Abstract
With increased recent interest in the utilization of industrial by-products, finding different sources, optimizing extracting conditions and characterization of collagen extracts have recently become important research topics. This study addresses the isolation of acid-soluble and pepsin-soluble forms of collagen from dried jellyfish and squid, and their partial characterization. The properties of these proteins have been studied and a comparison made of the protein patterns of collagen extracted from marine organisms with those from other organisms, to determine which collagen subtypes are present, and in what proportions. Pepsin-soluble collagen (PSC) from dried jellyfish and dried squid contained a collagen form classified as type I, of molecular composition comparable with that of collagen type I from rat tail. Peptide maps of collagens digested by achromopeptidase were slightly different, indicating some differences in amino acid sequence or conformation. The collagen showed high solubility at acidic pH (4-5) but its solubility markedly decreased in the presence of sodium chloride (NaCl) up to 2%. Collagen type I from dried jellyfish and dried squid could be a useful alternative to mammalian collagen, with potential use in the biomedical, pharmaceutical and nutraceuticals industries. Key words: Collagen, pepsin-soluble form, acid-soluble form, partial characterization.
Highlights
Collagen is a major class of structural proteins in bone, skin, cartilage and connective tissue (Liu et al, 2007; Ogawa et al, 2003; Bateman et al, 1996)
In the case of collagen extracted from jellyfish, the acid-soluble collagen (ASC) fraction contained no high-molecular weight bands, there was a band of molecular weight about 21 kDa, which was found in the pepsin-soluble collagen (PSC) fraction and bands of α1 and α2 chains were visible near 116 kDa in the PSC fraction
Bands below 116 kDa represent the products of enzymatic hydrolysis of collagen
Summary
Collagen is a major class of structural proteins in bone, skin, cartilage and connective tissue (Liu et al, 2007; Ogawa et al, 2003; Bateman et al, 1996). It plays an important role in tissue development and is the most abundant protein in vertebrates, constituting about 30% of the total. Collagen finds a wide range of applications in the food, cosmetic, biomedical, pharmaceutical, leather and film industries. The collagens from different tissues vary considerably in polypeptide chain composition, amino acid composition and physiochemical characteristics, thereby meeting the specific functional requirements of the tissues.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
