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International Journal of Biological Macromolecules

International Journal of Biological Macromolecules

IF: 7.7
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The role of extraction method to collagen substrates in enzymolysis of type I collagenase

Published:25 November 2024 DOI: 10.1016/j.ijbiomac.2024.138086 PMID: 39603305
Sijin Wu, Xuewei Zhou, Haiming Cheng

Abstract

Collagens are ubiquitous biomaterials in animal tissues whose characteristic triple-helical structure can only be hydrolyzed under physiological conditions by a few specific proteases. At present, information on the differences of collagenase hydrolysis behavior to collagen substrate caused by extraction methods is still lacking. Acid-relaxed extracted collagen (ARC) and acetic acid-pepsin extracted collagen (APC) were obtained from bovine hide by acetic acid and acetic acid-pepsin extraction method, respectively. The enzymolysis behavior of type I collagenase on ARC and APC were investigated by means of fluorescence spectra, UV spectra, and determination the release of hydrolysates into the supernatant. The results revealed that APC showed a lower molecular weight, a higher pI (5.59) and denaturation temperature (Td?=?66.9?°C) than that of ARC (pI?=?4.67, Td?=?57.8?°C). Moreover, APC demonstrated greater resistance to type I collagenase than ARC. The cleavage on the non-helical terminal domains by pepsin might play the role in the better thermal stability, the higher pI, and the more collagenase resistance of APC than ARC. The findings of this work should provide new insights into collagenase hydrolysis behavior and facilitate targeted utilization of collagen extracted by various method.

Substances (5)

Materials
Procduct Name CAS Molecular Formula Supplier Price
Glycine 56-40-6 C2H5NO2 1440 suppliers $5.00-$37817.00
Tris(hydroxymethyl)aminomethane 77-86-1 C4H11NO3 1138 suppliers $5.00-$8920.00
Sodium dodecyl sulfate 151-21-3 C12H25NaO4S 1117 suppliers $6.00-$3140.00
Trypsin 9002-07-7 C35H47N7O10 454 suppliers $17.70-$24930.00
Pepsin 9001-75-6 n.a. 451 suppliers $23.30-$10280.00

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