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Stabilization of type I collagen using dialdehyde cellulose

Paper ID Volume ID Publish Year Pages File Format Full-Text
35486 45092 2009 6 PDF Available
Title
Stabilization of type I collagen using dialdehyde cellulose
Abstract

Type I collagen from rat tail tendon (RTT) fibres was crosslinked with dialdehyde cellulose to bring about stabilization of the matrix. Dialdehyde cellulose (DAC) was prepared by periodate oxidation of hydrolyzed cellulose. Autoclaving of DAC resulted in hydrolysis and lower molecular weight oligomeric species. The formation of the crosslinked network between DAC and the collagen fibres has brought about significant thermal and enzymatic stability to collagen. DAC crosslinked collagen fibres exhibited an increase in hydrothermal stability by 20 °C with autoclaved DAC at pH 8. The collagen matrix resulted in an increase in denaturation peak temperature (TD) and an increase in phase change of activation energy (Ea) and enthalpy change (ΔH) for the shinking process indicating intermolecular crosslinking arising from covalent interactions. Thermal stability and crosslinking efficiency was found to increase with pH and concentration of DAC. DAC treated collagen exhibited 93% resistance to collagenolytic hydrolysis.

Keywords
Collagen; Dialdehyde cellulose; Crosslinking; Thermal stability; Collagenase; Enzyme stability
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 869–874
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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