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LE Magazine January 2002


Competition for glutathione precursors between the immune system and the skeletal muscle: pathogenesis of chronic fatigue syndrome.

The chronic fatigue syndrome (CFS) is typically associated or follows a recognized or presumed infection. Abnormalities of both humoral and cellular immunity have been demonstrated in a substantial proportion of patients with CFS. The most consistent findings are of impaired lymphocyte responses to mitogen. As an antioxidant, glutathione (GSH) is essential for allowing the lymphocyte to express its full potential without being hampered by oxiradical accumulation. Hence, protracted challenge of the immunocytes may lead to cellular GSH depletion. Because GSH is also essential to aerobic muscular contraction, an undesirable competition for GSH precursors between the immune and muscular systems may develop. It is conceivable that the priority of the immune system for the survival of the host has drawn to this vital area the ever-diminishing GSH precursors, thus depriving the skeletal muscle of adequate GSH precursors to sustain a normal aerobic metabolism resulting in fatigue and eventually myalgia.

Med Hypotheses 1999 Oct;53(4):347-9

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

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.

J Dairy Res 2001 Aug;68(3):471-81

Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics.

Casein and whey protein were hydrolyzed using 11 different commercially available enzyme preparations. Emulsion-forming ability and emulsion stability of the digests were measured as well as biochemical properties with the objective to study the relations between hydrolysate characteristics and emulsion properties. All whey protein hydrolysates formed emulsions with bimodal droplet size distributions, signifying poor emulsion-forming ability. Emulsion-forming ability of some casein hydrolysates was comparable to that of intact casein. Emulsion instability was caused by creaming and coalescence. Creaming occurred mainly in whey hydrolysate emulsions and in casein hydrolysate emulsions containing large emulsion droplets. Coalescence was dominant in casein emulsions with a broad particle size distribution. Emulsion instability due to coalescence was related to apparent molecular weight distribution of hydrolysates; a relative high amount of peptides larger than 2 kDa positively influences emulsion stability.

J Agric Food Chem 2001 Oct;49(10):5005-12

Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties.

Surface hydrophobicity of whey protein concentrate (WPC) under heated (85 degrees C for 5, 10, 20, 30, 40, and 60 min) and unheated conditions was measured using cis-parinaric acid (CPA), 1-anilino-8-naphthalenesulfonate (ANS), and a fluorescence quenching method using acrylamide as a quencher. This last method evaluates the degree of exposure of tryptophanyl residues in proteins to the solvent. The initial slope of Stern-Volmer plots, K(app), was used as an index of protein hydrophobicity. Surface hydrophobicity of WPC exhibited good relation with surface functional properties such as emulsifying and foaming. Analysis of the data obtained in this work showed that the fluorescence quenching method gave results similar to those obtained using CPA and ANS. Therefore, this simple technique is satisfactory in effectively obtaining information about the hydrophobicity of whey proteins.

J Agric Food Chem 2001 Oct;49(10):4784-9

Mechanical characterization of network formation during heat-induced gelation of whey protein dispersions.

The formation of gel network structures during isothermal heating of whey protein aqueous dispersions was probed by mechanical spectroscopy. It was anticipated that the pathway of the sol-to-gel transition of whey protein dispersions is quite different from that of ordinary cross-linking polymers (e.g., percolation-type transition), since aqueous solutions of native whey proteins have been shown to be highly structured even before gelation, in our previous study. At 20 degrees C, aqueous dispersions of beta-lactoglobulin, the major whey protein, and those of whey protein isolate (WPI), a mixture of whey proteins, exhibited solid-like mechanical spectra, i.e., the predominant storage modulus G’ over the loss modulus G”, in a certain range of the frequency omega (1-100 rad/s), regardless of the presence or absence of added NaCl. The existence of the added salt was, however, a critical factor for determining transitions in mechanical spectra during gelation at 70 degrees C. beta-Lactoglobulin dispersions in 0.1 mol/dm(3) NaCl maintained the solid-like nature during the entire gelation process and, after passing through the gelation point, satisfied parallel power laws (G’ approximately G” approximately omega(n)) that have been proposed for a critical gel (i.e., the gel at the gelation point) that possesses a self-similar or fractal network structure. In contrast, beta-lactoglobulin dispersions without added salt exhibited a transition from solid-like [G’(omega) > G”(omega)] to liquid-like [G’(omega) < G”(omega)] mechanical spectra before gelation, but no parallel power law behavior was recognized at the gelation point. During extended heating time (aging), beta-lactoglobulin gels with 0.1 mol/dm(3) NaCl showed deviations from the parallel power laws, while spectra of gels without added NaCl approached the parallel power laws, suggesting that post-gelation reactions also significantly affect gel network structures. A percolation-type sol-to-gel transition was found only for WPI dispersions without added salt.

