Casein and whey differ in amino acid composition and in the rate of absorption; however, the absorption rate of casein can be increased to mimic that of whey by exogenous hydrolysis. The objective of the present study was to compare the effects of hydrolysed casein (HC), intact casein (IC) and intact whey (IW) on energy expenditure (EE) and appetite regulation, and thereby to investigate the influence of amino acid composition and the rate of absorption. In the present randomised cross-over study, twenty-four overweight and moderately obese young men and women consumed three isoenergetic dietary treatments that varied in protein source. The study was conducted in a respiration chamber, where EE, substrate oxidation and subjective appetite were measured over 24 h at three independent visits. Moreover, blood and urine samples were collected from the participants. The results showed no differences in 24 h and postprandial EE or appetite regulation. However, lipid oxidation, estimated from the respiratory quotient (RQ), was found to be higher after consumption of IW than after consumption of HC during daytime (P= 0·014) as well as during the time after the breakfast meal (P= 0·008) when the food was provided. Likewise, NEFA concentrations were found to be higher after consumption of IW than after consumption of HC and IC (P< 0·01). However, there was no overall difference in the concentration of insulin or glucagon-like peptide 1. In conclusion, dietary treatments when served as high-protein mixed meals induced similar effects on EE and appetite regulation, except for lipid oxidation, where RQ values suggest that it is higher after consumption of IW than after consumption of HC.
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http://dx.doi.org/10.1017/S000711451400213X | DOI Listing |
Anal Biochem
April 2025
Advanced Electrophoresis Solutions Ltd., 380 Jamieson Parkway, Unit 7 and 8, ON, N3C 4N4, Canada; AES Biotech Jiaxing Ltd., No. 501 South Changsheng Road, Economic and Technological Development Zone, Jiaxing City, Zhejiang Province, PR China. Electronic address:
Characterizing major bovine milk proteins, including whey and casein, is of significant interest in the dairy industry. The diverse array of protein proteoforms can be different in terms of genetic variation, breed ways, lactation stage, and animal nutritional status. Current routine methods for bovine milk protein profiling are typically based on immunological techniques, infrared spectroscopy, slab gel isoelectric focusing, capillary electrophoresis, and high-performance liquid chromatography.
View Article and Find Full Text PDFAnal Chem
January 2025
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Intact protein analysis using mass spectrometry (MS) is an important technique to characterize and provide a comprehensive overview of protein complexity. It is also the basis of "top-down" approaches in proteomics to describe the proteoforms of single protein's post-translational modifications (PTMs). MS-based analysis of intact proteins benefits from high-resolution separations prior to electrospray ionization.
View Article and Find Full Text PDFFood Res Int
November 2024
STLO, L'Institut Agro, INRAE, 35042 Rennes, France. Electronic address:
Food Chem
February 2025
Chair of Food Chemistry, Department Chemistry and Pharmacy, Friedrich-Alexander Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Str. 10, 91058 Erlangen, Germany. Electronic address:
Foods
August 2024
Department of Dairy and Food Science, Midwest Dairy Foods Research Center, South Dakota State University, Brookings, SD 57007, USA.
In dairy-based imitation mozzarella cheese (IMC) formulations, intact casein is critical and imparts IMC with a firm and elastic, stringy, melted texture. Rennet casein (RCN) is the desired ingredient to provide intact casein in IMC and is preferred over milk protein concentrate (MPC) and micellar casein concentrate (MCC). Transglutaminase (TGase), a crosslinking enzyme, alters the physical properties of MPC or MCC and may change IMC functionality.
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