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dc.contributor.authorCai, He
dc.contributor.authorGrunwald, Eric W.
dc.contributor.authorPark, Sung Yong
dc.contributor.authorLei, Benfang
dc.contributor.authorRichards, Mark P.
dc.date.accessioned2016-06-23T15:17:34Z
dc.date.available2016-06-23T15:17:34Z
dc.date.issued2013-05
dc.identifier.citationCai H, Grunwald EW, Park SY, Lei B, Richards MP. 2013. Lipid Oxidation in Trout Muscle Is Strongly Inhibited by a Protein That Specifically Binds Hemin Released from Hemoglobin. Journal of Agricultural and Food Chemistry. 61:4180-4187en_US
dc.identifier.issn0021-8561
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9904
dc.description.abstractThe recombinant streptococcal protein apoShp can be used as a probe for hemoglobin (Hb) reactivity in fish muscle due to its specific affinity for hemin that is released from Hb at post-mortem pH values. Hemin affinity measurements indicated that apoShp binds hemin released from Hb but not myoglobin (Mb). Hemin affinity of holoShp was higher at pH 5.7 compared to pH 8.0. This may be attributed to enhanced electrostatic interaction of His58 with the heme-7-propionate at lower pH. ApoShp readily acquired hemin that was released from trout IV metHb in the presence of washed cod muscle during 2 °C storage at pH 6.3. This was based on increases in redness in the washed cod matrix, which occurs when apoShp binds hemin that is released from metHb. ApoShp prevented Hb-mediated lipid oxidation in washed cod muscle during 2 °C storage. The prevention of Hb-mediated lipid oxidation by apoShp was likely due to bis-methionyl coordination of hemin that dissociated from metHb. This hexacoordination of hemin appears to prevent peroxide-mediated redox reactions, and there is no component in the matrix capable of dissociating hemin from Shp. ApoShp was also added to minced muscle from rainbow trout (Oncorhynchus mykiss) to examine the degree to which Hb contributes to lipid oxidation in trout muscle. Addition of apoShp inhibited approximately 90% of the lipid oxidation that occurred in minced trout muscle during 9 days of 2 °C storage on the basis of lipid peroxide, hexanal, and thiobarituric acid reactive substances (TBARS) values. These results strongly suggest that Hb is the primary promoter of lipid oxidation in trout muscle.en_US
dc.titleLipid Oxidation in Trout Muscle Is Strongly Inhibited by a Protein That Specifically Binds Hemin Released from Hemoglobinen_US
dc.typeArticleen_US
mus.citation.extentfirstpage4180en_US
mus.citation.extentlastpage8187en_US
mus.citation.issue17en_US
mus.citation.journaltitleJournal of Agricultural and Food Chemistryen_US
mus.citation.volume61en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1021/jf4006142en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US


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