Whey protein fractionation: Isoelectric precipitation of α-lactalbumin under gentle heat treatment

1997 ◽  
Vol 56 (4) ◽  
pp. 391-397 ◽  
Author(s):  
C. Bramaud ◽  
P. Aimar ◽  
G. Daufin
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Protein Fractionation ◽  
Isoelectric Precipitation

scholarly journals The effect of direct and indirect heat treatment on the attributes of whey protein beverages

2018 ◽  
Vol 85 ◽  
pp. 144-152 ◽  
Author(s):  
Clodagh M. Kelleher ◽  
James A. O'Mahony ◽  
Alan L. Kelly ◽  
Donal J. O'Callaghan ◽  
Kieran N. Kilcawley ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Whey Protein

Gelation of casein-whey mixtures: effects of heating whey proteins alone or in the presence of casein micelles

2001 ◽  
Vol 68 (3) ◽  
pp. 471-481 ◽  
Author(s):  
CATHERINE SCHORSCH ◽  
DEBORAH K. WILKINS ◽  
MALCOLM G. JONES ◽  
IAN T. NORTON
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Protein Denaturation ◽  
Whey Proteins ◽  
Treatment Sequence ◽  
Gel Properties ◽  
Casein Micelles ◽  
Gelation Kinetics ◽  
Milk Gelation

The aim of the present work was to investigate the role of whey protein denaturation on the acid induced gelation of casein. This was studied by determining the effect of whey protein denaturation both in the presence and absence of casein micelles. The study showed that milk gelation kinetics and gel properties are greatly influenced by the heat treatment sequence. When the whey proteins are denatured separately and subsequently added to casein micelles, acid-induced gelation occurs more rapidly and leads to gels with a more particulated microstructure than gels made from co-heated systems. The gels resulting from heat-treatment of a mixture of pre-denatured whey protein with casein micelles are heterogeneous in nature due to particulates formed from casein micelles which are complexed with denatured whey proteins and also from separate whey protein aggregates. Whey proteins thus offer an opportunity not only to control casein gelation but also to control the level of syneresis, which can occur.

Separation of bovine κ-casein glycomacropeptide from sweet whey protein products with undetectable level of phenylalanine by protein precipitation followed by anion exchange chromatography

2018 ◽  
Vol 85 (1) ◽  
pp. 110-113 ◽  
Author(s):  
Takuo Nakano ◽  
Lech Ozimek ◽  
Mirko Betti
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Whey Protein ◽  
Anion Exchange ◽  
Large Scale ◽  
Dry Weight ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Shift ◽  
Sweet Whey

Bovine κ-casein glycomacropeptide (GMP) found in sweet whey is a 64 amino acid residue glycopeptide, which does not contain phenylalanine or other aromatic amino acids. There is, however, little information available concerning isolation of phenylalanine free GMP from sweet whey. In the study reported in this Research Communication, GMP was purified from three samples of sweet whey protein products (SWPP) by a procedure involving: (1) precipitation of protein by heat treatment; (2) precipitation of protein by pH shift to 4·6; and (3) diethylaminoethyl (DEAE)-Sephacel anion exchange chromatography of soluble portion of each sample obtained after removal of protein precipitates. The total protein precipitated with both heat treatment and pH shift accounted for average 61% of dry weight of SWPP. The GMP fraction obtained by DEAE-Sephacel chromatography accounted for average 7·5% of dry weight of SWPP. Amino acid analysis showed that there was no detectable level of phenylalanine in GMP fractions from all samples examined. The present method may help develop large scale methods of production of GMP.

scholarly journals The effect of heat treatment on the microstructure and functional properties of whey protein from goat milk

2020 ◽  
Vol 103 (2) ◽  
pp. 1289-1302 ◽  
Author(s):  
Xuan Zhao ◽  
Ming Cheng ◽  
Xuexi Zhang ◽  
Xiangying Li ◽  
Di Chen ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Functional Properties ◽  
Goat Milk
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