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The Bright Side of Gelatinous Blooms: Nutraceutical Value and Antioxidant Properties of Three Mediterranean Jellyfish (Scyphozoa).

Leone A, Lecci RM, Durante M, Meli F, Piraino S - Mar Drugs (2015)

Bottom Line: The content and composition of proteins, amino acids, phenolics, and fatty acids of the three species were recorded and compared.Protein content (mainly represented by collagen) up to 40% of jellyfish dry weight were found in two of the three jellyfish species (C. tuberculata and R. pulmo), whereas the presence of ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) was significantly higher in the zooxanthellate jellyfish C. tuberculata only.The abundance of collagen, peptides and other bioactive molecules make these Mediterranean gelatinous biomasses a largely untapped source of natural compounds of nutraceutical, cosmeceutical and pharmacological interest.

View Article: PubMed Central - PubMed

Affiliation: Institute of Sciences of Food Production, National Research Council, Unit of Lecce (CNR, ISPA), Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. antonella.leone@ispa.cnr.it.

ABSTRACT
Jellyfish are recorded with increasing frequency and magnitude in many coastal areas and several species display biological features comparable to the most popular Asiatic edible jellyfish. The biochemical and antioxidant properties of wild gelatinous biomasses, in terms of nutritional and nutraceutical values, are still largely unexplored. In this paper, three of the most abundant and commonly recorded jellyfish species (Aurelia sp.1, Cotylorhiza tuberculata and Rhizostoma pulmo) in the Mediterranean Sea were subject to investigation. A sequential enzymatic hydrolysis of jellyfish proteins was set up by pepsin and collagenase treatments of jellyfish samples after aqueous or hydroalcoholic protein extraction. The content and composition of proteins, amino acids, phenolics, and fatty acids of the three species were recorded and compared. Protein content (mainly represented by collagen) up to 40% of jellyfish dry weight were found in two of the three jellyfish species (C. tuberculata and R. pulmo), whereas the presence of ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) was significantly higher in the zooxanthellate jellyfish C. tuberculata only. Remarkable antioxidant ability was also recorded from both proteinaceous and non proteinaceous extracts and the hydrolyzed protein fractions in all the three species. The abundance of collagen, peptides and other bioactive molecules make these Mediterranean gelatinous biomasses a largely untapped source of natural compounds of nutraceutical, cosmeceutical and pharmacological interest.

No MeSH data available.


Polypeptide patterns of pepsin hyrolysates (a) or collagenase hyrolysates (b) separated by 12% reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight size marker (range of 250–15kDa), was run in parallel with samples for molecular weight estimation. Each line contained 30 μg of proteins and bands were visualized by staining gels with Coomassie Brillian Blue R-250 dye.
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marinedrugs-13-04654-f004: Polypeptide patterns of pepsin hyrolysates (a) or collagenase hyrolysates (b) separated by 12% reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight size marker (range of 250–15kDa), was run in parallel with samples for molecular weight estimation. Each line contained 30 μg of proteins and bands were visualized by staining gels with Coomassie Brillian Blue R-250 dye.

Mentions: The SDS-PAGE electrophoretic separation of jellyfish proteins was carried out after hydrolysis with pepsin (a) and collagenase (b) on samples subjected to different solvent extractions in PBS (A), in 80% ethanol (B) or methanol (C) or on non-pre-extracted (NT) samples (Figure 4). Patterns of soluble polypeptides with a size higher than 15 kDa were compared. Polypeptide patterns derived from pepsin digestion slightly differed among jellyfish species and extraction methods (Figure 4a), with pepsin-hydrolysed peptides ranging around 30–40 kDa, 70–100 kDa and 150kDa. The patterns of soluble peptides after pepsin digestion were more complex in C. tuberculata and R. pulmo samples than in Aurelia, confirming the composite nature of rhizostomae species [8]. A large band of polypeptides with molecular weight around 40 kDa were common to all pepsin-hydrolysate jellyfish samples. For each jellyfish species, comparison among peptide patterns from pre-extracted and non-treated samples did not reveal major differences, indicating that the preliminary aqueous or hydroalcoholic extractions have no effect on the bulk of jellyfish proteins. The polypeptide patterns derived from collagen of chicken cartilage (C), hydrolysed by pepsin (PHC) and by pepsin followed by collagenase (PCHC), appear quite different from jellyfish samples, showing a different composition of pepsin digestible collagen in vertebrate as compared to jellyfish specimens (Figure 4a).


