Microstructure and Physical–Chemical Properties of Chicken Collagen

Publication date: Available online 22 February 2016 Source:Food Structure Author(s): Anja Maria Oechsle, Dila Akgün, Franziska Krause, Christiane Maier, Monika Gibis, Reinhard Kohlus, Jochen Weiss The global consumption of sausages has increased immensely over the last few years, while bovine collagen has become scarce. Thus, collagen from alternative sources is being considered for application in the food industry. Therefore, chicken skin and bone collagen were characterized and compared with the bovine telopeptide-poor collagen aiming at the feasibility of producing pure, co-extruded chicken sausages. Hence, the chemical composition, microstructure and rheological properties of the different collagen samples were examined and SDS-PAGE, mass spectroscopy, and ζ-potential analysis were conducted. Weak bands in the SDS-PAGE gel indicated only partial maceration of chicken bone collagen, whereas chicken skin and telopeptide-poor collagen revealed distinct bands indicating collagen type I and III. This was also verified by mass spectroscopy. Large fragments were visible in optical microscopy for chicken bone collagen, whereas chicken skin collagen revealed a delicate network. Moreover, the highest dynamic consistency index, at 14146Pas n*, was determined for chicken bone collagen, followed by chicken skin and telopeptide-poor collagen at 606 and 320Pa s n*, respectively. By contrast, the intrinsic viscosity was the highest for telopeptide-poor collagen (3.16 ...

Source: Food Structure - February 22, 2016 Category: Food Science Source Type: research