Abstract

In this report, acid-soluble collagen (ASC-MC) and pepsin-soluble collagen (PSC-MC) were extracted from the scales of miiuy croaker (Miichthys miiuy) with yields of 0.64 ± 0.07% and 3.87 ± 0.15% of dry weight basis, respectively. ASC-MC and PSC-MC had glycine as the major amino acid with the contents of 341.8 ± 4.2 and 344.5 ± 3.2 residues/1000 residues, respectively. ASC-MC and PSC-MC had lower denaturation temperatures (32.2 °C and 29.0 °C for ASC-MC and PSC-MC, respectively) compared to mammalian collagen due to their low imino acid content (197.6 and 195.2 residues/1000 residues for ASC-MC and PSC-MC, respectively). ASC-MC and PSC-MC were mainly composed of type I collagen on the literatures and results of amino acid composition, SDS-PAGE pattern, ultraviolet (UV) and Fourier-transform infrared spectroscopy (FTIR) spectra. The maximum solubility of ASC-MC and PSC-MC was appeared at pH 1–3 and a sharp decrease in solubility was observed when the NaCl concentration was above 2%. Zeta potential studies indicated that ASC-MC and PSC-MC exhibited a net zero charge at pH 6.66 and 6.81, respectively. Furthermore, the scavenging capabilities on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, hydroxyl radical, superoxide anion radical and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical of ASC-MC and PSC-MC were positively correlated with their tested concentration ranged from 0 to 5 mg/mL and PSC-MC showed significantly higher activity than that of ASC-MC at most tested concentrations (p < 0.05). In addition, the scavenging capability of PSC-MC on hydroxyl radical and superoxide anion radical was higher than those of DPPH radical and ABTS radical, which suggested that ASC-SC and PSC-SC might be served as hydroxyl radical and superoxide anion radical scavenger in cosmeceutical products for protecting skins from photoaging and ultraviolet damage.

Highlights

  • Collagen is the most abundant protein constituting nearly 30% of all proteins in the animal body and is a primary component of the extracellular matrix [1]

  • Radical of acid-soluble collagen (ASC)-MC and pepsin-soluble collagen (PSC)-MC were positively correlated with their tested concentration ranged from 0 to 5 mg/mL and PSC-MC showed significantly higher activity than that of ASC-MC at most tested concentrations (p < 0.05)

  • The data indicated that the vast majority (>95%) of inorganic substances were removed from the scales of miiuy croaker by demineralization process

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Summary

Introduction

Collagen is the most abundant protein constituting nearly 30% of all proteins in the animal body and is a primary component of the extracellular matrix [1]. Large quantities of scales are discarded as waste during processing and filleting due to lower economic value, which give rise to some additional ecological environmental problems especially in developing countries Effective use of those resources solves the problem of environmental pollution and increases economic returns for the fishery industry. There are some differences in structure and amino acid composition of collagens from different fish scales due to the living environment and species, which further influence the physicochemical and bioactive properties of collagens. Pepsin-soluble collagen (PSC-MC) from the scales of miiuy croaker (M. miiuy) were prepared and their physicochemical and antioxidant properties were characterized for their potential applications in the cosmetic and biomedical industries

Proximate and Yield Analysis
Amino Acid Analysis
SDS-PAGE
ASC-MC and and PSC-MC
Peptide
Ultraviolet
Fourier-Transform
Relative viscosity changes and pepsin-soluble pepsin-solublecollagen collagen
Collagen
2.10. Antioxidant Activity
Experimental Section
Extraction
Proximate Analysis
Electrophoretic Pattern
Peptide Hydrolysis Patterns
UV Measurements
FTIR Spectral Analysis
Viscosity
3.10. Solubility
3.10.1. Effect of pH on Solubility
3.10.2. Effect of NaCl on Solubility
3.11. Zeta Potential
3.12. Collagen Ultrastructure
3.13. Antioxidant Activity
3.14. Statistical Analysis
Conclusions
Full Text
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