Astaxanthin binding protein in Atlantic salmon

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DOIResolve DOI: http://doi.org/10.1016/j.cbpb.2006.02.007
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TypeArticle
Journal titleComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
Volume21
Issue2
Pages215219; # of pages: 5
SubjectAlpha actinin; astaxanthin; carotenoid; pigment; salmon coloration
AbstractThe rubicund pigmentation in salmon and trout flesh is unique and is due to the deposition of dietary carotenoids, astaxanthin and canthaxanthin in the muscle. The present study was undertaken to determine which protein was responsible for pigment binding. Salmon muscle proteins were solubilized by sequential extractions with non-denaturing, low ionic strength aqueous solutions and segregated as such into six different fractions. Approximately 91% of the salmon myofibrillar proteins were solubilized under non-denaturing conditions using a protocol modified from a method described by Krishnamurthy et al. [Krishnamurthy, G., Chang, H.S., Hultin, H.O., Feng, Y., Srinivasan, S., Kelleher. S.D., 1996. Solubility of chicken breast muscle proteins in solutions of low ionic strength. J. Agric. Food Chem. 44: 408–415.] for the dissolution of avian muscle. To our knowledge, this is the first time this solubilization approach has been applied to the study of molecular interactions in myofibrillar proteins. Astaxanthin binding in each fraction was determined using an in vitro binding assay. In addition, SDS-PAGE and quantitative densitometry were used to separate and determine the relative amounts of each of the proteins in the six fractions. The results showed that ?-actinin was the only myofibrillar protein correlating significantly (P < 0.05) with astaxanthin binding. Alpha-actinin was positively identified using electrophoretic techniques and confirmed by tandem mass spectroscopy. Purified salmon ?-actinin bound synthetic astaxanthin in a molar ratio of 1.11:1.00. The study was repeated using halibut ?-actinin, which was found to have a molar binding ratio of astaxanthin to ?-actinin of 0.893:1. These results suggest that the difference in pigmentation between white fish and Atlantic salmon is not due to binding capacity in the muscle, but rather differences in the metabolism or transport of pigment.
Publication date
PublisherElsevier
LanguageEnglish
AffiliationNRC Institute for Marine Biosciences; National Research Council Canada; Industrial Research Assistance Program; Aquatic and Crop Resource Development
Peer reviewedYes
NRC number55558
1568
NPARC number3538234
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Record identifier41ee314a-921a-4ff4-b104-03fb9d77eb14
Record created2009-03-01
Record modified2016-05-09
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