Abstract

The aim of this study was to characterize the collagens from the body of surf clam shell (Coelomactra antiquata). Guanidine hydrochloride and pepsin were used to extract collagens. Guanidine hydrochloride soluble collagen (GSC) and pepsin soluble collagen (PSC) were separately isolated from the body of surf clam shell. Results showed that the moisture, protein, carbohydrate, and ash contents of the body of surf clam shell were 82.46%, 11.56%, 3.05%, and 2.38%, respectively, but the fat content was only 0.55%. The yields were 0.59% for GSC and 3.78% for PSC. Both GSC and PSC were composed of α1 and α2 chains and a β chain, however, GSC and PSC showed distinct differences from each other and the type I collagen from grass carp muscle on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). GSC and PSC contained glycine as the major amino acid and had imino acid of 150 and 155 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) spectra of GSC and PSC revealed the presence of a triple helix. The GSC appeared to have a dense sheet-like film linked by random-coiled filaments and PSC had fine globular filaments under scanning electron microscopy (SEM). The maximum transition temperature (Tmax) of GSC and PSC was 33.05 °C and 31.33 °C, respectively. These results provide valuable scientific information for the texture study and development of surf clam shell or other bivalve mollusks.

Highlights

  • IntroductionMarine-based species comprise approximately one half of the total global biodiversity, and the oceans and aquatic environments in general offer plenty of resources for novel bioactive components

  • Marine-based species comprise approximately one half of the total global biodiversity, and the oceans and aquatic environments in general offer plenty of resources for novel bioactive components.Marine species contain bioactive compounds and much attention has been paid to them, as they play pivotal roles in disease prevention and the maintenance of human health

  • Appeared to have a dense sheet-like film linked by random-coiled filaments and pepsin soluble collagen (PSC) had fine globular filaments under scanning electron microscopy (SEM)

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Summary

Introduction

Marine-based species comprise approximately one half of the total global biodiversity, and the oceans and aquatic environments in general offer plenty of resources for novel bioactive components. Marine species contain bioactive compounds and much attention has been paid to them, as they play pivotal roles in disease prevention and the maintenance of human health. These marine bioactive compounds exhibit significant biological properties that contribute to their nutraceutical and pharmaceutical potential and are considered to be safer alternatives to some existing synthetic drugs [1,2,3]. The major component of extracellular matrix (ECM) proteins, are a heterogeneous family of structural proteins representing nearly one-third of the total proteins.

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