Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support
Bioactive peptides are produced by isolating and enriching them from food protein hydrolysates, which serve as functional food ingredients aimed at disease prevention and health maintenance. However, the manufacturing process is complex and costly, creating opportunities for further development. In...
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Taylor & Francis Group
2025-12-01
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| Series: | Journal of Chemical Engineering of Japan |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/00219592.2025.2501969 |
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| author | Yuta Matsunaga Hirokazu Akiyama Kazunori Shimizu Hiroyuki Honda |
| author_facet | Yuta Matsunaga Hirokazu Akiyama Kazunori Shimizu Hiroyuki Honda |
| author_sort | Yuta Matsunaga |
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| description | Bioactive peptides are produced by isolating and enriching them from food protein hydrolysates, which serve as functional food ingredients aimed at disease prevention and health maintenance. However, the manufacturing process is complex and costly, creating opportunities for further development. In this study, we focused on the bioactivity of pancreatic lipase inhibition and prepared casein pepsin hydrolysate (CPH) and soy protein pepsin hydrolysate (SPH). Both hydrolysates exhibited pancreatic lipase inhibitory (PLI) activity, and a comparison based on IC50 values showed that SPH had approximately six times higher activity than CPH. Amino acid composition analysis revealed that SPH contained a higher proportion of small side-chain amino acids such as glycine (G) and alanine (A), as well as basic amino acid residues such as histidine (H), lysine (K), and arginine (R). Therefore, we attempted to enrich peptides containing basic amino acid residues using heat treated porous silica gel (HTSG), which allows selective adsorption and desorption of these peptides. As a result, the PLI activity of both hydrolysates increased, with SPH exhibiting approximately three times higher activity than before enrichment. LC-MS/MS analysis before and after enrichment identified 772 peptides from CPH and 1354 peptides from SPH. To assess the enrichment effect, we calculated the enrichment ratio and synthesized 20 peptides with the highest enrichment ratios to evaluate their PLI activity. Nine of these peptides exhibited PLI activity, revealing a trend that peptides with higher enrichment ratios tended to show stronger activity. These findings demonstrate that considering amino acid residue bias and performing group-specific peptide enrichment enables the simple acquisition of highly bioactive peptide mixtures and the identification of highly active sequences. This approach holds promise as a novel production method for bioactive peptides. |
| format | Article |
| id | doaj-art-73e61d1d57fd4954b677e1b3749bb5c4 |
| institution | Kabale University |
| issn | 0021-9592 1881-1299 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
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| series | Journal of Chemical Engineering of Japan |
| spelling | doaj-art-73e61d1d57fd4954b677e1b3749bb5c42025-08-20T03:47:28ZengTaylor & Francis GroupJournal of Chemical Engineering of Japan0021-95921881-12992025-12-0158110.1080/00219592.2025.2501969Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption SupportYuta Matsunaga0Hirokazu Akiyama1Kazunori Shimizu2Hiroyuki Honda3Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603, JapanDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603, JapanDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603, JapanDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603, JapanBioactive peptides are produced by isolating and enriching them from food protein hydrolysates, which serve as functional food ingredients aimed at disease prevention and health maintenance. However, the manufacturing process is complex and costly, creating opportunities for further development. In this study, we focused on the bioactivity of pancreatic lipase inhibition and prepared casein pepsin hydrolysate (CPH) and soy protein pepsin hydrolysate (SPH). Both hydrolysates exhibited pancreatic lipase inhibitory (PLI) activity, and a comparison based on IC50 values showed that SPH had approximately six times higher activity than CPH. Amino acid composition analysis revealed that SPH contained a higher proportion of small side-chain amino acids such as glycine (G) and alanine (A), as well as basic amino acid residues such as histidine (H), lysine (K), and arginine (R). Therefore, we attempted to enrich peptides containing basic amino acid residues using heat treated porous silica gel (HTSG), which allows selective adsorption and desorption of these peptides. As a result, the PLI activity of both hydrolysates increased, with SPH exhibiting approximately three times higher activity than before enrichment. LC-MS/MS analysis before and after enrichment identified 772 peptides from CPH and 1354 peptides from SPH. To assess the enrichment effect, we calculated the enrichment ratio and synthesized 20 peptides with the highest enrichment ratios to evaluate their PLI activity. Nine of these peptides exhibited PLI activity, revealing a trend that peptides with higher enrichment ratios tended to show stronger activity. These findings demonstrate that considering amino acid residue bias and performing group-specific peptide enrichment enables the simple acquisition of highly bioactive peptide mixtures and the identification of highly active sequences. This approach holds promise as a novel production method for bioactive peptides.https://www.tandfonline.com/doi/10.1080/00219592.2025.2501969Bioactive peptideFood protein hydrolysisPancreas lipase inhibitionPorous silica gelEnrichment |
| spellingShingle | Yuta Matsunaga Hirokazu Akiyama Kazunori Shimizu Hiroyuki Honda Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support Journal of Chemical Engineering of Japan Bioactive peptide Food protein hydrolysis Pancreas lipase inhibition Porous silica gel Enrichment |
| title | Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support |
| title_full | Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support |
| title_fullStr | Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support |
| title_full_unstemmed | Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support |
| title_short | Enrichment and Identification of Pancreas Lipase Inhibitory Peptides from Food Protein Hydrolysate Using Group-Selective Peptide Adsorption Support |
| title_sort | enrichment and identification of pancreas lipase inhibitory peptides from food protein hydrolysate using group selective peptide adsorption support |
| topic | Bioactive peptide Food protein hydrolysis Pancreas lipase inhibition Porous silica gel Enrichment |
| url | https://www.tandfonline.com/doi/10.1080/00219592.2025.2501969 |
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