Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, <i>Homarus gammarus</i> a study by <sup>13</sup>C magic angle spinning NMR

Weesie, R. J.; Askin, David; Jansen, F. J. H. M.; Groot, Huub J. M. de; Lugtenburg, J.; Britton, George

doi:10.1016/0014-5793(95)00191-b

Cited by 37 publications

(50 citation statements)

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“…de Sá and Rodriguez-Amaya (2003) Bernhardt and Schlich (2006) Soybean sprout a-Catonete 0.0007 Kim et al (2007) b-Carotene 0.0088 Kim et al (2007) b-Cryptoxanthin nd Kim et al (2007) Lutein 0.0898 Kim et al (2007) Phytochem Rev (2008) 7:345-384 349 which is bound in a stoichiometric but non-covalent way to the apoprotein (Weesie et al 1995). According to Hart and Scott (1995) boiled green vegetables showed an increase of 31% of total carotenoids.…”

Section: Cooking Methodologiesmentioning

confidence: 94%

Effect of domestic processing on bioactive compounds

et al. 2007

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Section: Cooking Methodologiesmentioning

confidence: 94%

Effect of domestic processing on bioactive compounds

et al. 2007

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“…It is possible that the C-3 and C-3Ј hydroxy groups of lutein are involved in holding the carotenoid in the binding cavity of the protein and that other charged groups in the protein interact with the polyene system and affect the electronic configuration, resulting in a lower energy complex with a higher spectral shift. In ␣-crustacyanin, Weesie et al (22) have shown that a charge redistribution mechanism is the only cause for the bathochromic shift observed for astaxanthin. Britton et al (1) have reported that the presence of an oxo group in the carotenoid is important for binding to the protein and for production of a spectral shift through enolization, Schiff base formation, or hydrogen bonding to the amino acids of the protein.…”

Section: Spectral Characterization Of the Lutein-binding Protein And mentioning

confidence: 99%

Purification and Partial Characterization of a Lutein-binding Protein from the Midgut of the Silkworm

Jouni

Wells

1996

Journal of Biological Chemistry

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A lutein-binding protein was purified from fifth instar larval midgut of Bombyx mori by a combination of ammonium sulfate fractionation and three chromatographic procedures, gel filtration, chromatofocusing, and anion exchange chromatography. The protein has a pI of 5.4 and an apparent molecular mass of 35,000 Da, as determined by a linear gradient SDS-polyacrylamide gel electrophoresis. The lutein-protein complex is watersoluble and more stable than the carotenoid or protein alone. The carotenoid moiety was identified by thin layer chromatography, light absorption spectroscopy, and high performance liquid chromatography as alltrans-lutein. Lutein is specifically and stoichiometrically bound to the protein, with a ratio of 3 mol of lutein per mol of protein. Binding of lutein (absorption maximum in hexane at 454 nm) to the apoprotein results in a marked red spectral shift of about 38 nm, giving rise to absorption maxima at 432, 462, and 492 nm in 20 mM Tris-HCl, pH 7.0. The lutein-protein complex is characterized by fine spectral structure indicating that lutein is in a relatively rigid environment. This protein is distributed in equal amounts throughout the midgut and in all developmental stages of the larval B. mori.Carotenoids cannot be synthesized by animals or insects and must be acquired from exogenous sources. In many insects, absorption of dietary carotenoids is selective with a preference for carotenes in Orthoptera and Phasmida, and for xanthophylls (oxygenated carotenes) in Lepidoptera, as in the case for the silkworm, Bombyx mori, the subject of this study (1, 2). Once absorbed, carotenoids are either irreversibly or reversibly modified. Irreversible modification includes (a) decomposition of the carbon skeleton into smaller units or (b) the addition of new functional groups, e.g. hydroxylation. Reversible modification includes (a) esterification of the hydroxy carotenoids with long chain fatty acids, as observed in fat body (3, 4), or (b) conjugation of the carotenoids with proteins forming carotenoid-protein complexes (carotenoproteins) which are water-soluble and more stable than the carotenoids alone (5-7). Such carotenoproteins occur mainly in invertebrates and plants (8).In B. mori, a major fate of the absorbed carotenoids is incorporation into the cocoon, which imparts various colors to the cocoon depending on the type of carotenoid. The mechanisms by which carotenoids are transported from the lumen of the midgut to the hemolymph lipoprotein, lipophorin, and from lipophorin into the silk gland, where the cocoon is produced, are unknown. Cocoons of the wild-type B. mori are yellow in color due to presence of lutein. There are three known mutants in B. mori that produce white cocoons, and genetic analysis has revealed that two mutations are in midgut-expressed proteins, whereas the third mutation is in a silk gland-specific protein (9). Currently, we are using these mutants as a model system to examine, at the molecular level, the pathways by which dietary carotenoids are absorbed and transporte...

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“…This colour change, caused by the formation or dissociation of the complex, is because of the bathochromic shift (a change in the wavelength absorbed by compounds) (Weesie et al. , 1995; Cianci et al.…”

Section: Resultsmentioning

confidence: 99%

Preference ranking of colour in raw and cooked shrimps

Parisenti

Beirão

Tramonte

et al. 2011

International Journal of Food Science &Amp; Technology

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The reddish colour to shrimp, which has been associated with its high quality, is one of the major factors for its acceptability by consumers. The aim of this work was to analyse consumer preference regarding colour in raw and cooked shrimps. Farmed shrimps Litopenaeus vannamei (13.8 + 1.16 g) were fed with control or supplemented food (60 ppm of carotenoids). The shrimp samples were analysed in naked eye, confirmed by colorimetry and sorted in the following categories: dark grey (L* 27.99; h 168.16), grey (L* 32.58; h 124.60), and light grey (L* 36.2; h 119.35) for raw shrimps; and intense orange (L* 61.49; h 54.69), orange (L* 65.97; h 57.79) and light orange (L* 72.65; h 70.17) for cooked shrimps. A preference ranking test was performed with 35 judges invited to rank the samples in descending order of preference. Consumers prefer lighter raw shrimp (light grey and grey) and brightly orange cooked shrimps (orange and intense orange), which indicates that supplementing shrimp food for pigmentation should be followed by improving its acceptance by consumer. These results indicate a challenge for the shrimp industry, as the lightest raw shrimps are also not so brightly orange coloured after cooking.

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Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by ¹³C magic angle spinning NMR

Cited by 37 publications

References 15 publications

Effect of domestic processing on bioactive compounds

Effect of domestic processing on bioactive compounds

Purification and Partial Characterization of a Lutein-binding Protein from the Midgut of the Silkworm

Preference ranking of colour in raw and cooked shrimps

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Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13C magic angle spinning NMR

Cited by 37 publications

References 15 publications

Effect of domestic processing on bioactive compounds

Effect of domestic processing on bioactive compounds

Purification and Partial Characterization of a Lutein-binding Protein from the Midgut of the Silkworm

Preference ranking of colour in raw and cooked shrimps

Contact Info

Product

Resources

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Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by ¹³C magic angle spinning NMR