Camel whey protein microparticles for safe and efficient delivery of novel camel milk derived probiotics

LWT ◽  
2019 ◽  
Vol 108 ◽  
pp. 81-88 ◽  
Author(s):  
Mudasir Ahmad ◽  
Priti Mudgil ◽  
Sajid Maqsood
2015 ◽  
Vol 44 ◽  
pp. 277-284 ◽  
Author(s):  
Jorien P.C.M. Peters ◽  
Hannemieke Luyten ◽  
Arno C. Alting ◽  
Remko M. Boom ◽  
Atze Jan van der Goot

2013 ◽  
Vol 51 (2) ◽  
pp. 872-878 ◽  
Author(s):  
Clarice Gebara ◽  
Karina S. Chaves ◽  
Maria Cecília E. Ribeiro ◽  
Flavia N. Souza ◽  
Carlos R.F. Grosso ◽  
...  

2019 ◽  
Vol 135 ◽  
pp. 855-863 ◽  
Author(s):  
R.G. Kumar Lekshmi ◽  
M. Rahima ◽  
N.S. Chatterjee ◽  
C.S. Tejpal ◽  
K.K. Anas ◽  
...  

2000 ◽  
Vol 78 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Jean-Michel Girardet ◽  
Franck Saulnier ◽  
Jean-Luc Gaillard ◽  
Jean-Paul Ramet ◽  
Gérard Humbert

The camel (camelus dromedarius) milk proteose peptone 3 (PP3) was purified successively by size exclusion fast protein liquid chromatography and reversed phase high performance liquid chromatography and then characterized by amino acid residue composition determination and chemical microsequencing after CNBr or trypsin cleavages. In comparison with the previously reported structure of camel milk whey protein, the camel PP3 contains an insertion in the N-terminal region which has approximately 24 residues, whereas the remaining C-terminal regions of these two homologous proteins are essentially identical. The camel PP3 seems to contain a potential O-glycosylation site localized in this insertion and 2 or 3 phosphorylated serine residues. PP3 belongs to the glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) family and could therefore play an immunological role in the camel or its suckling young.


2016 ◽  
Vol 54 ◽  
pp. 170-178 ◽  
Author(s):  
Jorien P.C.M. Peters ◽  
Frank J. Vergeldt ◽  
Henk Van As ◽  
Hannemieke Luyten ◽  
Remko M. Boom ◽  
...  

2017 ◽  
Vol 63 ◽  
pp. 533-544 ◽  
Author(s):  
Jorien P.C.M. Peters ◽  
Frank J. Vergeldt ◽  
Henk Van As ◽  
Hannemieke Luyten ◽  
Remko M. Boom ◽  
...  

2012 ◽  
Vol 79 (2) ◽  
pp. 185-191 ◽  
Author(s):  
Katharina Hinz ◽  
Paula M O'Connor ◽  
Thom Huppertz ◽  
R Paul Ross ◽  
Alan L Kelly

Proteomic analysis of bovine, caprine, buffalo, equine and camel milk highlighted significant interspecies differences. Camel milk was found to be devoid of β-lactoglobulin, whereas β-lactoglobulin was the major whey protein in bovine, buffalo, caprine, and equine milk. Five different isoforms of κ-casein were found in camel milk, analogous to the micro-heterogeneity observed for bovine κ-casein. Several spots observed in 2D-electrophoretograms of milk of all species could tentatively be identified as polypeptides arising from the enzymatic hydrolysis of caseins. The understanding gained from the proteomic comparison of these milks may be of relevance both in terms of identifying sources of hypoallergenic alternatives to bovine milk and detection of adulteration of milk samples and products.


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