Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)
Introduction
Thailand is one of the largest surimi producers in Southeast Asia. At present, twelve surimi factories are located in Thailand, with a total production of about 60,000 metric tonne per year (Morrissey & Tan, 2000). The fish used for surimi production are mostly threadfin bream (Nemipterus spp.), bigeye snapper (Priacanthus spp.), croaker (Pennahia and Johnius spp.) and lizardfish (Saurida spp.) (Benjakul, Chantarasuwan, & Visessanguan, 2003). During surimi processing, numerous wastes, both liquid and solid form, are generated (Morrissey, Park, & Huang, 2000). The solid wastes constitute 50–70% of the original raw material, depending on the processing used. These wastes are a mixture of heads, viscera, skin and bone (Morrissey et al., 2000). Although the nutritional values of these wastes are fairly high, these useful resources have been mainly used as fish meal or fertiliser with low value (Nagai & Suzuki, 2000a). Also, improper disposal of these wastes may cause pollution and emit an offensive odour. Hence, optimal utilisation of surimi processing wastes, especially in the production of value-added products is a promising means to increase revenue for the producer and to decrease the cost of disposal or management of these wastes.
Collagen has a wide range of applications in leather and film industries, pharmaceutical, cosmetic and biomedical materials and food (Bailey & Light, 1989; Cavallaro, Kemp, & Kraus, 1994; Hood, 1987; Hassan & Sherief, 1994; Nimni, 1988; Slade & Levine, 1987; Stainsby, 1987). Generally, pig and cow skins and bones are the main sources of collagen isolation. However, the outbreak of mad cow disease has resulted in anxiety among users of cattle gelatin. Additionally, the collagen obtained from pig bones cannot be used, due to religious constraints (Sadowska, Kolodziejska, & Niecikowska, 2003). As a consequence, increasing attention has been paid to alternative collagen sources, especially fish skin and bone from seafood processing wastes. About 30% of these wastes consist of skin and bone, which are very rich in collagen (Gomez-Guillen et al., 2002; Shahidi, 1994). However, fish collagens have lower thermal stability than mammalian collagens because fish collagens contain lower imino acid contents than mammalian collagens (Foegeding, Lanier, & Hultin, 1996). So far, skin and bone collagen from several fish species have been isolated and characterised (Ciarlo, Paredi, & Fraga, 1997; Kimura, Miyauchi, & Uchida, 1991; Kimura, Ohno, Miyauchi, & Uchida, 1987; Nagai, Araki, & Suzuki, 2002; Nagai and Suzuki, 2000a, Nagai and Suzuki, 2000b; Sadowska et al., 2003; Yata, Yoshida, Mizuta, & Yoshinaka, 2001). However, no information regarding the collagen from tropical fish, particularly from surimi processing waste, has been reported. Bigeye snapper (Priacanthus tayenus) is commonly used for surimi production due to its high gel-forming ability (Benjakul, Visessanguan, Ishizaki, & Tanaka, 2001). Therefore, the objective of this investigation was to isolate and characterise acid-soluble collagen from skin and bone of bigeye snapper.
Section snippets
Fish skin and bone preparation
The skin and bones of bigeye snapper (Priacanthus tayenus) were obtained from Man A Frozen Foods Co. Ltd., Songkhla, Thailand. Residual meat was removed manually and cleaned samples were washed with tap water. The skin was descaled, followed by thorough washing. Descaled samples were then cut into small pieces (0.5 × 0.5 cm2), placed in polyethylene bags and stored at −20 °C until used. Bone was cut into small pieces (1–2 cm in length) and powdered by mixing the samples in liquid nitrogen for 20
Proximate analyses of bigeye snapper skin and bone and their collagen
The proximate analyses of bigeye snapper skin, bone and their collagen are shown in Table 1. Skin and bone contained a high moisture content (62.3–64.1%). The ash and fat contents of bone were greater than those of skin. Conversely, a lower protein content was observed in bone than in skin. Skin had a higher content of hydroxyproline than bone. Sadowska et al. (2003) reported that hydroxyproline content of cod skin was 14.6 mg/g sample, which was lower than that of bigeye snapper skin (19.5
Conclusion
Collagens extracted from skin and bone of bigeye snapper were classified as type I with slightly different amino acid compositions. Peptide maps of collagens from the skin and bone digested by V8 protease and lysyl endopeptidase were slightly different, indicating some differences in amino acid sequence or conformation. Collagens showed high solubility at acidic pH (2–5) and the solubility markedly decreased in presence of NaCl (above 3%).
Acknowledgements
The author thanks to Prince of Songkla University and Japanese Society for Promotion of Science (JSPS) for the financial support. The authors also thank Professor Akira Shinagawa of Faculty of Intercultural Studies, Environment Education Center, Gakushuin Women's College for his assistance in amino acid analysis.
References (58)
- et al.
Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish
Food Chemistry
(2003) - et al.
Structural and physical properties of gelatin extracted from different marine species: A comparative study
Food Hydrocolloids
(2002) - et al.
Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloiicas
International Journal of Biological Macromolecules
(2003) Wide distribution of the skin type I collagen α3 chain in bony fish
Comparative Biochemistry and Physiology Part B
(1992)- et al.
Scale and bone type I collagens of carp (Cyprinus carpio)
Comparative Biochemistry and Physiology Part B
(1991) - et al.
Fish type I collagen: Tissue specific existence of two molecular forms, (α1)2 α2 and α1α2α3, in Alaska pollack
Comparative Biochemistry and Physiology Part B
(1987) - et al.
Fish skin type I collagen: Wide distribution of an α3 subunit in teleosts
Comparative Biochemistry and Physiology Part B
(1987) - et al.
The connective tissues and collagens of cod during starvation
Comparative Biochemistry and Physiology Part B
(1976) - et al.
Characterization of an α3 chain from the skin type I collagen of chum salmon (Oncorhynchus keta)
Comparative Biochemistry and Physiology Part B
(1991) - et al.
Collagen of skin of ocellate puffer fish (Takifugu rubripes)
Food Chemistry
(2002)
Isolation of collagen from fish waste material-skin, bone and fins
Food Chemistry
Preparation and partial characterization of collagen from paper nautilus (Argo nauta argo, Linnaeus) outer skin
Food Chemistry
NMR and DSC studies during thermal denaturation of collagen
Food Chemistry
Isolation of collagen from the skins of Baltic cod (Gadus morhua)
Food Chemistry
Chemical, biochemical, functional and nutritional characteristics of collagen in food systems
Connective tissue in meat and meat products
Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus
Journal of Food Science
Two improved and simplified methods for the spectrophotometric determination of hydroxyproline
Analytical Chemistry
Collagen
Collagen fabrics as biomaterials
Biotechnology and Bioengineering
Isolation of soluble collagen from hake skin (Merluccius hubbsi)
Journal of Aquatic Food Product Technology
Collagen
The function of hydroxyproline in collagens
Nature
The chemistry and reactivity of collagen
Collagen in sausage casings
Role and application of fish collagen
Seafood Export Journal
The interstitial collagens of fish
Discrete reduction of type I collagen thermal stability upon oxidation
Biophysical Chemistry
Cited by (460)
Extraction and characterization of hyaluronic acid from the eyeball of Nile Tilapia (Oreochromis niloticus)
2023, International Journal of Biological Macromolecules