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Non–animal collagens as new options for cosmetic formulation
Author(s) -
Peng Y. Y.,
Stoichevska V.,
Vashi A.,
Howell L.,
Fehr F.,
Dumsday G. J.,
Werkmeister J. A.,
Ramshaw J. A. M.
Publication year - 2015
Publication title -
international journal of cosmetic science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.532
H-Index - 62
eISSN - 1468-2494
pISSN - 0142-5463
DOI - 10.1111/ics.12243
Subject(s) - circular dichroism , chemistry , chromatography , ionic strength , recombinant dna , gel electrophoresis , proteolytic enzymes , western blot , biochemistry , enzyme , organic chemistry , aqueous solution , gene
Synopsis Objective To examine the potential of non‐animal collagens as a new option for cosmetic applications. Methods Non‐animal collagens from three species, S treptococcus pyogenes , S olibacter usitatus and M ethylobacterium sp 4‐46, have been expressed as recombinant proteins in E scherichia coli using a cold‐shock, p C old, expression system. The proteins were purified using either metal affinity chromatography or a simple process based on precipitation and proteolytic digestion of impurities, which is suitable for large‐scale production. Samples were examined using a range of analytical procedures. Results Analyses by gel electrophoresis and mass spectrometry were used to examine the purity and integrity of the products. Circular dichroism spectroscopy showed stabilities around 38°C, and calculated p I values were from 5.4 to 8.6. UV ‐visible light spectroscopy showed the clarity of collagen solutions. The collagens were soluble at low ionic strength between p H 5 and p H 8, but were less soluble under more acidic conditions. At lower p H , the insoluble material was well dispersed and did not form the fibrous associations and aggregates found with animal collagens. The materials were shown to be non‐cytotoxic to cells in culture. Conclusions These novel, non‐animal collagens may be potential alternatives to animal collagens for inclusion in cosmetic formulations.