A method for the process of collagen modified polyester from fish scales waste.

In this study, we introduced a novel polymerization method of polyester using collagen peptides derived from fish scale waste. After the extraction process of collagen peptide from fish scales, putting collagen peptide, ethylene glycol and Benzenedicarboxylic acid into a container, and mixing them to form a mixture; heating the mixture for executing an esterification reaction, to product esters and water; heating the esters, and stirring the esters via a mixer; in a specific period, decreasing the pressure in the container for executing a polycondensation reaction; decreasing the pressure in the container to a second pressure, and stirring the esters via the mixer, to produce a collagen modified polyester. Collagen peptides are rich in glycine, proline, and hydroxyproline, and by forming a triple helix structure, such as that of the copolyester, gain better hydrophilicity, antistaticity, and ductility. As a result, the produced collagen modified polyester fiber keeps the characteristics of the traditional polyethylene terephthalate fibers including strength, durability, and resistance to wrinkle and shrink. However, the supramolecular collagen modified polyester containing animal collagen peptides has naturally a soft touch and champagne-like color. Consequently, it can be used as a suitable material for skin-friendly functional clothes with or without additional dying. In brief,•This study introduces a novel method for collagen modified polyester.•Upcycled fish scale waste brings the sustainable benefits of circular economy.•Collagen modified polyester provides a new direction for future technological development in the textile industry.

A Study on Circular Economy Material Using Fish Scales as a Natural Flame Retardant and the Properties of Its Composite Materials.

Fish scales (FSs) are fishery wastes that can cause environmental pollution. This study aimed to solve this environmental problem. FSs were used as a flame retardant for polymer materials, making them valuable. Fish scales were combined with a commercial flame retardant, ammonium polyphosphate (APP), through synergistic effects to reduce the amount of commercial flame retardant. The use of FSs conforms to the concept of a circular economy and lowers costs by reducing the consumption of APP. Thermogravimetric analysis (TGA), integral procedural decomposition temperature (IPDT), pyrolysis kinetics, limiting oxygen index (LOI), the Underwriters Laboratories 94 (UL94) flammability test, scanning election microscopy, Raman spectroscopy, and energy-dispersive X-ray spectroscopy were used to determine the thermal properties, flame retardant properties, flame retardant mechanism, char morphology, and composition of the composites. The TGA results indicated that the addition of 40% flame retardant raised the char residue from 16.45 wt.% (pure EP) to 36.07 wt.%; IPDT from 685.6 °C (pure EP) to 1143.1°C; LOI from 21% (pure EP) to 30%; and UL94 classification from fail (pure EP) to V-0. These results suggest an increase in char residue, which indicates better protection of the polymer matrix material. The improvements in IPDT, LOI, and UL94 classification, which indicate greater thermal stability, lower flammability (from flammable to fireproof), and higher flammability rating (from fail to V-0), respectively, suggest that the composite material has favorable thermal properties and is less inflammable.

Comparative assessment of physico-chemical characteristics and fibril formation capacity of thermostable carp scales collagen.

Collagen and collagen fibers have been widely documented as a potential and competitive biomaterial for medical applications. However, the searches for safe and realistic new collagen sources are still underway. Currently, fishery by-products (scales), a promising collagen source are usually discarded. In the present study, in vitro fibril-forming ability of the extracted fish scale collagen is reported. The aim of the investigation was to evaluate the concomitant comparison of fibril-forming abilities and characteristics of acid and pepsin soluble collagens from the scales of Indian major carp catla (Catla catla) and rohu (Labeo rohita). The extracted collagens were characterized as type I, with a total yield of 2.80-4.11% (w/w). Denaturation temperature determined for all collagens were between 35.9 and 37.7°C. All collagens exhibited high solubility in acidic pH and low NaCl concentrations. SEM clarified the lyophilized collagens and their fibril-forming capacity. Amino acid content and radical scavenging efficacy were also analyzed for the extracted collagen. The results revealed that extracted scale collagen from a renewable biological source could be used as biomaterials in various sectors. It might be suitable for preparing collagen gel for biomedical devices or as a scaffold for cell culture because of its high stability and fibril formation capacity.