Purification and characterization of immunomodulatory peptides from enzymatic hydrolysates of duck egg ovalbumin

2021 ◽  
Author(s):  
Ping He ◽  
Qian Wang ◽  
Qiping Zhan ◽  
Leiman Pan ◽  
Xuan Xin ◽  
...  
Keyword(s):  
Egg White ◽  
Purification And Characterization ◽  
Enzymatic Hydrolysates ◽  
Duck Egg ◽  
Immunomodulatory Peptides

Duck egg white (DEW) is considered as an abandoned protein resource.

scholarly journals Purification and characterization of cystatin from duck egg white.

1995 ◽  
Vol 42 (3) ◽  
pp. 351-356 ◽  
Author(s):  
M Warwas ◽  
J Gburek ◽  
J Osada ◽  
K Gołab
Keyword(s):  
Egg White ◽  
Amino Acid Sequences ◽  
Size Exclusion ◽  
Molecular Forms ◽  
Sds Page ◽  
Peptidase Inhibitor ◽  
Size Exclusion Hplc ◽  
Duck Egg ◽  
Chicken Cystatin

It is the second peptidase inhibitor, after ovostatin, which showing the same antipapain activity in egg white in different avian species implies differences in amino-acid sequences. Cystatin from duck egg white was purified by carboxymethylpapain affinity chromatography and size-exclusion HPLC. The purified inhibitor which showed partial identity in the immunodiffusion test with chicken egg white cystatin, had an apparent molecular mass of 9.3 kDa as determined by SDS/PAGE. IEF analysis revealed five molecular forms of pI in the range 7.8-8.4. The obtained cystatin was neither glycosylated nor phosphorylated as it is in the case of chicken cystatin. The determined Ki (0.005 +/- 0.001 nM) was similar to that reported for human and chicken cystatin C.

scholarly journals ISOLATION AND CHARACTERIZATION OF DUCK EGG WHITE OVOMUCIN

2018 ◽  
Vol 45 (5) ◽  
pp. 1721-1728
Author(s):  
Hala Abd Elgalil ◽  
A. Osman ◽  
A. Abo Eita ◽  
S. El Saadany
Keyword(s):  
Egg White ◽  
Isolation And Characterization ◽  
Duck Egg

scholarly journals Purification and Characterization of Avian β-Defensin 11, an Antimicrobial Peptide of the Hen Egg

2010 ◽  
Vol 54 (10) ◽  
pp. 4401-4409 ◽  
Author(s):  
Virginie Hervé-Grépinet ◽  
Sophie Réhault-Godbert ◽  
Valérie Labas ◽  
Thierry Magallon ◽  
Chrystelle Derache ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Disulfide Bonds ◽  
Egg White ◽  
Gram Negative Bacteria ◽  
Purification And Characterization ◽  
Natural Antimicrobial ◽  
Reverse Phase ◽  
Purification Scheme ◽  
Hen Egg

ABSTRACTNatural antimicrobial peptides are present in different compartments (eggshell, egg white, and vitelline membranes) of the hen egg and are expected to be involved in the protection of the embryo during its development and to contribute to the production of pathogen-free eggs. In the present study, we used vitelline membranes from hen (Gallus gallus) eggs as a source of avian β-defensin 11 (AvBD11). A purification scheme using affinity chromatography and reverse-phase chromatography was developed. Purified AvBD11 was analyzed by a combination of mass spectrometry approaches to characterize its primary sequence and structure. A monoisotopic molecular species at [M + H]+of 9,271.56 Da was obtained, and its N- and C-terminal sequences were determined. We also examined posttranslational modifications and identified the presence of 6 internal disulfide bonds. AvBD11 was found to exhibit antimicrobial activity toward both Gram-positive and Gram-negative bacteria.

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