EFFICIENCY OF PRE-INCUBATIVE PROCESSING OF EGGS WITH EGG PROTEIN SOLUTION

Author(s):  
A.A. LINNIK ◽  
◽  
S.A. ALEKSEYEVА ◽  
O.Y. KUZNETSOV ◽  
◽  
...  
Keyword(s):  
2020 ◽  
Vol 14 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Dan Tian ◽  
Dan-Ni Yu ◽  
Yi-Ming Xu ◽  
Xu-Yin Ding ◽  
Zhou-Yu Zhang ◽  
...  

Background: Though there are many patents on silk, patents on sea silk are rare. Sea silk is one of the most coveted materials in the world, and the technology to make sea silk is at an extremely high risk of extinction. Unlike spider dragline silk and silkworm silk, this natural silk has been forgotten in the academic commune for millennia, though it has many fascinating properties: high strength, remarkable adhesion, extreme lightweight, and others. Method: Here we report that mussel-derived silk fibers can be fabricated by electrospinning. Instead of extracting proteins from byssus, we directly use the protein solution from alive blue mussels, which are intensely commercially used. The protein solution and the polyvinyl alcohol solution are mixed together to produce mussel-based silk fibers. Results: The mussel-based silk fibers have many special properties like high mechanical strength, remarkable super-contraction and good wetting properties. Conclusion: The electrospinning mussel-based silk fibers have the potential for use as a replacement for the rarest sea silk and as a new bio-inspired material with multi-functions.


Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.


Antibodies ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 21
Author(s):  
Alexandre Ambrogelly

The color of a therapeutic monoclonal antibody solution is a critical quality attribute. Consistency of color is typically assessed at time of release and during stability studies against preset criteria for late stage clinical and commercial products. A therapeutic protein solution’s color may be determined by visual inspection or by more quantitative methods as per the different geographical area compendia. The nature and intensity of the color of a therapeutic protein solution is typically determined relative to calibrated standards. This review covers the analytical methodologies used for determining the color of a protein solution and presents an overview of protein variants and impurities known to contribute to colored recombinant therapeutic protein solutions.


2021 ◽  
Vol 116 ◽  
pp. 106632
Author(s):  
Catherine Russell ◽  
Aikaterini A. Zompra ◽  
Georgios A. Spyroulias ◽  
Karina Salek ◽  
Stephen R. Euston

Author(s):  
Ana Carolina Fradique de Lyra ◽  
Amanda L. dos Santos Silva ◽  
Elane Cristina L. dos Santos ◽  
Ana Maria Queijeiro López ◽  
Júlio Cosme S. da Silva ◽  
...  

2013 ◽  
Vol 41 (5) ◽  
pp. 320-336 ◽  
Author(s):  
A. Martorell ◽  
E. Alonso ◽  
J. Boné ◽  
L. Echeverría ◽  
M.C. López ◽  
...  
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