Comprehensive characterization of bioactive peptides from Buffalo ( Bubalus bubalis ) colostrum and milk fat globule membrane proteins

2017 ◽  
Vol 97 ◽  
pp. 95-103 ◽  
Author(s):  
N. Brijesha ◽  
H.S. Aparna
2010 ◽  
Vol 90 (5) ◽  
pp. 601-609 ◽  
Author(s):  
Shenghua He ◽  
Ying Ma ◽  
Jiaqi Wang ◽  
Qiming Li ◽  
Shanhu Tang ◽  
...  

2020 ◽  
Vol 86 ◽  
pp. 103386 ◽  
Author(s):  
María Visitación Calvo ◽  
María Carmen Martín-Hernández ◽  
Alba García-Serrano ◽  
María Pilar Castro-Gómez ◽  
Loreto Alonso-Miravalles ◽  
...  

1994 ◽  
Vol 1199 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Naohito Aoki ◽  
Hidenori Kuroda ◽  
Miho Urabe ◽  
Yoshimi Taniguchi ◽  
Takahiro Adachi ◽  
...  

2002 ◽  
Vol 69 (4) ◽  
pp. 555-567 ◽  
Author(s):  
SUNG JE LEE ◽  
JOHN W. SHERBON

The effects of heat treatment and homogenization of whole milk on chemical changes in the milk fat globule membrane (MFGM) were investigated. Heating at 80 °C for 3–18 min caused an incorporation of whey proteins, especially β-lactoglobulin (β-lg), into MFGM, thus increasing the protein content of the membrane and decreasing the lipid. SDS-PAGE showed that membrane glycoproteins, such as PAS-6 and PAS-7, had disappeared or were weakly stained in the gel due to heating of the milk. Heating also decreased free sulphydryl (SH) groups in the MFGM and increased disulphide (SS) groups, suggesting that incorporation of β-lg might be due to association with membrane proteins via disulphide bonds. In contrast, homogenization caused an adsorption of caseins to the MFGM but no binding of whey proteins to the MFGM without heating. Binding of caseins and whey proteins and loss of membrane proteins were not significantly different between milk samples that were homogenized before and after heating. Viscosity of whole milk was increased when milk was treated with both homogenization and heating.


1978 ◽  
Vol 171 (3) ◽  
pp. 549-557 ◽  
Author(s):  
G H Farrar ◽  
R Harrison

Treatment of sialoglycopeptides derived from bovine milk-fat-globule membrane with alkaline borohydride released a reduced oligosaccharide fraction from which a tetrasaccharide and two trisaccharides were isolated. Periodate-oxidation studies coupled with methylation analysis and g.l.c.-mass spectrometry established their structures as: N-acetylneuraminyl-(2 leads to 3)-beta-D-galactopyranosyl-(1 leads to 3)-[N-acetylneuraminyl-(2 leads to 6)]-N-acetyl-D-galactosaminitol, N-acetylneuraminyl-(2 leads to 3)-D-glactopyranosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol and beta-D-galactopyranosyl-(1 leads to 3)-[N-acteylneuraminyl-(2 leads to 6)]-N-acetyl-D-galactosaminitol respectively.


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