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Enzymatic hydrolysis of collagen by pancreatin and thrombin as a step in the formation of scaffolds

High-molecular collagen was isolated from cod skin and subjected to enzymatic hydrolysis with pancreatin and thrombin. The resulting products were characterized by molecular weight parameters. It is shown that formation of two oligomeric fractions with molecular masses of 9 kDa (>80%) and 17–18 k...

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Bibliographic Details
Published in:Russian chemical bulletin 2020, Vol.69 (1), p.164-168
Main Authors: Semenycheva, L. L., Egorikhina, M. N., Chasova, V. O., Valetova, N. B., Podguzkova, M. V., Astanina, M. V., Kuznetsova, Yu. L.
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Language:English
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Summary:High-molecular collagen was isolated from cod skin and subjected to enzymatic hydrolysis with pancreatin and thrombin. The resulting products were characterized by molecular weight parameters. It is shown that formation of two oligomeric fractions with molecular masses of 9 kDa (>80%) and 17–18 kDa (2–4%) is characteristic of both the pancreatin and thrombin hydrolysis of the peptide bonds in collagen.
ISSN:1066-5285
1573-9171
DOI:10.1007/s11172-020-2738-2