Rennet induced gelation of reconstituted milk protein concentrates: The role of calcium and soluble proteins during reconstitution

2013 ◽  
Vol 29 (2) ◽  
pp. 68-74 ◽  
Author(s):  
S. Sandra ◽  
M. Corredig
2020 ◽  
Vol 52 (11) ◽  
pp. 1191-1201
Author(s):  
Ling Chen ◽  
Rongfu Tian ◽  
Huilin Zhang ◽  
Xiaolin Liu

Abstract NFκB1/p105 is the critical member of the NFκB family which can suppress inflammation, ageing, and cancer when p50/p50 homodimer is formed. Currently, the research about the role of NFκB1/p105 during cow mastitis is limited. Here, we analyzed the correlation of six single-nucleotide variants of the NFκB1 gene with somatic cell count, milk yield, milk fat content, and milk protein content in 547 Chinese Holstein cows, and explored the mRNA expression profiles of the NFκB family and ubiquitin ligases (βTrCP1, βTrCP2, KPC1, KPC2) in LPS-induced bovine mammary epithelial cells (MECs) by transcriptome-Seq. The association analysis showed that cows with SNV2-TT and SNV6-CC in the NFκB1 gene had significantly higher milk protein content (P < 0.05), while cows with SNV5-TT in the NFκB1 gene had significantly lower somatic cell score (SCS), but CC genotype at SNV5 locus was not detected in our Holstein cows. The transcriptome-Seq results demonstrated the mRNA expression of NFκB1 was increased and peaked at 4 h post-induction, while the mRNA expressions of both KPC1 and BCL3 that promote the anti-inflammation function of NFκB1/p105 were decreased in LPS-induced bovine MECs. TNFAIP3, an inhibitor of both degradation and processing of p105 precursor, was markedly increased by more than 3 folds. Furthermore, bta-miR-125b which targets at the 3ʹUTR of TNFAIP3 was reduced by 50%. These results indicated that SNV5-TT of the NFκB1 gene with lower SCS may be an anti-mastitis genotype that could cope with infection more efficiently in Chinese Holstein cows. In addition, the anti-inflammation role of NFκB1/p105 seemed to be inhibited in LPS-induced-bovine MECs because the formation of the p50/p50 homodimer was arrested. This study provides a new perspective to understand the inflammatory mechanism in dairy mastitis.


2018 ◽  
Vol 85 ◽  
pp. 299-310 ◽  
Author(s):  
An Thi-Binh Nguyen ◽  
Michaël Nigen ◽  
Luciana Jimenez ◽  
Hassina Ait-Abderahim ◽  
Charles Cunault ◽  
...  

2013 ◽  
Vol 711 ◽  
pp. 32-38
Author(s):  
Zdzisław Wiśniowski ◽  
Mateusz Banach ◽  
Irena Roterman

The possible mechanism protecting the organisms against the freezing is shown. The presence of highly soluble proteins with no specific interaction allows the organism surviving the temperature below zero Celsius degree. The role of hydrophobic core and its structure (recognized as accordant with the idealized one) appears to be critical for antifreeze function of protein. The possible application of the model for biotechnological preparation of compounds protecting the solutions against freezing is discussed.


2006 ◽  
Vol 84 (5) ◽  
pp. 1070-1079 ◽  
Author(s):  
Magali Lacroix ◽  
Cécile Bos ◽  
Joëlle Léonil ◽  
Gheorge Airinei ◽  
Catherine Luengo ◽  
...  

1989 ◽  
Vol 94 (3) ◽  
pp. 585-591
Author(s):  
A. Koffer ◽  
B.D. Gomperts

This study addresses the question of the role of cytoplasmic proteins in exocytosis from permeabilised rat mast cells. We have used two different methods of cell permeabilisation (ATP4- and streptolysin O) to regulate the size of the plasma membrane lesions, and thus to dictate the rate and extent of efflux of the cytosolic proteins, and compared the secretory response of the two preparations. We report evidence for the existence of two factors present in the cytosol, which affect the exocytotic mechanism in opposing manners. One of these is required for the maintenance of cell responsiveness; it is retained for more than 120 min by ATP4- -permeabilised cells but lost within 60 min from cells permeabilised by streptolysin O. The other factor, which leaks immediately from cells treated from streptolysin O, but only gradually from cells treated with ATP4-, has the effect of suppressing the affinity for both Ca2+ and guanine nucleotide in the exocytotic reaction.


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