Structural and molecular characterization of collagen-type I extracted from lamb feet
Küçük Resim Yok
Tarih
2023
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Wiley
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
This 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 alpha- and beta-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.
Açıklama
Anahtar Kelimeler
characterization, lamb feet, triple helix, type I collagen, ultrasound treatment, Acid-Soluble Collagen, Skin, Bone, Food
Kaynak
Journal of Food Science
WoS Q Değeri
Q2
Scopus Q Değeri
Q1
