Pro-oxidative activity of trout and bovine hemoglobin during digestion using a static in vitro gastrointestinal model
Wu, Haizhou ; Tullberg, Cecilia LU
; Ghirmai, Semhar
and Undeland, Ingrid
(2022)
In Food Chemistry
393.
- Abstract
The degradation of trout and bovine hemoglobin (Hb) and their pro-oxidant activities in washed cod muscle mince (WCM) were studied using simple pH-shifts to simulate gastrointestinal (GI) conditions (pH 7 → 6 → 3 → 7), as well as full static in vitro GI digestion. Following gastric acidification to pH 6, metHb formation increased, especially for trout Hb. Subsequent acidification to pH 3 promoted Hb unfolding and partial or complete heme group-loss. During full GI digestion, polypeptide/peptide analyses revealed more extensive Hb-degradation in the gastric than duodenal phase, without any species-differences. When digesting WCM +/-Hb, both Hbs strongly promoted malondialdehyde (MDA), 4-hydroxy-2-hexenal (HHE), and 4-hydroxy-2-nonenal... (More)
The degradation of trout and bovine hemoglobin (Hb) and their pro-oxidant activities in washed cod muscle mince (WCM) were studied using simple pH-shifts to simulate gastrointestinal (GI) conditions (pH 7 → 6 → 3 → 7), as well as full static in vitro GI digestion. Following gastric acidification to pH 6, metHb formation increased, especially for trout Hb. Subsequent acidification to pH 3 promoted Hb unfolding and partial or complete heme group-loss. During full GI digestion, polypeptide/peptide analyses revealed more extensive Hb-degradation in the gastric than duodenal phase, without any species-differences. When digesting WCM +/-Hb, both Hbs strongly promoted malondialdehyde (MDA), 4-hydroxy-2-hexenal (HHE), and 4-hydroxy-2-nonenal (HNE) formation, peaking at the end of the gastric phase. Trout-Hb stimulated MDA and HHE more than bovine Hb in the first gastric phase. Altogether, partially degraded Hb, and/or free hemin -both mammal and fish-derived- stimulated oxidation of PUFA-rich lipids under GI-conditions, especially gastric ones.
(Less)
- author
- Wu, Haizhou
; Tullberg, Cecilia
LU
; Ghirmai, Semhar
and Undeland, Ingrid
- publishing date
- 2022-11-01
- type
- Contribution to journal
- publication status
- published
- keywords
- 4-hydroxy-2-hexenal, 4-hydroxy-2-nonenal, Aldehydes, Heme protein, Hemin release, Lipid oxidation, Malondialdehyde, Protein hydrolysis
- in
- Food Chemistry
- volume
- 393
- article number
- 133356
- pages
- 10 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:85131460987
- pmid:35688086
- ISSN
- 0308-8146
- DOI
- 10.1016/j.foodchem.2022.133356
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © 2022 The Author(s)
- id
- 5117e18d-c104-4a52-aca9-89263cd1ecc9
- date added to LUP
- 2024-09-06 11:24:54
- date last changed
- 2025-11-02 02:52:53
@article{5117e18d-c104-4a52-aca9-89263cd1ecc9,
abstract = {{<p>The degradation of trout and bovine hemoglobin (Hb) and their pro-oxidant activities in washed cod muscle mince (WCM) were studied using simple pH-shifts to simulate gastrointestinal (GI) conditions (pH 7 → 6 → 3 → 7), as well as full static in vitro GI digestion. Following gastric acidification to pH 6, metHb formation increased, especially for trout Hb. Subsequent acidification to pH 3 promoted Hb unfolding and partial or complete heme group-loss. During full GI digestion, polypeptide/peptide analyses revealed more extensive Hb-degradation in the gastric than duodenal phase, without any species-differences. When digesting WCM +/-Hb, both Hbs strongly promoted malondialdehyde (MDA), 4-hydroxy-2-hexenal (HHE), and 4-hydroxy-2-nonenal (HNE) formation, peaking at the end of the gastric phase. Trout-Hb stimulated MDA and HHE more than bovine Hb in the first gastric phase. Altogether, partially degraded Hb, and/or free hemin -both mammal and fish-derived- stimulated oxidation of PUFA-rich lipids under GI-conditions, especially gastric ones.</p>}},
author = {{Wu, Haizhou and Tullberg, Cecilia and Ghirmai, Semhar and Undeland, Ingrid}},
issn = {{0308-8146}},
keywords = {{4-hydroxy-2-hexenal; 4-hydroxy-2-nonenal; Aldehydes; Heme protein; Hemin release; Lipid oxidation; Malondialdehyde; Protein hydrolysis}},
language = {{eng}},
month = {{11}},
publisher = {{Elsevier}},
series = {{Food Chemistry}},
title = {{Pro-oxidative activity of trout and bovine hemoglobin during digestion using a static <i>in vitro</i> gastrointestinal model}},
url = {{http://dx.doi.org/10.1016/j.foodchem.2022.133356}},
doi = {{10.1016/j.foodchem.2022.133356}},
volume = {{393}},
year = {{2022}},
}