Effects of protease-hydrolyzed egg white on the meringue batter properties and meringue textural and sensory properties during storage

Yükleniyor...
Küçük Resim

Tarih

2021

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

AZTI-Tecnalia

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

This study was focused to analyze the effects of different concentrations (0.5, 1.0, 1.5 w/v) of protease hydrolyzed liquid egg white (LEW) on meringues batter and cookies. The color (L*, a*, b*, ΔE), physical and aeration properties (batter specific density (BSD), cooked meringues specific volume (MSV)), water activity, texture analysis and sensorial profiles of the meringues during three months of extended storage at ambient temperature (23 ± 2°C) was investigated. Additionally, the creep recovery compliance parameters, colors, and physico-chemical characteristics of freshly whipped meringue batter were also evaluated. Protease hydrolyzed samples exhibited higher L* and lower b* parameter. The BSD values (g/cm3) for control - 0 % (0.51 ± 0.01) was significantly decreased (p < 0.05) after enzymatic treatment, lower values obtained in 1 % (0.37 ± 0.01) and 1.5 % (0.35 ± 0.01). The MSV values of cooked meringue was significantly increased (p < 0.05) depends on the protease concentrations. The strength of the meringue batter is increased after hydrolysis. However, the enzymatic hydrolysis reduced consumer satisfaction. This research points out the optimum (1.0 %) hydrolyzed LEW in preparation of meringue improved functionality, such as BSD and MSV parameters.

Açıklama

Anahtar Kelimeler

And storage stability, Liquid egg albumen, Meringue cookies, Organoleptic properties, Rheological behavior

Kaynak

International Journal of Gastronomy and Food Science

WoS Q Değeri

Q2

Scopus Q Değeri

Cilt

25

Sayı

Künye

Yüceer, M., & Caner, C. (2021). Effects of protease-hydrolyzed egg white on the meringue batter properties and meringue textural and sensory properties during storage. International Journal of Gastronomy and Food Science, 25, 100409. https://doi.org/10.1016/j.ijgfs.2021.100409