Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates
The biological importance of antioxidant peptides was the focus of new natural sources of food preservatives. Bombyx mori pupae are considered a valuable by-product of the silk-reeling industry due to their high-quality protein content. This study aimed to purify and identify the antioxidant peptide...
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Format: | Article |
Language: | English |
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Elsevier
2024-07-01
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Series: | Biochemistry and Biophysics Reports |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580824000712 |
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author | Suttida Chukiatsiri Nattakarn Wongsrangsap Pichamon Kiatwuthinon Wannarat Phonphoem |
author_facet | Suttida Chukiatsiri Nattakarn Wongsrangsap Pichamon Kiatwuthinon Wannarat Phonphoem |
author_sort | Suttida Chukiatsiri |
collection | DOAJ |
description | The biological importance of antioxidant peptides was the focus of new natural sources of food preservatives. Bombyx mori pupae are considered a valuable by-product of the silk-reeling industry due to their high-quality protein content. This study aimed to purify and identify the antioxidant peptides obtained from enzymatically hydrolyzed B. mori pupae, which could be used as new sources of natural food preservatives. Among the prepared hydrolysates, pepsin hydrolysate with the highest antioxidant activities was purified sequentially using ultrafiltration and reversed-phase high-performance liquid chromatography (RP-HPLC). The DPPH radical scavenging and ferrous ion chelating activity were used to evaluate antioxidant activity. Fractions with high activity were further analyzed by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Three peptides were identified as Glu-Asn-Ile-Ile-Leu-Phe-Arg (ENIILFR), Leu-Asn-Lys-Asp-Leu-Met-Arg (LNKDLMR), and Met-Leu-Ile-Ile-Ile-Met-Arg (MLIIIMR), respectively. All three novel identified peptides exhibited significantly stronger antioxidant capacity than synthetic antioxidants used in the food industry, including butylated hydroxyanisole (BHA), and butylated hydroxytoluene (BHT). ENIILFR showed the best antioxidant activity. These findings indicate that the three peptides have potential applications as natural antioxidants in the food industry. |
first_indexed | 2024-04-24T12:51:40Z |
format | Article |
id | doaj.art-fc0a14d0bd414dfa882ded58a39c43e7 |
institution | Directory Open Access Journal |
issn | 2405-5808 |
language | English |
last_indexed | 2025-03-21T17:58:37Z |
publishDate | 2024-07-01 |
publisher | Elsevier |
record_format | Article |
series | Biochemistry and Biophysics Reports |
spelling | doaj.art-fc0a14d0bd414dfa882ded58a39c43e72024-06-11T04:10:36ZengElsevierBiochemistry and Biophysics Reports2405-58082024-07-0138101707Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysatesSuttida Chukiatsiri0Nattakarn Wongsrangsap1Pichamon Kiatwuthinon2Wannarat Phonphoem3Corresponding author. Department of Biochemistry, Faculty of Science, Kasetsart University, 50 Ngam Wong Wan Road, Ladyao, Chatuchak, 10900, Bangkok, Thailand.; Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, ThailandDepartment of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, ThailandDepartment of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, ThailandDepartment of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, ThailandThe biological importance of antioxidant peptides was the focus of new natural sources of food preservatives. Bombyx mori pupae are considered a valuable by-product of the silk-reeling industry due to their high-quality protein content. This study aimed to purify and identify the antioxidant peptides obtained from enzymatically hydrolyzed B. mori pupae, which could be used as new sources of natural food preservatives. Among the prepared hydrolysates, pepsin hydrolysate with the highest antioxidant activities was purified sequentially using ultrafiltration and reversed-phase high-performance liquid chromatography (RP-HPLC). The DPPH radical scavenging and ferrous ion chelating activity were used to evaluate antioxidant activity. Fractions with high activity were further analyzed by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Three peptides were identified as Glu-Asn-Ile-Ile-Leu-Phe-Arg (ENIILFR), Leu-Asn-Lys-Asp-Leu-Met-Arg (LNKDLMR), and Met-Leu-Ile-Ile-Ile-Met-Arg (MLIIIMR), respectively. All three novel identified peptides exhibited significantly stronger antioxidant capacity than synthetic antioxidants used in the food industry, including butylated hydroxyanisole (BHA), and butylated hydroxytoluene (BHT). ENIILFR showed the best antioxidant activity. These findings indicate that the three peptides have potential applications as natural antioxidants in the food industry.http://www.sciencedirect.com/science/article/pii/S2405580824000712Bombyx mori pupaeProtein hydrolysatesAntioxidant peptidesAntioxidant activity |
spellingShingle | Suttida Chukiatsiri Nattakarn Wongsrangsap Pichamon Kiatwuthinon Wannarat Phonphoem Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates Biochemistry and Biophysics Reports Bombyx mori pupae Protein hydrolysates Antioxidant peptides Antioxidant activity |
title | Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates |
title_full | Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates |
title_fullStr | Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates |
title_full_unstemmed | Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates |
title_short | Purification and identification of novel antioxidant peptides derived from Bombyx mori pupae hydrolysates |
title_sort | purification and identification of novel antioxidant peptides derived from bombyx mori pupae hydrolysates |
topic | Bombyx mori pupae Protein hydrolysates Antioxidant peptides Antioxidant activity |
url | http://www.sciencedirect.com/science/article/pii/S2405580824000712 |
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