Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates
Nature-derived anti-allergic peptides are considered one of the promising therapeutic approaches in alleviating food allergy. The present focus aims to open up a new high-value and full-use way for processing industrial fish wastes while expecting to obtain anti-allergic peptides. In this research,...
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ftdoajarticles:oai:doaj.org/article:044fa3ab33794ec5b399fa53a86191d0 2023-05-15T15:30:29+02:00 Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates Kexin Wang Pramod Narayana Siddanakoppalu Ishfaq Ahmed Tushar Ramesh Pavase Hong Lin Zhenxing Li 2020-09-01T00:00:00Z https://doi.org/10.1016/j.jff.2020.104084 https://doaj.org/article/044fa3ab33794ec5b399fa53a86191d0 EN eng Elsevier http://www.sciencedirect.com/science/article/pii/S175646462030308X https://doaj.org/toc/1756-4646 1756-4646 doi:10.1016/j.jff.2020.104084 https://doaj.org/article/044fa3ab33794ec5b399fa53a86191d0 Journal of Functional Foods, Vol 72, Iss , Pp 104084- (2020) Salmon processing byproduct Enzymatic hydrolysates Bioactive peptides Anti-allergic activity High-value-use Nutrition. Foods and food supply TX341-641 article 2020 ftdoajarticles https://doi.org/10.1016/j.jff.2020.104084 2022-12-31T15:34:08Z Nature-derived anti-allergic peptides are considered one of the promising therapeutic approaches in alleviating food allergy. The present focus aims to open up a new high-value and full-use way for processing industrial fish wastes while expecting to obtain anti-allergic peptides. In this research, the anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct hydrolysate by pepsin hydrolysis, was purified and identified using consecutive chromatographic techniques such as Sephadex G-15 gel permeation chromatography, high performance liquid chromatography and LC/MS/MS. Among the fractions (C1-C6) obtained from RP-HPLC, C6 exerted the strongest anti-allergic activity (89.40%) significantly at 1 mg/mL (P<0.05). Afterwards, the novel peptide with eleven amino acids identified as TPEVHIAVDKF was proved to exert anti-allergic activity after synthesis by inhibiting the release of β-hexosaminidase in IgE-mediated RBL-2H3 cell degranulation at IC50 value: 1.39 mg/mL. Thus, Atlantic salmon byproduct can be a potential source of novel ingredients in food and pharmaceuticals for food allergy management. Article in Journal/Newspaper Atlantic salmon Salmo salar Directory of Open Access Journals: DOAJ Articles Journal of Functional Foods 72 104084 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Salmon processing byproduct Enzymatic hydrolysates Bioactive peptides Anti-allergic activity High-value-use Nutrition. Foods and food supply TX341-641 |
spellingShingle |
Salmon processing byproduct Enzymatic hydrolysates Bioactive peptides Anti-allergic activity High-value-use Nutrition. Foods and food supply TX341-641 Kexin Wang Pramod Narayana Siddanakoppalu Ishfaq Ahmed Tushar Ramesh Pavase Hong Lin Zhenxing Li Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
topic_facet |
Salmon processing byproduct Enzymatic hydrolysates Bioactive peptides Anti-allergic activity High-value-use Nutrition. Foods and food supply TX341-641 |
description |
Nature-derived anti-allergic peptides are considered one of the promising therapeutic approaches in alleviating food allergy. The present focus aims to open up a new high-value and full-use way for processing industrial fish wastes while expecting to obtain anti-allergic peptides. In this research, the anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct hydrolysate by pepsin hydrolysis, was purified and identified using consecutive chromatographic techniques such as Sephadex G-15 gel permeation chromatography, high performance liquid chromatography and LC/MS/MS. Among the fractions (C1-C6) obtained from RP-HPLC, C6 exerted the strongest anti-allergic activity (89.40%) significantly at 1 mg/mL (P<0.05). Afterwards, the novel peptide with eleven amino acids identified as TPEVHIAVDKF was proved to exert anti-allergic activity after synthesis by inhibiting the release of β-hexosaminidase in IgE-mediated RBL-2H3 cell degranulation at IC50 value: 1.39 mg/mL. Thus, Atlantic salmon byproduct can be a potential source of novel ingredients in food and pharmaceuticals for food allergy management. |
format |
Article in Journal/Newspaper |
author |
Kexin Wang Pramod Narayana Siddanakoppalu Ishfaq Ahmed Tushar Ramesh Pavase Hong Lin Zhenxing Li |
author_facet |
Kexin Wang Pramod Narayana Siddanakoppalu Ishfaq Ahmed Tushar Ramesh Pavase Hong Lin Zhenxing Li |
author_sort |
Kexin Wang |
title |
Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
title_short |
Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
title_full |
Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
title_fullStr |
Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
title_full_unstemmed |
Purification and identification of anti-allergic peptide from Atlantic Salmon (Salmo salar) byproduct enzymatic hydrolysates |
title_sort |
purification and identification of anti-allergic peptide from atlantic salmon (salmo salar) byproduct enzymatic hydrolysates |
publisher |
Elsevier |
publishDate |
2020 |
url |
https://doi.org/10.1016/j.jff.2020.104084 https://doaj.org/article/044fa3ab33794ec5b399fa53a86191d0 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_source |
Journal of Functional Foods, Vol 72, Iss , Pp 104084- (2020) |
op_relation |
http://www.sciencedirect.com/science/article/pii/S175646462030308X https://doaj.org/toc/1756-4646 1756-4646 doi:10.1016/j.jff.2020.104084 https://doaj.org/article/044fa3ab33794ec5b399fa53a86191d0 |
op_doi |
https://doi.org/10.1016/j.jff.2020.104084 |
container_title |
Journal of Functional Foods |
container_volume |
72 |
container_start_page |
104084 |
_version_ |
1766360926952357888 |