Identification of Egg White Proteins and Divergence in the Regulatory Region of the Ovalbumin Gene in Avians

2016 ◽  
Vol 24 (1) ◽  
pp. 12-25 ◽  
Author(s):  
Jindong Ren ◽  
Jianhong Hu ◽  
Li Chen ◽  
Yali Liu ◽  
Xiaoqin Xu ◽  
...  
1950 ◽  
Vol 184 (1) ◽  
pp. 377-383 ◽  
Author(s):  
Richard H. Forsythe ◽  
Joseph F. Foster
Keyword(s):  

1986 ◽  
Vol 35 (3) ◽  
pp. 657-666 ◽  
Author(s):  
J. F. Pageaux ◽  
C. Laugier ◽  
D. Pal ◽  
M. A. D’Almeida ◽  
D. Sandoz ◽  
...  

2004 ◽  
Vol 55 (8) ◽  
pp. 635-640 ◽  
Author(s):  
Kenji Yoshino ◽  
Kentaro Sakai ◽  
Yoko Mizuha ◽  
Ayako Shimizuike ◽  
Shigeru Yamamoto

2015 ◽  
Vol 1095 ◽  
pp. 287-290 ◽  
Author(s):  
Wei Xu ◽  
Hai Bin Wang ◽  
Tao Xiang

Gelling properties stability of the Maillard-type and dry-heating egg white proteins (MEW and DEW) were investigated. MEW were prepared by storing sugar-preserved egg white proteins and glucose at 60 °C and 79% relative humidity for 2 days, and DEW were prepared by storing at 80°C in dry state (7.5% moisture content) for 7 days. The results showed that both MEW and DEW have excellent gelling properties. After storage at room temperature for 180 days, gel hardness, spring and cohesiveness of MEW increased by 1.92%, 1.89% and 4.24% respectively, water holding capacity of MEW gel decreased by 1.42%, while storage time had a considerable effect on those of DEW gels. A tight and more uniform network with constant stability in the course of storage was observed in the gel of MEW (500×), while gaps in EWP gel network were larger and the gel texture became looser with storage time. The results demonstrated that gelling properties stability of MEW is better than DEW.


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