Biopolymers 2000;56(2):109-19

The effect of whey protein supplementation with and without creatine monohydrate combined with resistance training on lean tissue mass and muscle strength.

Our purpose was to assess muscular adaptations during 6 weeks of resistance training in 36 males randomly assigned to supplementation with whey protein (W; 1.2 g/kg/day), whey protein and creatine monohydrate (WC; 0.1 g/kg/day), or placebo (P; 1.2 g/kg/day maltodextrin). Measures included lean tissue mass by dual energy x-ray absorptiometry, bench press and squat strength (1-repetition maximum), and knee extension/flexion peak torque. Lean tissue mass increased to a greater extent with training in WC compared to the other groups, and in the W compared to the P group (p <.05). Bench press strength increased to a greater extent for WC compared to W and P (p <.05). Knee extension peak torque increased with training for WC and W (p <.05), but not for P. All other measures increased to a similar extent across groups. Continued training without supplementation for an additional 6 weeks resulted in maintenance of strength and lean tissue mass in all groups. Males that supplemented with whey protein while resistance training demonstrated greater improvement in knee extension peak torque and lean tissue mass than males engaged in training alone. Males that supplemented with a combination of whey protein and creatine had greater increases in lean tissue mass and bench press than those who supplemented with only whey protein or placebo. However, not all strength measures were improved with supplementation, since subjects who supplemented with creatine and/or whey protein had similar increases in squat strength and knee flexion peak torque compared to subjects who received placebo.

Int J Sport Nutr Exerc Metab 2001 Sep;11(3):349-64

Solubility and moisture sorption isotherms of whey-protein-based edible films as influenced by lipid and plasticizer incorporation.

Plasticized whey-protein and whey-protein emulsion films were produced using sorbitol and glycerol as plasticizers and butterfat and candelilla wax as lipids. Protein, plasticizer, and lipid ratios were optimized to obtain acceptable free-standing flexible films. Water solubility (20 degrees C, 24 h) and moisture sorption isotherms (0.18-0.90 a(w), 25 degrees C) of the films were determined. The experimental moisture sorption isotherm values were fitted using the Guggenheim-Anderson-DeBoer (GAB) model. Solubility and equilibrium moisture contents (EMC) of the films were influenced by plasticizer and lipid incorporation. EMCs of all films increased rapidly at a(w) > or = 0.65. Incorporation of lipids reduced solubilities and EMCs of sorbitol- and glycerol-plasticized films. The effects of plasticizer and lipid type on GAB constants were also determined.

J Agric Food Chem 2001 Sep;49(9):4388-91

Affinity enrichment of bovine lactoferrin in whey.

Bovine lactoferrin was enriched in various whey samples by affinity chromatography using immobilized gangliosides. Bovine gangliosides were isolated from fresh buttermilk using a combination of ultrafiltration and organic extraction. Isolated gangliosides were covalently immobilized onto controlled-pore glass beads. The immobilized matrix contained 66 micrograms of gangliosides per gram of beads. After loading the matrix with reconstituted whey protein isolate (WPI) or whey protein concentrate (WPC), the matrix was washed with sodium phosphate buffer (pH 7) followed by sodium acetate buffer (pH 4) before elution of lactoferrin with 1 M NaCl in sodium acetate buffer. From the intensities of the protein bands in SDS-PAGE, lactoferrin constituted a minimum of 40% of the total protein in the salt eluted sample. WPI, pretrated by heating and ultrafiltration, showed the highest lactoferrin purity among protein sources, while WPI (10% wt/vol) showed the highest recovery. These results show that immobilized gangliosides can be used to enrich the lactoferrin content of whey.

Prep Biochem Biotechnol 2001 Aug;31(3):229-40


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