), and trypsin (TH), and also fluted pumpkin leaf protein isolate (FLI) as a substrate. AH had the lowest degree of hydrolysis (16.37%) but exhibited overall superior antioxidant and enzyme inhibitory properties. Therefore, it was fractionated by membrane ultrafiltration to give 10 kDa peptide fractions. Gel permeation chromatography showed that the molecular weight of the FLI was 19.77 kDa and that of the hydrolysates was below 7.5 kDa. The hydrolysate peptides had a high content of hydrophobic amino acids but low levels of sulfur-containing amino acids, when compared to protein of FLI. Peptide sequence analysis showed that the hydrolysates consisted of dipeptides, tripeptides, and tetrapeptides with molecular weights below 500 Da. The hydrolysates were also stronger inhibitors of linoleic acid oxidation, α-amylase, α-glucosidase, and angiotensin converting enzyme (ACE) than FLI. Among the fractions, the <1 and 1-3 kDa were the most effective free radical scavengers and metal chelators in addition to their strong inhibitory activities against α-amylase, α-glucosidase, and ACE. We conclude that the AH and low molecular weight peptide fraction (<3 kDa) could find applications in formulating foods with various bioactive properties.http://www.journalssystem.com/pjfns/In-vitro-characterization-of-fluted-pumpkin-leaf-protein-hydrolysates-and-ultrafiltration,130401,0,2.htmlfluted pumpkin leafprotein hydrolysatesmembrane ultrafiltrationantioxidant activityantidiabetic activityantihypertensive activity |
| spellingShingle | Akinsola Albert Famuwagun Adeola Monisola Alashi Saka Olasunkanmi Gbadamosi Kehinde Adekunbi Taiwo Joseph Durodoluwa Oyedele Odunayo Clement Adebooye Rotimi Emmanuel Aluko In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties Polish Journal of Food and Nutrition Sciences fluted pumpkin leaf protein hydrolysates membrane ultrafiltration antioxidant activity antidiabetic activity antihypertensive activity |
| title | In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties |
| title_full | In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties |
| title_fullStr | In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties |
| title_full_unstemmed | In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties |
| title_short | In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties |
| title_sort | in vitro characterization of fluted pumpkin leaf protein hydrolysates and ultrafiltration of peptide fractions antioxidant and enzyme inhibitory properties |
| topic | fluted pumpkin leaf protein hydrolysates membrane ultrafiltration antioxidant activity antidiabetic activity antihypertensive activity |
| url | http://www.journalssystem.com/pjfns/In-vitro-characterization-of-fluted-pumpkin-leaf-protein-hydrolysates-and-ultrafiltration,130401,0,2.html |
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