The Effect of Different pH Conditions on Peptides’ Separation from the Skipjack Dark Meat Hydrolysate Using Ceramic Ultrafiltration

Supitchaya Pinrattananon, Franck Courtes, Nattawan Chorhirankul, Panwajee Payongsri, Thunyarat Pongtharangkul, Anja E.M. Janssen, Nuttawee Niamsiri*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)

Abstract

The conversion of Skipjack (Katsuwonus pelamis) dark meat into a hydrolysate via enzymatic hydrolysis is a promising approach to increase the value of tuna by-products as a source of bioactive peptides. Skipjack dark meat hydrolysate (SDMH) contains various sizes and sequences of peptides. To obtain and concentrate the targeted small peptides from SDMH, ultrafiltration, a key unit operation process, was employed to fractionate the protein hydrolysate due to its simplicity and productivity. The objective of this study was to investigate the effect of the feed pH on the membrane performance based on the permeate flux and the transmission of peptides. The fractionation of SDMH was performed using a ceramic membrane (molecular weight cut-off of 1 kDa) with three different pH values (5, 7, and 9) at various transmembrane pressures (TMP) (2.85, 3.85, and 4.85 bar). A high permeate flux and transmission were obtained at pH 9 due to the repulsive interactions between peptides and the membrane surface, leading to the reduction in concentration polarization that could promote high transmission. In addition, the combination of low TMP (2.85 bar) and pH 9 helped to even minimize the fouling formation tendency, providing the highest peptide transmission in this study. The fractionation process resulted in the enhancement of small peptides (MW < 0.3 kDa). The amino acid profiles were different at each pH, affirming the charge effect from the pH changes. In conclusion, the performance of the membrane was affected by the pH of the hydrolysate. Additionally, the ultrafiltration method served as an alternate method of peptide separation on a commercial scale.
Original languageEnglish
Article number3367
JournalFoods
Volume12
Issue number18
DOIs
Publication statusPublished - 8 Sept 2023

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