scholarly journals Isolation and Purification of Bioactive Proteins from Bovine Colostrum

Author(s):  
Mianbin Wu ◽  
Xuewan Wang ◽  
Zhengyu Zhang ◽  
Rutao Wang
2020 ◽  
Vol 11 (3) ◽  
pp. 2309-2327
Author(s):  
Dereck E. W. Chatterton ◽  
Sasha Aagaard ◽  
Tim Hesselballe Hansen ◽  
Duc Ninh Nguyen ◽  
Cristian De Gobba ◽  
...  

Bioactive proteins in bovine colostrum are affected by the type of pasteurization and spray drying and if gamma irradiation is used to improve microbial safety during packaging. Selection of the correct conditions preserves these important proteins.


1969 ◽  
Vol 18 (10) ◽  
pp. 2303-2311 ◽  
Author(s):  
Keiko Yamazaki ◽  
Hiroshi Moriya

2022 ◽  
Vol 12 ◽  
Author(s):  
Merve Kaplan ◽  
Ayşenur Arslan ◽  
Hatice Duman ◽  
Melda Karyelioğlu ◽  
Barış Baydemir ◽  
...  

Colostrum contains all essential nutrients for the neonate during the first days of life, with impacts that continue far beyond these first days. Bovine colostrum has been used for human consumption due to the high concentrations of bioactive proteins, vitamins, minerals, growth factors, as well as free and conjugated oligosaccharides. Processes involved in the preparation of bovine colostrum for human consumption play a pivotal role in preserving and maintaining the activity of the bioactive molecules. As bovine colostrum is a multifunctional food that offers a myriad of benefits for human health, assessing the main processes used in preparing it with both advantages and disadvantages is a crucial point to discuss. We discuss major processes effects for colostrum production on the nutritional value, some advanced technologies to preserve processed bovine colostrum and the end-product forms consumed by humans whether as dairy products or dietary supplements.


Author(s):  
F. A. Durum ◽  
R. G. Goldman ◽  
T. J. Bolling ◽  
M. F. Miller

CMP-KDO synthetase (CKS) is an enzyme which plays a key role in the synthesis of LPS, an outer membrane component unique to gram negative bacteria. CKS activates KDO to CMP-KDO for incorporation into LPS. The enzyme is normally present in low concentrations (0.02% of total cell protein) which makes it difficult to perform large scale isolation and purification. Recently, the gene for CKS from E. coli was cloned and various recombinant DNA constructs overproducing CKS several thousandfold (unpublished data) were derived. Interestingly, no cytoplasmic inclusions of overproduced CKS were observed by EM (Fig. 1) which is in contrast to other reports of large proteinaceous inclusion bodies in various overproducing recombinant strains. The present immunocytochemical study was undertaken to localize CKS in these cells.Immune labeling conditions were first optimized using a previously described cell-free test system. Briefly, this involves soaking small blocks of polymerized bovine serum albumin in purified CKS antigen and subjecting them to various fixation, embedding and immunochemical conditions.


2001 ◽  
Vol 120 (5) ◽  
pp. A673-A674
Author(s):  
D MACK ◽  
M LARSON ◽  
S WEI ◽  
A WEBER ◽  
T MCDONALD

2010 ◽  
Vol 28 (4) ◽  
pp. 383-387 ◽  
Author(s):  
Aiyi PENG ◽  
Xuewei QU ◽  
Hui LI ◽  
Lu GAO ◽  
Bo YU ◽  
...  

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