Collagen Peptides from Hyaline Cartilage for the Treatment and Prevention of Joint Diseases: Isolation and Characteristics


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Resumo

We studied the effects of Chymopsin and Caripazim on the proteolysis of collagen proteins from cattle tracheal hyaline cartilage. Homogenization of the cartilage under conditions of high pressure and temperature facilitated subsequent enzymatic hydrolysis: the degree of hydrolysis increased upon elevation of pressure from 40 to 80 mPa and temperature from 60 to 70°C. Proteolysis with Chymopsin yielded collagen peptides with molecular weights from 900 to 7000 Da, while Caripazim processing yielded collagen peptides with lower molecular weights from 250 to 780 Da consisting of 2-8 amino acids, which could be easily absorbed and intensely incorporated in the formation of the joint tissue structures.

Sobre autores

T. Nikolaeva

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Autor responsável pela correspondência
Email: tomivnik@yandex.ru
Rússia, Moscow

K. Laurinavicius

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences

Email: tomivnik@yandex.ru
Rússia, Moscow

V. Kaptsov

Institute of Cell Biophysics, Russian Academy of Sciences

Email: tomivnik@yandex.ru
Rússia, Moscow Region, Pushchino

R. Chernyi

P. N. Lebedev Physical Institute

Email: tomivnik@yandex.ru
Rússia, Moscow

P. Shekhovtsov

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Email: tomivnik@yandex.ru
Rússia, Moscow


Declaração de direitos autorais © Springer Science+Business Media, LLC, part of Springer Nature, 2019

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