Abstract
Collagen is widely used in drugs, biomaterials, foods, and cosmetics. By-products of the fishing industry are rich sources of collagen, which can be used as an alternative to collagen traditionally harvested from land mammals. However, commercial applications of fish-based collagen are limited by the low efficiency, low productivity, and low sustainability of the extraction process. This study applied a new technique (electrodialysis) for the extraction of Takifugu flavidus skin collagen. We found electrodialysis to have better economic and environmental outcomes than traditional dialysis as it significantly reduced the purification time and wastewater (~95%) while maintaining high extraction yield (67.3 ± 1.3 g/100 g dry weight, p < 0.05). SDS-PAGE, amino acid composition analysis, and spectrophotometric characterization indicated that electrodialysis treatment retained the physicochemical properties of T. flavidus collagen. Heavy metals and tetrodotoxin analyses indicated the safety of T. flavidus collagen. Notably, the collagen had similar thermal stability to calf skin collagen, with the maximum transition temperature and denaturation temperature of 41.8 ± 0.35 and 28.4 ± 2.5 °C, respectively. All evidence suggests that electrodialysis is a promising technique for extracting collagen in the fishing industry and that T. flavidus skin collagen could serve as an alternative source of collagen to meet the increasing demand from consumers.
Highlights
Collagen is the major structural component of various extracellular matrices in mammalian connective tissues, such as the skin, corneas, cartilage, bone, and blood vessel [1]
Some previous works have suggested that the accumulation of heavy metals in fish depends on the dietary ingestion rate and the concentration of heavy metals in the ingested food [21]
Our study showed that T. flavidus collagen residues/1000 amino acid residues) had significantly higher imino acid content than the skin (Table 2, 246 ± 0.04 residues/1000 amino acid residues) had significantly higher imino acid content collagen of bighead carp, bigeye snapper, grass carp, and T. rubripes (p < 0.05, 165–193 residues/1000 than the skin collagen of bighead carp, bigeye snapper, grass carp, and T. rubripes (p < 0.05, amino acid residues) [14,16,23,24]
Summary
Collagen is the major structural component of various extracellular matrices in mammalian connective tissues, such as the skin, corneas, cartilage, bone, and blood vessel [1]. Collagen is widely used in biomaterials, drugs, foods, and cosmetics [2]. Its high biocompatibility as well as the ability to support cell growth and differentiation has made it an important matrix for cell biology, cosmetics, and regenerative medicine [3,4]. Collagen is widely used as a gelatin precursor in the food industry for formulating emulsions, foams, colloids, and biodegradable films [5]. Despite high feasibility and biocompatibility, these mammalian origins potentially limit practical application of collagen due to sociocultural beliefs (e.g., in Muslim countries and India). The mammalian origins can further restrain collagen application by increasing additional sanitary costs for industrial production because of extensive consumer concerns regarding transmissible diseases from porcine and bovine [7,8]
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