The Bright Side of Gelatinous Blooms: Nutraceutical Value and Antioxidant Properties of Three Mediterranean Jellyfish (Scyphozoa).

Leone A, Lecci RM, Durante M, Meli F, Piraino S - Mar Drugs (2015)

Polypeptide patterns of pepsin hyrolysates (a) or collagenase hyrolysates (b) separated by 12% reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight size marker (range of 250–15kDa), was run in parallel with samples for molecular weight estimation. Each line contained 30 μg of proteins and bands were visualized by staining gels with Coomassie Brillian Blue R-250 dye.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4556998&req=5

marinedrugs-13-04654-f004: Polypeptide patterns of pepsin hyrolysates (a) or collagenase hyrolysates (b) separated by 12% reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight size marker (range of 250–15kDa), was run in parallel with samples for molecular weight estimation. Each line contained 30 μg of proteins and bands were visualized by staining gels with Coomassie Brillian Blue R-250 dye.
Mentions: The SDS-PAGE electrophoretic separation of jellyfish proteins was carried out after hydrolysis with pepsin (a) and collagenase (b) on samples subjected to different solvent extractions in PBS (A), in 80% ethanol (B) or methanol (C) or on non-pre-extracted (NT) samples (Figure 4). Patterns of soluble polypeptides with a size higher than 15 kDa were compared. Polypeptide patterns derived from pepsin digestion slightly differed among jellyfish species and extraction methods (Figure 4a), with pepsin-hydrolysed peptides ranging around 30–40 kDa, 70–100 kDa and 150kDa. The patterns of soluble peptides after pepsin digestion were more complex in C. tuberculata and R. pulmo samples than in Aurelia, confirming the composite nature of rhizostomae species [8]. A large band of polypeptides with molecular weight around 40 kDa were common to all pepsin-hydrolysate jellyfish samples. For each jellyfish species, comparison among peptide patterns from pre-extracted and non-treated samples did not reveal major differences, indicating that the preliminary aqueous or hydroalcoholic extractions have no effect on the bulk of jellyfish proteins. The polypeptide patterns derived from collagen of chicken cartilage (C), hydrolysed by pepsin (PHC) and by pepsin followed by collagenase (PCHC), appear quite different from jellyfish samples, showing a different composition of pepsin digestible collagen in vertebrate as compared to jellyfish specimens (Figure 4a).

Bottom Line: The content and composition of proteins, amino acids, phenolics, and fatty acids of the three species were recorded and compared.Protein content (mainly represented by collagen) up to 40% of jellyfish dry weight were found in two of the three jellyfish species (C. tuberculata and R. pulmo), whereas the presence of ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) was significantly higher in the zooxanthellate jellyfish C. tuberculata only.The abundance of collagen, peptides and other bioactive molecules make these Mediterranean gelatinous biomasses a largely untapped source of natural compounds of nutraceutical, cosmeceutical and pharmacological interest.

View Article: PubMed Central - PubMed

Affiliation: Institute of Sciences of Food Production, National Research Council, Unit of Lecce (CNR, ISPA), Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. antonella.leone@ispa.cnr.it.

ABSTRACT
Jellyfish are recorded with increasing frequency and magnitude in many coastal areas and several species display biological features comparable to the most popular Asiatic edible jellyfish. The biochemical and antioxidant properties of wild gelatinous biomasses, in terms of nutritional and nutraceutical values, are still largely unexplored. In this paper, three of the most abundant and commonly recorded jellyfish species (Aurelia sp.1, Cotylorhiza tuberculata and Rhizostoma pulmo) in the Mediterranean Sea were subject to investigation. A sequential enzymatic hydrolysis of jellyfish proteins was set up by pepsin and collagenase treatments of jellyfish samples after aqueous or hydroalcoholic protein extraction. The content and composition of proteins, amino acids, phenolics, and fatty acids of the three species were recorded and compared. Protein content (mainly represented by collagen) up to 40% of jellyfish dry weight were found in two of the three jellyfish species (C. tuberculata and R. pulmo), whereas the presence of ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) was significantly higher in the zooxanthellate jellyfish C. tuberculata only. Remarkable antioxidant ability was also recorded from both proteinaceous and non proteinaceous extracts and the hydrolyzed protein fractions in all the three species. The abundance of collagen, peptides and other bioactive molecules make these Mediterranean gelatinous biomasses a largely untapped source of natural compounds of nutraceutical, cosmeceutical and pharmacological interest.

No MeSH data available.