Nomenklatur und einige Eigenschaften der Molkenproteine. 2. Mitt. α‐Lactalbumin, Immunoglobuline, Proteose‐Peptone, Minorproteine und Enzyme

Sienkiewicz, T.

doi:10.1002/food.19810250405

Cited by 9 publications

(4 citation statements)

References 114 publications

(7 reference statements)

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“…The present study convincingly shows that IW, a dipeptide present in whey protein (Sienkiewicz 1981) and an enzymatically prepared hydrolysate from whey protein may fully attenuate the age-associated SBP rise in SHR similar to CAP (Fig. 1).…”

Section: Discussionsupporting

confidence: 75%

Antihypertensive and cardioprotective effects of the dipeptide isoleucine–tryptophan and whey protein hydrolysate

et al. 2015

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Whey protein hydrolysate and isoleucine-tryptophan powerfully inhibit plasma ACE resulting in antihypertensive effects. Moreover, isoleucine-tryptophan blunts tissue ACE activity, reduces matrix metalloproteinase-2 activity and improves coronary flow reserve. Thus, whey protein hydrolysate and particularly isoleucine-tryptophan may serve as innovative food additives with the goal of attenuating hypertension.

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Section: Discussionsupporting

confidence: 75%

Antihypertensive and cardioprotective effects of the dipeptide isoleucine–tryptophan and whey protein hydrolysate

et al. 2015

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“…This monomeric protein contains 123 amino acids, of which a high number is essential. α–lactalbumin possesses four disulfide bonds, but no free cysteine residues (Sienkiewicz, 1981b). …”

Section: Introductionmentioning

confidence: 99%

Effect of Sodium Sulfite, Sodium Dodecyl Sulfate, and Urea on the Molecular Interactions and Properties of Whey Protein Isolate-Based Films

et al. 2017

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Whey protein coatings and cast films are promising for use as food packaging materials. Ongoing research is endeavoring to reduce their permeability. The intention of this study was to evaluate the effect of the reactive additives sodium sulfite, sodium dodecyl sulfate (SDS), and urea on the oxygen barrier, water vapor barrier, and protein solubility of whey protein cast films. The concentration of the reactive additives was 1 to 20 wt.-%. Dried whey protein cast films were used as substrate materials. The water vapor transmission rate, the oxygen permeability, and the protein solubility were measured. Effective diffusion coefficients and effective sorption coefficients were calculated from the results of the water vapor sorption experiments. The presence of sodium sulfite resulted in an increased number of hydrophobic interactions and hydrogen bonds and a slightly decreased number of disulfide bonds. The oxygen permeability decreased from 68 to 46 cm3 (STP/standard temperature and pressure) 100 μm (m2 d bar)−1 for 1 wt.-% SDS in the whey protein cast film. The water vapor transmission rate decreased from 165 to 44 g 100 μm (m2 d)−1 measured at 50 to 0% r. h. for 20 wt.-% SDS in the whey protein cast film. The reduction in the water vapor transmission rate correlated with the lower effective diffusion coefficient.

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“…Both main components of cow milk, α‐Ltb (14.178 kDa, p I ≈ 4.2‐4.5) and ß‐Ltg (isoform A: M = 18.36 kDa; isoform B: M = 18.28 kDa; p I = 5.4), were also included in the arsenic‐binding studies. In the polypeptide chain of α‐Ltb, four structure‐forming disulfide bridges occur that give a globular structure to the protein.…”

Section: Resultsmentioning

confidence: 99%

Qualitative and quantitative characterization of the arsenic‐binding behaviour of sulfur‐containing peptides and proteins by the coupling of reversed phase liquid chromatography to electrospray ionization mass spectrometry

Schmidt

Mickein

2012

J. Mass. Spectrom.

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Phenylarsenic-substituted cysteine-containing peptides and proteins were completely differentiated from their unbound original forms by the coupling of reversed phase liquid chromatography with electrospray ionization mass spectrometry. The analysis of biomolecules possessing structure-stabilizing disulfide bridges after reduction provides new insights into requirements concerning the accessibility of cysteine residues for reducing agents as well as for arsenic compounds in a spatial protein structure. Complementary binding studies performed using direct ESI-MS without chromatographic coupling in different solvent systems demonstrated that more than one binding site were activated for aprotinin and lysozyme in denaturing solvents because of a stronger defolding. From the intensities of the different charge states occurring in the mass spectra as well as from the LC elution behaviour, it can be deduced that the folding state of the arsenic-bound protein species resembles the native, oxidized conformation. In contrast, although the milk protein α-lactalbumin has several disulfide bridges, only one phenylarsenic moiety was bound under strongly denaturing conditions. Because of the charge state distribution in the ESI mass spectra, a conformational change to a molten globule structure is assumed. For the second considered milk protein ß-lactoglobulin, a noncovalent interaction with phenylarsine oxide was detected. In general, smaller apparent binding constants for the condensation reactions of the biomolecules with phenylarsine oxide leading to covalent arsenic-sulfur bindings were determined from direct injection ESI-MS measurements than from LC-ESI-MS coupling. The following order of binding affinities for one phenylarsenic group can be assumed from both ESI-MS and LC-ESI-MS: nonapeptide vasopressin > nonapeptide vasotocin > lysozyme > aprotinin > α-lactalbumin > thioredoxin. Kinetic investigations by LC-ESI-MS yielded a partial reaction order of 2 for vasopressin, Lys and α-lactalbumin and corresponding half-lives of 0.93, 2.56 and 123.5 min, respectively.

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Nomenklatur und einige Eigenschaften der Molkenproteine. 2. Mitt. α‐Lactalbumin, Immunoglobuline, Proteose‐Peptone, Minorproteine und Enzyme

Cited by 9 publications

References 114 publications

Antihypertensive and cardioprotective effects of the dipeptide isoleucine–tryptophan and whey protein hydrolysate

Antihypertensive and cardioprotective effects of the dipeptide isoleucine–tryptophan and whey protein hydrolysate

Effect of Sodium Sulfite, Sodium Dodecyl Sulfate, and Urea on the Molecular Interactions and Properties of Whey Protein Isolate-Based Films

Qualitative and quantitative characterization of the arsenic‐binding behaviour of sulfur‐containing peptides and proteins by the coupling of reversed phase liquid chromatography to electrospray ionization mass spectrometry

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