The carbohydrate portions of milk glycoproteins

1979 ◽  
Vol 46 (2) ◽  
pp. 187-191 ◽  
Author(s):  
Pierre Jollès

SUMMARYk-Casein is the main glycoprotein of cow's milk. Its polysaccharide part is O-glycosidically linked to threonine residue 133. It contains only 3 different sugars (Gal, GalNAc, NeuNAc), but a microheterogeneity has been detected at the sugar level. Two main polysaccharides have so far been characterized. The structure of the trisaccharide is NeuNAc α → 3 Gal β1 →3 GalNAc; the tetrasaccharide contains one additional sialic acid. The polysaccharide part of ovine k-casein resembles that of bovine k-casein, but contains also N-glycolyl neuraminic acid. Human k-casein contains 3 times more carbohydrate than bovine k-casein with 2 additional sugars, GlcNAc and Fuc. The various polysaccharide parts isolated from bovine colostrum k-caseinoglycopeptide are much more complex than those obtained from the normal glycopeptide, indicating an evolution of the sugar part as a function of time after parturition. Some aspects of the secondary structure of k-casein and the role of the sugar part are discussed. The carbohydrate moiety of another milk protein, human lactotransferrin, is also discussed briefly. It is comprised of 2 identical glycan groups, N-glycosidically linked to the protein, and quite different from the k-casein carbohydrate moiety.

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 138
Author(s):  
Jin Wang ◽  
Rachit Saxena ◽  
Sai Kranthi Vanga ◽  
Vijaya Raghavan

Cow’s milk is considered an excellent protein source. However, the digestibility of milk proteins needs to be improved. This study aimed to evaluate the relationship between the functional properties of milk proteins and their structure upon microwave, ultrasound, and thermosonication treatments. The protein content, digestibility, and secondary-structure changes of milk proteins were determined. The results demonstrated that almost 35% of the proteins in the untreated samples had a α-helix structure and approximately 29% a β-sheet and turns structure. Regarding the untreated samples, the three treatments increased the α-helices and correspondingly decreased the β-sheets and turns. Moreover, the highest milk protein digestibility was observed for the ultrasound-treated samples (90.20–94.41%), followed by the microwave-treated samples (72.56–93.4%), whereas thermosonication resulted in a lower digestibility (68.76–78.81%). The milk protein content was reduced as the microwave processing time and the temperature increased. The final milk protein available in the sample was lower when microwave processing was conducted at 75 °C and 90 °C compared to 60 °C, whereas the ultrasound treatment significantly improved the protein content, and no particular trend was observed for the thermosonicated samples. Thus, ultrasound processing shows a potential application in improving the protein quality of cow’s milk.


2021 ◽  
Vol 230 ◽  
pp. 266-269
Author(s):  
Mitsuyoshi Urashima ◽  
Hiroshi Tachimoto

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