A comprehensive review on the composition and properties of buffalo milk

Abstract

International audienc

Physicochemical properties of Butter cheese from Marajó manufactured with buffalo milk and cow milk

“…As expected, cheese produced with 100% of buffalo milk had a higher value for luminosity (white component), differing only in B 60 . In the same way, formulation B 100 reached higher values of the chromaticity component of green color, caused by the presence of the blue-green pigment (biliverdin), which is present in buffalo milk and absent in cow milk [3]. However, the presence of β-carotene pigment in cow milk caused an increase in the yellow chromaticity component in formulations produced with this type of milk [3].…”

“…However, the mixture of those milks may bring alterations in physicochemical characteristics, texture and color parameters, caused by bovine milk composition that has a lower amount of fat, lactose, protein, ashes, Ca and A and C vitamins, and higher concentration of β-carotene, absent in buffalo milk [3] [4]. Buffalo milk has higher levels of fat with a minimum and maximum of 6.6 g 100 g -1 and 8.8 g 100 g -1 , while cow milk average is 3.3 g 100 g -1 [5].…”

Proteolysis and antioxidant activity of peptic, tryptic and chymotryptic hydrolysates of cow, buffalo, goat and camel caseins

“…Compared to cow's casein, buffalo casein showed slightly slower hydrolysis with all enzymes, but the differences were found to be statistically insignificant ( P < 0.05). This can be explained by the high homology (>95%) between the casein fractions from cow and buffalo milk (Abd El‐Salam and El‐Shibiny ). Trypsin specifically hydrolyses peptide bonds where basic amino acids (Lys, Arg) are involved.…”

Iron (II)-chelating activity of buffalo αS-casein hydrolysed by corolase PP, alcalase and flavourzyme

“…Similarly buffalo α S2 -casein is also a single polypeptide chain of 207 amino acid residues and has very high homology (97.9 %) compared with bovine α S2 -casein (Sukla et al 2007;D'Ambrosio et al 2008). Only 10 substitutions at His 2 -Asn, His 29 -Asn, Ile 44 -Val, Ile 147 -Phe, Asp 157 -Glu, His 170 -Arg, Thr 175 -Ala, Try 176 -Leu, Tyr 182 -His and Asn 199 -Lys have been reported between buffalo and bovine α S2 -casein (El-Salam and El-Shibiny 2011;D'Ambrosio et al 2008). But there is no difference in phosphorylation between buffalo and bovine α S2 -casein.…”