Abstract
The aim of this study was to investigate the physicochemical properties of silver catfish skin collagen as affected by acetic acid concentration (0.5M and 0.7M). Acid solubilised collagen (ASC) were isolated from the skin of silver catfish (Pangasius Sp.) and were compared with commercial collagen. The yields of extracted collagen using 0.5M and 0.7M acetic acid were 10.94±0.38% and 5.47±0.20%, respectively. The pH values for commercial collagen and extracted collagen for 0.5M and 0.7M acetic acid values were 6.52±0.04, 4.04±0.06 and 3.79±0.28, respectively. The functional group of collagen was successfully detected, along with a flaky and fibrous morphology structure. The relative viscosity for all samples decreased with an increase in temperature. Collagen extracted with 0.5M acetic acid is more efficient for use as a solvent for collagen extraction since it produces a higher yield and higher fibrous collagen thickness. This study found that collagen extracted from silver catfish (Pangasius sp.) had the potential to be used as alternative fish collagen in various fields.
Highlights
Collagen is a fibrous protein and is the most abundant protein in animals, constituting approximately 30% of total proteins (Zhang et al, 2010)
3.1 Yield of collagen extracted from the skin of silver catfish (Pangasius sp.)
The yield of acid-soluble collagen (ASC) extracted by 0.5M acetic acid was higher than that of 0.7M acetic acid, perhaps due to the presence of low levels of collagen content caused by denaturation of protein during the extraction process as affected by different acid concentration (Rigo et al, 2002)
Summary
Collagen is a fibrous protein and is the most abundant protein in animals, constituting approximately 30% of total proteins (Zhang et al, 2010). A total of 27 different types of collagen have been identified. Type I collagen is widely found in collagen connective tissue (Guillén et al, 2011). Due to its wide range of industrial applications, collagen is one of the most useful biomaterials. Its high protein content and good functional properties, including water absorption capacity, gel formation, and the ability to form and stabilize emulsions have led to strong demand for collagen in the food industry (Schmidt et al, 2016). The supply of mammalian collagen has declined in recent years due to concerns regarding bovine and porcine health, such as the emergence of bovine spongiform encephalopathy and foot and mouth disease (Nagai et al, 2010). A realistic alternative to mammalian collagen is fish collagen derived from skin, scales, and bone (Thuy et al, 2014)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
