The use of Fourier‐transform infrared spectroscopy to characterize connective tissue components in skeletal muscle of Atlantic cod (Gadus morhua L.)

Abstract

In the present study, Fourier‐transform infrared spectroscopy (FTIR) is investigated as a method to measure connective tissue components that are important for the quality of Atlantic cod filets (Gadus morhua L.). The Atlantic cod used in this study originated from a feeding trial, which found that fish fed a high starch diet contained relative more collagen type I, while fish fed a low starch (LS) diet contained relative more glycosaminoglycans (GAGs) in the connective tissue. FTIR spectra of pure commercial collagen type I and GAGs were acquired to identify spectral markers and compare them with FTIR spectra and images from connective tissue. Using principal component analysis, high and LS diets were separated due to collagen type I in the spectral region 1800 to 800 cm−1. The spatial distribution of collagen type I and GAGs were further investigated by FTIR imaging in combination with immunohistochemistry. Pixel‐wise correlation images were calculated between preprocessed connective tissue images and preprocessed pure components spectra of collagen type I and GAGs, respectively. For collagen, the FTIR images reveal a collagen distribution that closely resembles the collagen distribution as imaged by immunohistochemistry. For GAGs, the concentration is very low. Still, the FTIR images detect the most GAGs rich regions.

New Insight into Natural Extracellular Matrix: Genipin Cross-Linked Adipose-Derived Stem Cell Extracellular Matrix Gel for Tissue Engineering

“…Thus, our developed, porous gel might be suitable for cell migration and growth. The FTIR spectrum showed the typical bands of amide I, II, and III for the cross-linked ADSC ECM gel, and the presence of amide III relating to C-N stretching and NH reveals the triple helical structure of collagen is preserved [ 66 , 67 ]. Moreover, the spectrum of the cross-linked ADSC ECM gel showed a decrease in the characteristic peak of amine (–NH 2 ) stretch at 1541 cm −1 , and this result was consistent with genipin cross-linked tissue-derived ECM [ 68 ].…”

Contribution of quasi-fibrillar superstructures in peroxide quenching by collagen peptides derived from fish processing by-products and their application as natural food additives

“…A prominent peak at 1451-6cm -1 and a smaller band at 1336-8cm -1 were attributed to the wagging of proline CH 2 and the presence of side chain vibrations, respectively [44]. The Amide III bands displayed a peak at 1202cm -1 and a shoulder peak around 1244cm -1 .…”

“…The presence of GPO triplets confers endo-exo imino ring pucker motions that, coupled with the peptide backbone, leads to expansion and compression of the regions surrounding the triplets [45]. and side-chain vibrations in collagen respectively [44]. The stretches around 1400-1450 and 983-1058cm -1 corresponded to carbonates and skeletal stretches arising due to GPO triplets respectively.…”

Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology

“…FTIR microspectroscopy and imaging have proven to be an excellent tool for analyzing protein structures in tissue related to microstructure (Böcker et al, 2006). The authors have previously shown that connective tissue components important for fish fillet quality were detectable with FTIR spectroscopy [19]. With Principal Component Analysis (PCA), it was possible to detect differences in the relative collagen content.…”