Abstract

  Collagen is a major structural protein of connective tissues. It can be used as a prosthetic biomaterial applicable to artificial skin, tendon ligaments and development collagen implants. In the present study, an attempt was made to isolate and characterize collagen from the marine sponge, Spirastrella inconstans. The total protein content of sponge collagen was relatively high (32%). While determining the molecular weight of crude and purified collagen through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the crude showed three bands (80, 60 and 59 kDa molecular weight) and purified showed only a single band (58 kDa). The structural properties were analyzed by using fourier transform infra red (FT-IR) spectrum and the stability of collagen was also given the single transition peak in differential scanning calorimetry (DSC). The microstructure of sponge collagen showed highly porous and interconnected scaffolds in scanning electron microscopic (SEM) analysis.   Key words: Collagen, Spirastrella inconstans, SDS-PAGE, Fourier transform infrared (FT-IR), differential scanning calorimetry (DSC), scanning electron microscopy (SEM)

Highlights

  • Collagen is a fibrous protein found ubiquitously in all multicellular animals

  • The structural properties were analyzed by using fourier transform infra red (FT-IR) spectrum and the stability of collagen was given the single transition peak in differential scanning calorimetry (DSC)

  • Total protein and collagen content In S. inconstans, the total protein content corresponds to\ 32% and the yield of collagen was found to be 0.16%.The sponge collagen was examined by SDS-PAGE, using a 12% resolving gel and the molecular weight of purified collagen from S. inconstans was recorded as 58 kDa (Figure 1)

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Summary

Introduction

Collagen is a fibrous protein found ubiquitously in all multicellular animals It is rigid and inextensible extracellular matrix protein that serves as a major constituent of many connective tissues. It is distributed in skin, bones, cartilage, tendons, ligaments, blood vessels, teeth, cornea and all other organs of vertebrates and constitutes approximately 30% of total animal protein (Muyonga et al, 2004; Senaratne et al, 2006). The characteristic feature of a typical collagen is long, stiff, triple-stranded helix, in which three collagen polypeptide chains are wrapped around one another in the form of a rope-like upper helix.

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