Abstract
Collagen is a protein that is a major component of animal skins and tendons. It is used in various medical, cosmetic, and food products through extraction and purification. The fibrous products of purified collagen fibers extracted from raw mammal materials have relatively excellent mechanical properties and are used for high-end medical products. In this study, we examined collagen materials produced from porcine and fish skins, which are major sources of collagen raw materials. We examined a method for spinning collagen fibers from fish skin-based collagen and analyzed the physical properties of those collagen fibers. In addition, we examined the characteristics and advantages of conjugated fibers according to their porcine- and/or fish skin-based compositions. The spinnability and mechanical properties of these conjugated fibers were analyzed according to their compositions. The mechanical properties of collagen structure are determined by hydroxyproline content and can be manipulated by the composition of collagen in the conjugated fibers.
Highlights
Collagen is a natural protein that is the primary material in animals and is abundant in skin, tendons, cartilage, and bones
The proline and hydroxyproline contents were lower to a previous study [22], the hydroxyproline content was low in collagen extracted from for flatfish, which live in relatively cold-water environments compared to tilapia, which fish, and varied between fish species
Collagen fibers have different mechanical properties depending on their amino acid compositions, which vary according to the raw material from which the collagen was extracted
Summary
Collagen is a natural protein that is the primary material in animals and is abundant in skin, tendons, cartilage, and bones. Collagen is perfectly biocompatible and is widely used as a medical and cosmetic material. It is used in various surgical materials and cell research as a biopolymer that can be used both inside and outside the human body [3]. Mammal-skin-based Type-I natural collagen fibers generally have an elastic modulus of 0.3 to 1.2 GPa and an elongation of approximately 10%. A modulus of 1.8 to 2.25 GPa was observed due to higher molecular packing [5]. These mechanical properties were attributed to the amino acid sequence and the coiling of a collagen fibril with a particular triple-helical structure [6]. Collagen has been used in various studies because of its typical physical and chemical
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