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Properties of gelatin and poly (3-hydroxybutyrate-co-3-hydroxy-valerate) blends
Published in Ai Sheng, Energy, Environment and Green Building Materials, 2015
Ya Li, Jing-Kuan Duan, Ya-Juan Wang, Lan Jiang, Kai-Qi Shi, Shuang-Xi Shao
Gelatin can be widely found in nature and is the major constituent of skin, bones and connective tissue, it can be obtained by a controlled hydrolysis of fibrous insoluble protein and collagen[Fan, L. H. et al 2005, Zhang, Y. Z. et al 2005, Pawde, S. M. and Deshmukh, K. 2008]. It is widely used in various applications as manufacturing of pharmaceutical products, X-ray and photographic films development and food processing et al.[Yannas, I. V. 1972]. Gelatin is characterized by having a high content of the amino acid glycine (33 mol%) and the presence of the amino acid hydroxyproline (10 mol%) and hydroxylysine (0.5 mol%). The properties of gelatin as a typical rigid-chain high molecular weight compound are in many respects similar to those of rigid-chain synthetic polymers, but it is different from the common biopolymers for the presence of both acidic and basic functional groups in the gelatin macromolecules[Kozlov, P. V. & Burdygina, G. I. 1983].
Proteins and Proteomics
Published in Firdos Alam Khan, Biotechnology Fundamentals, 2020
Lysine: Lysine is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. The codons of this essential amino acid are AAA and AAG. Lysine is a base, as are arginine and histidine. The ε-amino group often participates in hydrogen bonding and as a general base in catalysis. Common PTMs include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyl lysine. The latter occurs in calmodulin. Other PTMs at lysine residues include acetylation and ubiquitination. Collagen contains hydroxylysine which is derived from lysine by lysyl hydroxylase. O-Glycosylation of lysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.
Biomolecules and Tissue Properties
Published in Joseph W. Freeman, Debabrata Banerjee, Building Tissues, 2018
Joseph W. Freeman, Debabrata Banerjee
Type I collagen fibers have an elastic modulus of 5–900 MPa and a ultimate tensile strength (UTS) of 2–92 MPa.2,3 Collagenous tissues increase in strength with the development of crosslinks, which stabilize collagen fibers. The formation of these crosslinks involves histidine, lysine, and hydroxylysine residues (Figure 3.11).
Spectroscopic imaging: Nuclear magnetic resonance and Raman spectrometry for the detection of collagen cross-linking from giant squid mantle, fin, and tentacle tissues
Published in Instrumentation Science & Technology, 2018
Héctor M. Sarabia-Sainz, Wilfrido Torres-Arreola, Josafat Marina Ezquerra-Brauer
Recent years have seen increased interest in identifying and characterizing bioactive proteins derived from marine sources. Among them, squid by-products are valuable underutilized sources of protein, where the predominant protein is collagen. Collagen is a fibrous insoluble protein mostly found in skin, cartilage, and connective tissues, whose primary function is to provide support; this protein maintains the union between cells.[1] Several types of collagen have been identified; the primary characteristics of all types are amino acid arrangements that are rich in proline and glycine. These arrays form three chains that intertwine to create a triple helix, which varies in composition and size.[2] The principal collagen fiber cross-linking mechanism reported is the oxidation of hydroxylysine by lysyl oxidase, which results in pyridinoline.[3] Pyridinoline is an aromatic molecule that can be covalently linked to up to three collagen chains.[4]