Multilevel systems biology modeling characterized the atheroprotective efficiencies of modified dairy fats in a hamster model.

We assessed the atheroprotective efficiency of modified dairy fats in hyperlipidemic hamsters. A systems biology approach was implemented to reveal and quantify the dietary fat-related components of the disease. Three modified dairy fats (40% energy) were prepared from regular butter by mixing with a plant oil mixture, by removing cholesterol alone, or by removing cholesterol in combination with reducing saturated fatty acids.

GI symptoms in infants are a potential target for fermented infant milk formulae: a review.

Besides pre- and pro-biotic-containing infant formulae, fermented infant formulae are commonly used to relieve or prevent symptoms of gastrointestinal (GI) discomfort in young infants. During the fermentation process in cow's milk-based formulae, the beneficial bacteria modulate the product by forming several beneficial compounds, which contribute to the alleviation of the symptoms observed. This review summarizes the clinical evidence on the impact of fermented infant formulae on common pediatric GI-symptoms.

Individual and combined action of pancreatic lipase and pancreatic lipase-related proteins 1 and 2 on native versus homogenized milk fat globules.

Pancreatic lipase (PL) and pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2) display different functional properties, despite close structures. The aim of the study was to compare the kinetic properties of recombinant human PLRP1, PLRP2, and PL on a physiological substrate: the milk fat under native and homogenized structures. No lipolytic activity is measured for PLRP1.

Role of the structural domains in the functional properties of pancreatic lipase-related protein 2.

Although structurally similar, classic pancreatic lipase (PL) and pancreatic lipase-related protein (PLRP)2, expressed in the pancreas of several species, differ in substrate specificity, sensitivity to bile salts and colipase dependence. In order to investigate the role of the two domains of PLRP2 in the function of the protein, two chimeric proteins were designed by swapping the N and C structural domains between the horse PL (Nc and Cc domains) and the horse PLRP2 (N2 and C2 domains). NcC2 and N2Cc proteins were expressed in insect cells, purified by one-step chromatography, and characterized.

High-level expression of nonglycosylated human pancreatic lipase-related protein 2 in Pichia pastoris.

The human pancreatic lipase-related protein 2 (HPLRP2) was produced in the methylotrophic yeast Pichia pastoris. The HPLRP2 cDNA corresponding to the protein coding sequence including the native signal sequence, was cloned into the pPIC9K vector and integrated into the genome of P. pastoris.

Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions.

The major sources of vitamin A in the human diet are retinyl esters (mainly retinyl palmitate) and provitamin A carotenoids. It has been shown that classical pancreatic lipase (PL) is involved in the luminal hydrolysis of retinyl palmitate (RP), but it is not known whether pancreatic lipase-related proteins 1 (PLRP1) and 2 (PLRP2), two other lipases recovered in the human pancreatic juice, are also involved. The aim of this study was to assess whether RP acts a substrate for these lipase-related proteins.