An Improved Production Method of Bioactive Peptides from Sturgeon Fish Cartilage

Abstract

This study aims to develop an extraction and purification method for production of type II collagen and its bioactive peptides from sturgeon fish cartilage. Initially, freeze-dried sturgeon fish cartilage was powdered for extraction of pepsin soluble collagen (PSC) using 0.5 M acetic acid and 10% pepsin with a PSC yield of 34.59%. Optimization of PSC hydrolysis revealed that a high hydrolysis degree (34.23%) was obtained using an enzyme combination of 4.5% alcalase plus 4.5% flavourzyme, PSC to water ratio at 1:30 (w/v), pH at 8, temperature at 50 °C and hydrolysis time at 6 h to obtain sturgeon cartilage collagen peptide (SCCP). Both PSC and SCCP were characterized for collagen type and molecular weight (MW) range by SDS-PAGE, amino acid composition by HPLC-DAD, MW distribution by MALDI-TOF-MS, functional group by FTIR and absorption spectra by UV analysis confirming the presence of type II collagen in sturgeon fish cartilage with amino acids including glycine, glutamic acid, hydroxyproline, proline and alanine dominating in both PSC and SCCP. Furthermore, the SCCP possessed < 500 Da MW distribution accounting for 89.71% of the total signal, with a peptide fragment at MW 344.721 Da being present in the highest proportion.