Characteristics and Properties of Acid- and Pepsin-Solubilized Collagens from the Tail Tendon of Skipjack Tuna (Katsuwonus pelamis)

Sagun Chanmangkang; Sutee Wangtueai; Nantipa Pansawat; Pramvadee Tepwong; Atikorn Panya; Jirawan Maneerote

doi:10.3390/polym14235329

Characteristics and Properties of Acid- and Pepsin-Solubilized Collagens from the Tail Tendon of Skipjack Tuna (Katsuwonus pelamis)

Polymers (Basel). 2022 Dec 6;14(23):5329. doi: 10.3390/polym14235329.

Authors

Sagun Chanmangkang¹, Sutee Wangtueai¹, Nantipa Pansawat², Pramvadee Tepwong², Atikorn Panya³, Jirawan Maneerote²

Affiliations

¹ College of Maritime Studies and Management, Chiang Mai University, Samut Sakhon 74000, Thailand.
² Department of Fishery Products, Faculty of Fisheries, Kasetsart University, Bangkok 10900, Thailand.
³ Food Biotechnology Research Unit, National Center for Genetic Engineering and Biotechnology, Pathum Thani 12120, Thailand.

Abstract

The tail tendons of skipjack tuna (Katsuwonus pelamis), a by-product from the meat-separation process in canned-tuna production, was used as an alternative source of collagen extraction. The acid-solubilized collagens using vinegar (VTC) and acetic-acid (ATC) extraction and pepsin-solubilized collagen (APTC) were extracted from tuna-tail tendon. The physiochemical properties and characteristics of those collagens were investigated. The obtained yield of VTC, ATC, and APTC were 7.88 ± 0.41, 8.67 ± 0.35, and 12.04 ± 0.07%, respectively. The determination of protein-collagen solubility, the effect of pH and NaCl on collagen solubility, Fourier-transform infrared spectroscopy (FTIR) spectrum, and microstructure of the collagen-fibril surface using a scanning electron microscope (SEM) were done. The protein solubility of VTC, ATC, and APTC were 0.44 ± 0.03, 0.52 ± 0.07, and 0.67 ± 0.12 mg protein/mg collagen. The solubility of collagen decreased with increasing of NaCl content. These three collagens were good solubility at low pH with the highest solubility at pH 5. The FTIR spectrum showed absorbance of Amide A, Amide B, Amide I, Amide II, and Amide III groups as 3286-3293 cm^-1, 2853-2922 cm^-1, 1634-1646 cm^-1, 1543-1544 cm^-1, and 1236-1237 cm^-1, respectively. The SEM analysis indicated a microstructure of collagen surface as folding of fibril with small pore.

Keywords: Katsuwonus pelamis; collagen; collagen properties; tuna-tail tendon.

Grants and funding

This research was funded by Kasetsart University Research and Development Institute (KURDI), FF(KU)7.65 under the research program “Development of functional ingredients from by-products of canned tuna processing”.