Pectenovarin, A New Ovarian Carotenoprotein from Japanese Scallop Mizuhopecten yessoensis.

Satoko Matsunaga,Ryuichi Sakai,Hiroki Ikeda

doi:10.3390/molecules25133042

Satoko Matsunaga, Ryuichi Sakai + Show 1 more

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https://doi.org/10.3390/molecules25133042

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Abstract

The scallop Mizuhopecten yessoensis accumulates carotenoids in the ovary during the maturation stage. Its conspicuous pink color implies the presence of carotenoprotein. However, the carotenoprotein from the scallop ovary has never been isolated and characterized, probably due to its instability and complexity. Here, we developed an extraction and isolation procedure for the carotenoprotein by employing a basic buffer containing potassium bromide to facilitate its efficient extraction from the ovary, and we succeeded in obtaining the carotenoprotein, termed pectenovarin. The carotenoid composition of the pectenovarin was similar to that of the ovary. The N-terminal and internal amino acid sequences of pectenovarin showed a high similarity to those of vitellogenin, the precursor of egg yolk protein under analysis.

Highlights

Carotenoids are one of the essential classes of metabolites in a wide variety of living organisms.More than 750 different carotenoids have been reported to date [1]
We found that the association of carotenoid to the protein resulted in a bathochromic shift of more than 20 nm, leading the compound to be categorized as a “true carotenoprotein” [13]
We report the isolation and properties of pink carotenoprotein from the ovary of edible Japanese Scallop, Mizuhopecten yessoensis

Summary

Introduction

Carotenoids are one of the essential classes of metabolites in a wide variety of living organisms.More than 750 different carotenoids have been reported to date [1]. Carotenoids are one of the essential classes of metabolites in a wide variety of living organisms. It is known that carotenoids bind to proteins, termed carotenoproteins, to stabilize themselves against light or heat or to manipulate their physical properties, including solubility and color. Crustacyanin, one of the most representative carotenoproteins, binds to a red keto carotenoid, astaxanthin, but exhibits conspicuous blue color because of the bathochromic shift in the visible light region, due to the interaction between the carotenoids and the apoprotein. The structural evidence for specific binding between astaxanthin and the protein was observed by X-ray crystallography [2]. The blue color of crustacyanin is stable in an ambient milieu, this conspicuous color turns reddish-orange by heating or immersion in organic solvents. The molecular basis of the blue shift is an intriguing subject for biophysical research [2,3,4]

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