Biochimica et Biophysica Acta (BBA) - General Subjects
The appearance of free hydroxyproline as the major product of degradation of newly synthesized collagen in cell culture
References (17)
- et al.
J. Biol. Chem.
(1980) Int. Rev. Connect. Tissue Res.
(1970)- et al.
Biochim. Biophys. Acta
(1976) - et al.
Anal. Biochem.
(1966) - et al.
J. Biol. Chem.
(1974) - et al.
Biochim. Biophys. Acta
(1969) - et al.
FEBS Lett.
(1981) - et al.
Nature
(1978)
Cited by (21)
Studying on effects of boiling on texture, microstructure and physiochemical properties of sea cucumber body wall and its mechanism using second harmonic generation (SHG) microscopy
2023, Food ChemistryCitation Excerpt :After 4 h of boiling, the corresponding values were increased to 13.83 ± 0.11 mg/g, 164.23 ± 0.50 μg/g, 2.34 ± 0.04 mg/g and 0.86 ± 0.01 mg/g, respectively. The triple helix collagen in sea cucumbers is insoluble while its degradation products (collagen polypeptides) become water-soluble (Imberman, Oppenheim, & Franzblau, 1982). Hyp and GAGs are the characteristic component of collagen and interfibrillar proteoglycan bridge, respectively.
Effects of heat treatments on texture of abalone muscles and its mechanism
2021, Food BioscienceCitation Excerpt :Collagen is the key structural component of collagenous tissues (Tornberg, 2005). Collagen with a triple helix structure is almost water-insoluble while it becomes water-soluble via degradation (Imberman et al., 1982). Thus, the contents of soluble collagen, dissolution rate of Hyp and GAG were determined to estimate changes in collagenous tissue proteins in abalone muscles during heat treatment.
Effects of proteolysis and oxidation on mechanical properties of sea cucumber (Stichopus japonicus) during thermal processing and storage and their control
2020, Food ChemistryCitation Excerpt :Compared to the blank control group, the two inhibitors significantly retarded the release of water-soluble Hyp, GAGs, and proteins, the increase in TCA-soluble peptide content, and the disintegration of secondary structure of proteins. Collagen with complete triple helix structure is almost water-insoluble, while it becomes water-soluble when degraded into collagen polypeptides (Imberman, Oppenheim, & Franzblau, 1982). Therefore, the release of water-soluble Hyp indicates the degradation of collagen because Hyp is a characteristic amino acid for collagen.
Action of endogenous proteases on texture deterioration of the bay scallop (Argopecten irradians) adductor muscle during cold storage and its mechanism
2020, Food ChemistryCitation Excerpt :Collagen is the main structural component of the connective tissues (Tornberg, 2005). Generally, collagen with a triple helix structure is almost water-insoluble, however, it becomes water-soluble when degraded into collagen polypeptides (Imberman, Oppenheim, & Franzblau, 1982). Therefore, the release of water-soluble Hyp indicates the degradation of collagens.
Inhibitory effect of natural metal ion chelators on the autolysis of sea cucumber (Stichopus japonicus) and its mechanism
2020, Food Research InternationalCitation Excerpt :Among which, the combination of TP and OA showed the best inhibitory effects, followed by OA and TP. Collagen with a complete triple helix structure is almost completely water-insoluble, however it becomes water-soluble when degraded into collagen polypeptides (Imberman, Oppenheim, & Franzblau, 1982). Therefore, the release of water-soluble Hyp, the characteristic amino acid of collagen, is a marker for the degradation of monomeric collagen.
Effect of moisture status on the stability of thermal gels from the body wall of sea cucumbers (Apostichopus japonicus)
2016, LWTCitation Excerpt :Collagen is a major component of the body wall of sea cucumbers, and it accounts for about 70% of the total protein in the body wall (Saito, Kunisaki, Urano, & Kimura, 2002). The degree of collagen degradation in sea cucumbers can be represented by free hydroxyproline content (Imberman, Oppenheim, & Franzblau, 1982; Sakamoto et al., 2015). The free hydroxyproline concentration of samples with different moisture content increased significantly during the entire storage period, as shown in Table 2 (p < 0.05), which indicates that collagen decomposed in all the samples to different degrees.