Preparation of egg white liquid hydrolysate (ELH) and its radical-scavenging activity

Dong Ouk Noh, Hyung Joo Suh

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

In the present study, an optimum protease was selected to hydrolyze the egg white liquid protein for the antioxidant peptides. Alcalase treatment yielded the highest amount of α-amino groups (15.27 mg/mL), while the control (no enzymatic hydrolysis) showed the lowest amount of α-amino groups (1.53 mg/mL). Alcalase also gave the highest degree of hydrolysis (DH) value (43.2%) and was more efficient for egg white liquid hydrolysis than the other enzymes. The Alcalase hydrolysate had the highest radical-scavenging activity (82.5%) at a concentration of 5.0 mg/mL. The conditions for enzymatic hydrolysis of egg white liquid with Alcalase were selected as substrate: water ratio of 2:1. Five percent Alacalse treatment did not show significant (P>0.05) increases of DH and α-amino nitrogen content after 24 hhydrolysis. Thirty two hour-hydrolysis with 5% Alcalase is sufficient to make antioxidative egg white liquid hydrolysate from egg white liquid. DPPH and ABTS radical-scavenging activities were significantly (P

Original languageEnglish
Pages (from-to)183-189
Number of pages7
JournalPreventive Nutrition and Food Science
Volume20
Issue number3
DOIs
Publication statusPublished - 2015 Sep 1

Fingerprint

Egg White
subtilisin
Subtilisins
egg albumen
hydrolysates
Hydrolysis
hydrolysis
liquids
enzymatic hydrolysis
amino nitrogen
Egg Proteins
nitrogen content
proteinases
peptides
Peptide Hydrolases
Nitrogen
antioxidants
Antioxidants
Peptides
enzymes

Keywords

  • Alcalase
  • Egg-white liquid
  • Hydrolysate
  • Radical scavenger

ASJC Scopus subject areas

  • Food Science
  • Nutrition and Dietetics

Cite this

Preparation of egg white liquid hydrolysate (ELH) and its radical-scavenging activity. / Noh, Dong Ouk; Suh, Hyung Joo.

In: Preventive Nutrition and Food Science, Vol. 20, No. 3, 01.09.2015, p. 183-189.

Research output: Contribution to journalArticle

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