Amino acid profile of collagen fractions extracted from by-products of Ophistonema libertate and Scomber japonicus

Abstract

The objective of this study was to identify the amino acid profile (AAp) of collagen extracted from Ophistonema libertate and Scomber japonicus head:tail homogenates. Salt (SSC)-, acid (ASC)-, and pepsin (PSC)-soluble collagens and insoluble collagen (IC) were extracted by solubility. The homogenates of both species exhibited high concentrations of proline, aspartic acid, glutamic acid, arginine, histidine, and hydroxyproline. Higher concentrations of aspartic acid and lysine were registered in S. japonicus SSC compared with O. libertate. S. japonicus PSC showed significantly higher concentrations for most of the amino acids (AAs) evaluated compared with O. libertate, including aspartic acid, glutamic acid, serine, glycine, alanine, tyrosine, proline, hydroxyproline, arginine, threonine, methionine, valine, phenylalanine, isoleucine, leucine, lysine, and histidine. Hydroxyproline showed no significant differences among both species homogenates; however, O. libertate IC was higher than S. japonicus IC. Differences detected in the AAp of both species could suggest different properties of the collagen extracted.