Enzymatic hydrolysis and extensive heat treatment induce distinct modifications of cow's and camel milk proteins of relevance for production of infant formula

TY - JOUR

T1 - Enzymatic hydrolysis and extensive heat treatment induce distinct modifications of cow's and camel milk proteins of relevance for production of infant formula

AU - Maryniak, Natalia Z.

AU - Sancho, Ana I.

AU - Nielsen, Søren Drud-Heydary

AU - Larsen, Lotte Bach

AU - Gao, Yumei

AU - Bøgh, Katrine L.

AU - Hansen, Egon Bech

PY - 2024/1/1

Y1 - 2024/1/1

N2 - Camel milk is an alternative to cow's milk as protein source for infant formula. Reduced allergenicity is usually obtained through enzymatic hydrolysis of milk proteins. Heat treatment is another route to modify allergenicity. This study investigated the effect of enzyme hydrolysis and extensive heat treatment on the size, aggregation mechanisms, and modifications of camel milk proteins in comparison to the effect on cow's milk proteins. Disulphide bonds stabilized casein micelles in cow's milk but not in camel milk. The formation of large stable complexes by extensive heat treatment was prominent in cow's milk and not in camel milk. In both milks heat treatment led to equal levels of Maillard reaction, whereas sugar independent cross-linking was less pronounced in camel milk. Low sequence identity, different relative composition, and complete absence of β-lactoglobulin in camel milk are likely explanations for the different properties of cow's and camel milk. Production of infant formula based on camel milk should accordingly employ process parameters specifically adapted to this type of milk.

AB - Camel milk is an alternative to cow's milk as protein source for infant formula. Reduced allergenicity is usually obtained through enzymatic hydrolysis of milk proteins. Heat treatment is another route to modify allergenicity. This study investigated the effect of enzyme hydrolysis and extensive heat treatment on the size, aggregation mechanisms, and modifications of camel milk proteins in comparison to the effect on cow's milk proteins. Disulphide bonds stabilized casein micelles in cow's milk but not in camel milk. The formation of large stable complexes by extensive heat treatment was prominent in cow's milk and not in camel milk. In both milks heat treatment led to equal levels of Maillard reaction, whereas sugar independent cross-linking was less pronounced in camel milk. Low sequence identity, different relative composition, and complete absence of β-lactoglobulin in camel milk are likely explanations for the different properties of cow's and camel milk. Production of infant formula based on camel milk should accordingly employ process parameters specifically adapted to this type of milk.

KW - Alcalase

KW - Camel milk peptides

KW - Maillard reaction

KW - Trypsin

UR - http://www.scopus.com/inward/record.url?scp=85178654598&partnerID=8YFLogxK

U2 - 10.1016/j.lwt.2023.115591

DO - 10.1016/j.lwt.2023.115591

M3 - Journal article

SN - 1096-1127

VL - 191

JO - LWT - Food Science and Technology

JF - LWT - Food Science and Technology

M1 - 115591

ER -