Functionality of egg yolk lecithin and protein and functionality enhancement of protein by controlled enzymatic hydrolysis

2007 ◽  
Author(s):  
Guang Wang
2019 ◽  
Vol 97 ◽  
pp. 105224 ◽  
Author(s):  
Yang Gao ◽  
Junhua Li ◽  
Cuihua Chang ◽  
Chenying Wang ◽  
Yanjun Yang ◽  
...  

1972 ◽  
Vol 55 (5) ◽  
pp. 975-978
Author(s):  
J G Navarro ◽  
F Borie ◽  
J Saavedra

Abstract A residual lipid which is not removed by solvent extraction was detected and determined after enzymatic hydrolysis of defatted egg yolk protein. Free fatty acids were found to be the type of lipid bonded to the egg yolk protein. The mode of attachment of these fatty acids to the egg yolk protein is suggested and the composition of the fatty acids is reported.


LWT ◽  
2019 ◽  
Vol 110 ◽  
pp. 214-222 ◽  
Author(s):  
Shitao Tang ◽  
Xin Zhou ◽  
Mostafa Gouda ◽  
Zhaoxia Cai ◽  
Yongguo Jin

LWT ◽  
2021 ◽  
pp. 112075
Author(s):  
Luping Gu ◽  
Han Jiao ◽  
David Julian McClements ◽  
Mengyao Ji ◽  
Junhua Li ◽  
...  

1968 ◽  
Vol 19 (03/04) ◽  
pp. 383-388 ◽  
Author(s):  
R Losito ◽  
C. A Owen ◽  
E. V Flock ◽  

SummaryThe metabolism of vitamin K1- 14C and menadione-14C (vitamin K3-14C) was studied in normal and hepateetomized rats. After the administration of menadione, about 70% of the 14C was excreted in the urine in 24 hrs in both types of rats. Two urinary metabolites were identified by enzymatic hydrolysis: one a glucuronide and the other a sulfate of reduced menadione. Thus, the liver is not necessary for the metabolism of menadione. In the vitamin K1 studies, the intact rats excreted only 10% of the 14C and the hepatectomized rats excreted less than 0.5%. The retention of vitamin K1 may explain its superiority over menadione as an antidote for overdosages of oral anticoagulants.


Sign in / Sign up

Export Citation Format

Share Document