Elsevier

Food Chemistry

Volume 89, Issue 3, February 2005, Pages 363-372
Food Chemistry

Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)

https://doi.org/10.1016/j.foodchem.2004.02.042Get rights and content

Abstract

The compositions and some properties of acid-soluble collagens (ASC) of the skin and bone of bigeye snapper, (Priacanthus tayenus) were investigated. The collagens were extracted with the yields of 10.94% and 1.59% on the basis of wet weight, from skin and bone, respectively. Similar electrophoretic patterns of collagens from the skin and bone were observed. Both collagens comprised two different α chains, α1 and α2 and were classified as type I collagen. However, peptide maps of collagen from the skin and bone of bigeye snapper, digested by V8 protease and lysyl endopeptidase, revealed differences between collagens from skin and bone, and both were completely different from those of calf skin collagen. Collagen rehydrated in acetic acid had lower Tmax and enthalpy than those rehydrated in deionised water, suggesting a conformational change caused by acid. Collagens form the skin and bone had the highest solubility at pH 2 and 5, respectively. No changes in solubility were observed in the presence of NaCl up to 3% (w/v). However, a sharp decrease in solubility was found with NaCl above 3% (w/v).

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.

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