scholarly journals Cosmetic Potential of Marine Fish Skin Collagen

Cosmetics ◽  
2017 ◽  
Vol 4 (4) ◽  
pp. 39 ◽  
Author(s):  
Ana Alves ◽  
Ana Marques ◽  
Eva Martins ◽  
Tiago Silva ◽  
Rui Reis
Keyword(s):  
Marine Fish ◽  
Fish Skin ◽  
Skin Collagen ◽  
Fish Skin Collagen

scholarly journals Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes

Nutrients ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 2657
Author(s):  
Maryam Atef ◽  
Yasmina Ait Chait ◽  
Seyed Mahdi Ojagh ◽  
Ali Mohammad Latifi ◽  
Mina Esmaeili ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Degree Of Hydrolysis ◽  
Fish Skin ◽  
Small Peptides ◽  
Skin Collagen ◽  
Dependent Inhibition ◽  
Acetone Fractionation ◽  
Chain Lengths ◽  
Peptide Fractions ◽  
Fish Skin Collagen

This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight < 10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.

Biochemical and structural characterization of sturgeon fish skin collagen ( Huso huso )

2020 ◽  
Vol 44 (8) ◽  
Author(s):  
Maryam Atef ◽  
Seyed Mahdi Ojagh ◽  
Ali Mohammad Latifi ◽  
Mina Esmaeili ◽  
Chibuike C. Udenigwe
Keyword(s):  
Structural Characterization ◽  
Huso Huso ◽  
Fish Skin ◽  
Skin Collagen ◽  
Sturgeon Fish ◽  
Fish Skin Collagen

scholarly journals Collagen Based Materials in Cosmetic Applications: A Review

Materials ◽  
2020 ◽  
Vol 13 (19) ◽  
pp. 4217 ◽  
Author(s):  
Alina Sionkowska ◽  
Katarzyna Adamiak ◽  
Katarzyna Musiał ◽  
Magdalena Gadomska
Keyword(s):  
Review Paper ◽  
Structural Protein ◽  
Fish Skin ◽  
Academic Interest ◽  
Structural Support ◽  
Recent Advances ◽  
Cosmetic Industry ◽  
Skin Collagen ◽  
Fish Skin Collagen

This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish skin. Collagen has attracted significant academic interest as well as the attention of the cosmetic industry due to its interesting properties that include being a natural humectant and moisturizer for the skin. This review paper covers the biosynthesis of collagen, the sources of collagen used in the cosmetic industry, and the role played by this protein in cosmetics. Future aspects regarding applications of collagen-based materials in cosmetics have also been mentioned.

Studies on calcification efficacy of stingray fish skin collagen for possible use as scaffold for bone regeneration

2014 ◽  
Vol 12 (2) ◽  
pp. 98-106 ◽  
Author(s):  
Swarnakumari Balakrishnan ◽  
Rajamani Selvam ◽  
Kavitha Sundar ◽  
Shanthi Chittibabu ◽  
Usha Ramamoorthy ◽  
...  
Keyword(s):  
Bone Regeneration ◽  
Fish Skin ◽  
Skin Collagen ◽  
Fish Skin Collagen

Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states

Biomaterials ◽  
2000 ◽  
Vol 21 (9) ◽  
pp. 899-906 ◽  
Author(s):  
Marie-Madeleine Giraud-Guille ◽  
Laurence Besseau ◽  
Christine Chopin ◽  
Patrick Durand ◽  
Daniel Herbage
Keyword(s):  
Liquid Crystalline ◽  
Fish Skin ◽  
Ordered Arrays ◽  
Skin Collagen ◽  
Structural Aspects ◽  
Fish Skin Collagen

scholarly journals Effects of Temperature on the FT NIR Raman Spectra of Fish Skin Collagen

2021 ◽  
Vol 11 (18) ◽  
pp. 8358
Author(s):  
Maria Połomska ◽  
Leszek Kubisz ◽  
Jacek Wolak ◽  
Dorota Hojan-Jezierska
Keyword(s):  
Molecular Structure ◽  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Raman Spectra ◽  
Molecular Organization ◽  
Fish Skin ◽  
Temperature Range ◽  
Skin Collagen ◽  
Α Helix ◽  
Fish Skin Collagen

The development of regenerative medicine turns attention toward native collagen as a biocompatible material. Particularly interesting is fish skin collagen, which is relatively easy to extract comparing mammalian tissues and free of some pathogens that are dangerous to humans. The paper presents results of IR Raman spectroscopy studies of silver carp (Hypophthalmichthys molitrix) skin collagen. As collagen properties result from its structure and conformation, both sensitive to temperature, FT NIR Raman spectroscopy is an excellent tool to characterize the molecular structure of fish skin collagen, particularly in temperature range typical for the manufacturing processes of biomedical products. Therefore, the Raman spectra were recorded in a temperature range of 300 to 403 K. The analysis of Raman spectra of prepared collagen films, particularly in the range of the bands related to amide I and amide III entities, showed a high content of α-helix and α-helix type molecular organization in fish skin collagen. Additionally, the secondary structure of the studied fish skin collagen is stable up to ~358 K. Heating to 403 K leads to irreversible changes in the molecular structure of fish skin collagen. It was found that the Raman spectrum of fish skin collagen preheated in this manner becomes similar to the spectrum of the collagen obtained from bovine Achilles tendon, whose secondary structure does not change up to 403 K.

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