Structural and molecular characterization of collagen‐type I extracted from lamb feet

Abstract

AbstractThis study aimed to extract collagen‐I from lamb feet (LF) and examine the effects of ultrasound treatment on the structural and molecular characteristics of the collagen. Compared to ultrasonic bath treatment and conventional extraction methods, ultrasonic probe (USP) treatment significantly increased the collagen content of the extract (p < 0.05). The electrophoretic profiles confirmed the presence of α‐ and β‐chains, indicating it as type I. Furthermore, X‐ray diffraction, Fourier‐transform infrared spectroscopy, and circular dichroism spectra analyses revealed that the extraction method did not adversely affect the triple helix structure of the collagen. Moreover, the fibrillar structure of the collagen samples was verified through scanning electron microscopy analyses. Notably, the LF collagen exhibited a high thermal denaturation temperature owing to its elevated imino acid content. The collagen samples exhibited high solubility in acidic pH but low solubility in high salt concentrations. The present findings signified that sonication with USP can effectively enhance the yield of collagen from LF without compromising its quality.Practical ApplicationThis study showed that ultrasonication enhanced the collagen concentration without disturbing the integrity of lamb feet collagen. We expect that lamb feet collagen can be used for industrial processes and consumer products thanks to unique product properties.