Physicochemical properties of acid‐soluble collagens from different tissues of large yellow croaker (Larimichthys crocea)

Abstract

Acid-soluble collagens (ASCs) were extracted and characterised from different tissues of large yellow croaker (Larimichthys crocea). The yields of ASCs in bones, skins, scales and muscles were 3.22 AE 0.47%, 42.30 AE 1.15%, 2.82 AE 0.31% and 0.89 AE 0.12%, respectively. SDS-PAGE and ATR-FTIR analysis showed that all ASCs were type I collagen with intact triple helical structure and consisted of α1,3-chain, α2-chain, β-chain and γ-chain. Quantitative analysis of SDS-PAGE revealed that the ratio of β-chains in ASC from scales was lower than other tissues. The imino acid contents of ASC from bones, skins, scales and muscles were 169, 167, 162 and 173 residues/1000 residues, respectively. The maximum transition temperature (T m ) of ASC from scales was 30.15 °C, lower than the other three ASCs, indicated that the thermal stability of collagen was affected by both the content of imino acid and β-chains. The results also implied that thermal stability of ASC might exist the tissue specificity among different fish species.

Comparative assessment of bone collagen recovered from different livestock and poultry species: microstructure, physicochemical characteristics and functional properties

“…Sun et al . (2021b) reported that the β‐chain intensities were correlated with the thermal stability in fish collagen, which was different from this study results. This difference was possible related to the different sources or extraction procedure.…”

“…The ratio of band intensity of α1/α2‐chains were approximately 2:1 in all LBCs (Fig. 1b), indicating that there existed inter‐ and intra‐molecular cross‐linkages in LBC molecules, which might be positively related to the thermal stability of collagen (Sun et al ., 2021b). Pepsin was able to remove the cross‐linked telopeptide to convert β‐ and γ‐chains to α‐chains.…”

“…To our knowledge, it is the collagen structural difference determines the variety of physicochemical and functional properties. A comparative study confirmed that the T m value of fish collagen is directly related to imino acid contents (Sun et al, 2021b). Akita et al (2020) extracted collagen I from several cold and warm water fish and explored the correlation among the ratio of positive peak intensity to negative peak intensity in CD analysis (Rpn), tryptophan content, imino acid contents and denaturation temperature.…”

“…To our knowledge, it is the collagen structural difference determines the variety of physicochemical and functional properties. A comparative study confirmed that the T m value of fish collagen is directly related to imino acid contents (Sun et al ., 2021b). Akita et al .…”

Preparation and Characterization of Tilapia Collagen-Thermoplastic Polyurethane Composite Nanofiber Membranes

“…The two high-molecular-weight components had weights over 200 kDa. These were identified as a β-chain consisting of two α-chains and a γ-chain consisting of three α-chains, respectively [ 24 ]. In addition, the ratio of α1 and α2 was calculated with Image J software (VERSION 1.8.0, National Institute of Mental Health, Bethesda, MD, USA); specifically, approximately 2:1 was consistent with the molecular structure of type I collagen [α1] 2 α2, thus indicating that the prepared TSC was type I collagen.…”