hen egg
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2021 ◽  
pp. 107450
Author(s):  
Arne M.R. Huyst ◽  
Lomme J. Deleu ◽  
Trui Luyckx ◽  
Dieter Buyst ◽  
John Van Camp ◽  
...  

Author(s):  
Joao Ramos ◽  
Valerie Laux ◽  
Michael Haertlein ◽  
V. Trevor Forsyth ◽  
Estelle Mossou ◽  
...  

The biological function of a protein is intimately related to its structure and dynamics, which in turn are determined by the way in which it has been folded. In vitro refolding is commonly used for the recovery of recombinant proteins that are expressed in the form of inclusion bodies and is of central interest in terms of the folding pathways that occur in vivo. Here, biophysical data are reported for in vitro-refolded hydrogenated hen egg-white lysozyme, in combination with atomic resolution X-ray diffraction analyses, which allowed detailed comparisons with native hydrogenated and refolded perdeuterated lysozyme. Distinct folding modes are observed for the hydrogenated and perdeuterated refolded variants, which are determined by conformational changes to the backbone structure of the Lys97–Gly104 flexible loop. Surprisingly, the structure of the refolded perdeuterated protein is closer to that of native lysozyme than that of the refolded hydrogenated protein. These structural differences suggest that the observed decreases in thermal stability and enzymatic activity in the refolded perdeuterated and hydrogenated proteins are consequences of the macromolecular deuteration effect and of distinct folding dynamics, respectively. These results are discussed in the context of both in vitro and in vivo folding, as well as of lysozyme amyloidogenesis.


2021 ◽  
Vol 18 (117) ◽  
pp. 1-12
Author(s):  
Seyedeh Arefeh Hosseini ◽  
ahmad banakar ◽  
Saeid Minaei ◽  
Saman Abdanan Mehdizadeh

Author(s):  
Jarosław Wawer ◽  
Emilia Kaczkowska ◽  
Jakub Karczewski ◽  
Danuta Augustin-Nowacka ◽  
Joanna Krakowiak

2021 ◽  
Vol 18 (2) ◽  
pp. 93
Author(s):  
Maulida Hayuningtyas ◽  
Christina Winarti ◽  
Sari Intan Kailaku ◽  
Hoerudin Hoerudin

<p>Hen egg is the most consumed animal food due to its high nutritional content, affordable and easy to obtain. However, eggs have the disadvantage for their short shelf life of about 7 days at room temperature. An effort to extend the shelf life of eggs including storing at low temperatures and/or coating. The research objective was to determine changes in the physical quality and morphology of chicken eggs coated with two material coating stored at room (25–29 °C) and AC/low (18–22 °C) temperature. The treatments tested were two kinds of coatings, namely gelatin and lime solution, and two storage temperature conditions, namely room and low temperature for 30 days. The study was conducted with three replications, each replication was observed on 5 eggs. The parameters observed were weight loss, Egg white index, Egg yolk index, air cavity, Haugh Unit and surface morphology. The results showed that at the end of storage for 30 days the eggs quality still met the SNI standards I to III. AC storage temperature was better than room temperature. The egg treated with coating produced better quality than without coating. The longer the storage, the lower the weight loss, HU, IPT and IKT. The best treatment was gelatin coating stored at AC temperature.</p>


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