14 Jul 2016

Protein analysis with Specac equipment

Carbon dating bone

Collagens are the most abundant protein in mammals. Historic England (formerly known as English Heritage) used our Golden Gate ATR accessory for the prescreening of collagen content in a bone they were radiocarbon-dating.

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In collaboration with the University of Oxford, Historic England analyzed bone samples from archaeological sites. Nitrogen was detected and used as an indicator of collagen content. Read more here.

Proteins in single silk fibres

Our Golden Gate ATR spectrometer accessory was also used to analyze the orientation and conformation of a single silk fibroin filament of the silkworm Bombyx mori that is about 10 μm in diameter.

Read more here.

Fish skin collagens

For a variety of industrial purposes bovine collagens and porcine are extracted from the animal waste materials.

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The collagens, found in the animal gelatin, are highly beneficial for cell healing and proliferation, for medical procedures such as transplants.

Europe consumption of gelatin alone increases by 2-3% annually and exceeds ahead of production. Due to the high collagen demand, fish waste, otherwise known as hard wastes, can be used as a gelatin substitue. 

The heads and backbones of fish have similar collagen levels to bovine and porcine waste, between 14-25%. Fish collagen is actually less cross-linked than bovine/porcine collagen and so in its native form, it is much more soluble. 

For the experiment linked to here, the African Catfish, Baltic Cod and Salmon were analyzed. Our Golden Gate ATR was used to find the FTIR spectra of dry collagen preparation.

Check out #SpectroscopySolutions for more.