Abstract
This study aimed to isolate and characterize the acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of the sharpnose stingray (Dasyatis zugei). Isolated ASC and PSC were subjected to chemical and physical characterizations. The yield of PSC (34.84±1.26%) was significantly higher than that of ASC (20.48±4.41%) (p<0.05). There were no significant differences between ASC and PSC in terms of chemical composition (p>0.05). Both ASC and PSC were thermally stable at high temperatures, with denaturation temperatures of 24.1°C and 25.2°C, respectively, and maximum temperatures of 31.94±0.13°C and 31.79±0.23°C, respectively. Fourier transform infrared (FTIR) investigations showed the presence of triple helical structure with strong hydrogen bonding in both ASC and PSC. Meanwhile, both collagens were highly solubilized at acidic pH but at different optimal pH. The surface morphologies of ASC and PSC were loose and possessed slender, less uniform and irregular fibrous network structures with large and irregular pores observed between the fibrils. This finding showed that the alternative source of marine collagen possesses good physicochemical properties which highly potential for nutraceutical, pharmaceutical or cosmeceutical application.
Highlights
Recent years have seen the proliferation of infectious diseases such as bovine spongiform encephalopathy (BSE), transmissible spongiform encephalopathy (TSE), foot-and-mouth disease (FMD) and avian influenza (Baderi and Sarbon, 2019)
To make more effective use of the wastes generated during fish processing, this study aims to isolate and characterize acid-solubilized collagen (ASC) and pepsin solubilized collagen (PSC) from the skin of the sharpnose stingray
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from the skin of the sharpnose stingray and their yield was calculated according to their respective sample weight
Summary
The origin of the word ‘collagen’ is from a Greek term, ‘kola’ which has a definition of gum/glue and ‘gen’ which means producing. Collagen can be extracted from various tissues, such as tendons, ligaments, and other connective tissues (Silvipriya et al, 2015). Recent years have seen the proliferation of infectious diseases such as bovine spongiform encephalopathy (BSE), transmissible spongiform encephalopathy (TSE), foot-and-mouth disease (FMD) and avian influenza (Baderi and Sarbon, 2019). Recent studies have emphasized on the extraction of collagen from marine organisms to replace bovine and porcine collagen (El-Rashidy et al, 2015). Collagen can be extracted through a series of complex procedures, beginning with the collection of raw materials, pretreatment, extraction, purification and some more steps before to be used in different industries. On the basis of the extraction methods, collagens can extract by four distinct methods which are salting-out method, alkali method, acid method and enzyme method (Schmidt et al, 2016)
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