Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle
Objective: Bioactive peptides with an inhibitory effect on dipeptidyl peptidase-IV (DPP-IV) were prepared from pearl mussel muscle. Methods: Two-step enzymatic hydrolysis was adopted and enzymatic hydrolysis conditions were optimized. Fractions with in vitro DPP-IV inhibitory activity were concentra...
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China Food Publishing Company
2024-09-01
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| Series: | Shipin Kexue |
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| Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2024-45-17-008.pdf |
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| author | ZHANG Chuhan, CHEN Yinge, MA Ting, WENG Ling, ZHANG Lingjing, ZHANG Genfang, CAO Minjie |
| author_facet | ZHANG Chuhan, CHEN Yinge, MA Ting, WENG Ling, ZHANG Lingjing, ZHANG Genfang, CAO Minjie |
| author_sort | ZHANG Chuhan, CHEN Yinge, MA Ting, WENG Ling, ZHANG Lingjing, ZHANG Genfang, CAO Minjie |
| collection | DOAJ |
| description | Objective: Bioactive peptides with an inhibitory effect on dipeptidyl peptidase-IV (DPP-IV) were prepared from pearl mussel muscle. Methods: Two-step enzymatic hydrolysis was adopted and enzymatic hydrolysis conditions were optimized. Fractions with in vitro DPP-IV inhibitory activity were concentrated by ultrafiltration, and purified by SuperdexTM peptide 10/300 GL gel filtration column chromatography and reverse phase-high performance liquid chromatography (RP-HPLC). DPP-IV inhibitory peptides were purified from the enzymatic hydrolysate and their amino acid sequences were identified by liquid chromatography-tandem mass spectrometry. Results: Both neutral protease and alkaline protease could effectively hydrolyze pearl mussel muscle. After concentration using a 3 kDa cut-off ultrafiltration membrane, the DPP-IV inhibition rate of the enzymatic hydrolysate reached 67.4%. After separation by gel filtration column and purification by RP-HPLC, 6 active peptides were obtained, whose sequences were FNAPAM, FIPNY, IYNPPTPF, LAMPYP, FFVVMP and LAGMP, respectively. Furthermore, the interactions between these peptides and DPP-IV were analyzed by molecular docking. Conclusion: Our present study provides a theoretical reference for the effective utilization of fish processing byproducts as raw materials for functional food production. |
| format | Article |
| id | doaj-art-a0988e1dd0574e3db7a749c3b807d3e8 |
| institution | OA Journals |
| issn | 1002-6630 |
| language | English |
| publishDate | 2024-09-01 |
| publisher | China Food Publishing Company |
| record_format | Article |
| series | Shipin Kexue |
| spelling | doaj-art-a0988e1dd0574e3db7a749c3b807d3e82025-08-20T02:17:52ZengChina Food Publishing CompanyShipin Kexue1002-66302024-09-014517637010.7506/spkx1002-6630-20240125-233Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel MuscleZHANG Chuhan, CHEN Yinge, MA Ting, WENG Ling, ZHANG Lingjing, ZHANG Genfang, CAO Minjie0(1. Physical Education Institute of Jimei University, Xiamen 361021, China; 2. College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; 3. Agriculture College, Jinhua University of Vocational Technology, Jinhua 321000, China)Objective: Bioactive peptides with an inhibitory effect on dipeptidyl peptidase-IV (DPP-IV) were prepared from pearl mussel muscle. Methods: Two-step enzymatic hydrolysis was adopted and enzymatic hydrolysis conditions were optimized. Fractions with in vitro DPP-IV inhibitory activity were concentrated by ultrafiltration, and purified by SuperdexTM peptide 10/300 GL gel filtration column chromatography and reverse phase-high performance liquid chromatography (RP-HPLC). DPP-IV inhibitory peptides were purified from the enzymatic hydrolysate and their amino acid sequences were identified by liquid chromatography-tandem mass spectrometry. Results: Both neutral protease and alkaline protease could effectively hydrolyze pearl mussel muscle. After concentration using a 3 kDa cut-off ultrafiltration membrane, the DPP-IV inhibition rate of the enzymatic hydrolysate reached 67.4%. After separation by gel filtration column and purification by RP-HPLC, 6 active peptides were obtained, whose sequences were FNAPAM, FIPNY, IYNPPTPF, LAMPYP, FFVVMP and LAGMP, respectively. Furthermore, the interactions between these peptides and DPP-IV were analyzed by molecular docking. Conclusion: Our present study provides a theoretical reference for the effective utilization of fish processing byproducts as raw materials for functional food production.https://www.spkx.net.cn/fileup/1002-6630/PDF/2024-45-17-008.pdfpearl mussel; enzymatic hydrolysis; separation and purification; dipeptidyl peptidase-iv; inhibitory peptides |
| spellingShingle | ZHANG Chuhan, CHEN Yinge, MA Ting, WENG Ling, ZHANG Lingjing, ZHANG Genfang, CAO Minjie Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle Shipin Kexue pearl mussel; enzymatic hydrolysis; separation and purification; dipeptidyl peptidase-iv; inhibitory peptides |
| title | Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle |
| title_full | Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle |
| title_fullStr | Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle |
| title_full_unstemmed | Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle |
| title_short | Preparation and Purification of Dipeptidyl Peptidase-IV Inhibitory Peptides from Pearl Mussel Muscle |
| title_sort | preparation and purification of dipeptidyl peptidase iv inhibitory peptides from pearl mussel muscle |
| topic | pearl mussel; enzymatic hydrolysis; separation and purification; dipeptidyl peptidase-iv; inhibitory peptides |
| url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2024-45-17-008.pdf |
| work_keys_str_mv | AT zhangchuhanchenyingematingwenglingzhanglingjingzhanggenfangcaominjie preparationandpurificationofdipeptidylpeptidaseivinhibitorypeptidesfrompearlmusselmuscle |