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Compositions, Protease Inhibitor and Gelling Property of Duck Egg Albumen as Affected by Salting
Korean J. Food Sci. An. 2018;38:14-25
Published online February 28, 2018
© 2018 Korean Society for Food Science of Animal Resources

Tran Hong Quan and Soottawat Benjakul*

Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand
Correspondence to: Soottawat Benjakul
Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand
Tel: +66-7428-6334
Fax: +66-7455-8866
E-mail: soottawat.b@psu.ac.th
Received September 20, 2017; Revised November 19, 2017; Accepted November 25, 2017.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
Chemical compositions, trypsin inhibitory activity, and gelling properties of albumen from duck egg during salting of 30 days were studied. As the salting time increased, moisture content decreased, the salt content and surface hydrophobicity increased (p<0.05). Trypsin inhibitory activity and specific activity were continuously decreased throughout the salting time of 30 days (p<0.05). This coincided with the decrease in band intensity of inhibitor with molecular weight of 44 kDa as examined by inhibitory activity staining. Nevertheless, no differences in protein patterns were observed in albumen during the salting of 30 days. Based on texture profile analysis, hardness, springiness, gumminess, chewiness, and resilience of albumen gel decreased with increasing salting time. Conversely, salted albumen gels exhibited higher cohesiveness and adhesiveness, compared to those of fresh albumen. Scanning electron microscopic study revealed that gel of salted albumen showed the larger voids and less compactness. In general, salting lowered trypsin inhibitory activity and gelling property of albumen from duck egg to some extent. Nevertheless, the salted albumen with the remaining inhibitor could be an alternative additive for surimi or other meat products to prevent proteolysis.
Keywords : albumen, duck egg, gelling property, inhibitory activity, salting, trypsin inhibitor


June 2018, 38 (3)