Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine

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Standard

Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine. / Nielsen, Line R.; Nielsen, Søren B.; Zhao, Zichen; Olsen, Karsten; Nielsen, Jacob H.; Lund, Marianne Nissen.

I: Journal of Agricultural and Food Chemistry, Bind 66, Nr. 27, 2018, s. 7110-7120.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Nielsen, LR, Nielsen, SB, Zhao, Z, Olsen, K, Nielsen, JH & Lund, MN 2018, 'Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine', Journal of Agricultural and Food Chemistry, bind 66, nr. 27, s. 7110-7120. https://doi.org/10.1021/acs.jafc.8b01172

APA

Nielsen, L. R., Nielsen, S. B., Zhao, Z., Olsen, K., Nielsen, J. H., & Lund, M. N. (2018). Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine. Journal of Agricultural and Food Chemistry, 66(27), 7110-7120. https://doi.org/10.1021/acs.jafc.8b01172

Vancouver

Nielsen LR, Nielsen SB, Zhao Z, Olsen K, Nielsen JH, Lund MN. Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine. Journal of Agricultural and Food Chemistry. 2018;66(27):7110-7120. https://doi.org/10.1021/acs.jafc.8b01172

Author

Nielsen, Line R. ; Nielsen, Søren B. ; Zhao, Zichen ; Olsen, Karsten ; Nielsen, Jacob H. ; Lund, Marianne Nissen. / Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine. I: Journal of Agricultural and Food Chemistry. 2018 ; Bind 66, Nr. 27. s. 7110-7120.

Bibtex

@article{d140bfaae4bb4c36856d5ca8f9f02522,
title = "Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine",
abstract = "The effect of free cysteine (in different concentrations) on the thermal aggregation of calcium-saturated (Ca-sat) and -depleted (Ca-dep) alpha-lactalbumin (alpha-LA) was investigated at 25, 50, and 70 degrees C. The temperatures chosen were below the denaturation temperature (T-d) of Ca-dep and Ca-sat alpha-LA (25 degrees C), above the T-d of Ca-dep alpha-LA and below that of Ca-sat alpha-LA (50 degrees C), and above the T-d of Ca-sat alpha-LA (70 degrees C). Size-exclusion chromatography coupled to multiangle light scattering showed that no aggregation or only minor aggregation was obtained at the investigated temperatures for both Ca-dep and Casat alpha-LA even at extended holding times. Aggregates of Ca-sat alpha-LA were larger than those developed for Ca-dep alpha-LA. The addition of cysteine, a low-molecular-mass free thiol, resulted in increased aggregation of both Ca-sat and Ca-dep alpha-LA. Comparisons of SDS-PAGE run under reducing and nonreducing conditions showed that the formed cross-links were primarily disulfide bonds, but Western blots also showed small contributions from dityrosine cross-link formation. The aggregation kinetics related to monomer loss during heat treatment were determined by RP-UPLC and showed that the addition of cysteine increased the rate of aggregation. The activation energies for Ca-dep alpha-LA with 0.35 and 0.7 mM cysteine were found to be 59 +/- 1 and 46 +/- 4 kJ/mol, respectively, which showed that less energy was needed for the enhanced thermal aggregation of alpha-LA when the cysteine concentration was increased. This study showed that it was possible to control the aggregation size of alpha-LA by manipulating the incubation temperature and the cysteine concentration.",
keywords = "alpha-lactalbumin, calcium, cysteine, aggregation, thiol-disulfide exchange, kinetics",
author = "Nielsen, {Line R.} and Nielsen, {S{\o}ren B.} and Zichen Zhao and Karsten Olsen and Nielsen, {Jacob H.} and Lund, {Marianne Nissen}",
year = "2018",
doi = "10.1021/acs.jafc.8b01172",
language = "English",
volume = "66",
pages = "7110--7120",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "27",

}

RIS

TY - JOUR

T1 - Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine

AU - Nielsen, Line R.

AU - Nielsen, Søren B.

AU - Zhao, Zichen

AU - Olsen, Karsten

AU - Nielsen, Jacob H.

AU - Lund, Marianne Nissen

PY - 2018

Y1 - 2018

N2 - The effect of free cysteine (in different concentrations) on the thermal aggregation of calcium-saturated (Ca-sat) and -depleted (Ca-dep) alpha-lactalbumin (alpha-LA) was investigated at 25, 50, and 70 degrees C. The temperatures chosen were below the denaturation temperature (T-d) of Ca-dep and Ca-sat alpha-LA (25 degrees C), above the T-d of Ca-dep alpha-LA and below that of Ca-sat alpha-LA (50 degrees C), and above the T-d of Ca-sat alpha-LA (70 degrees C). Size-exclusion chromatography coupled to multiangle light scattering showed that no aggregation or only minor aggregation was obtained at the investigated temperatures for both Ca-dep and Casat alpha-LA even at extended holding times. Aggregates of Ca-sat alpha-LA were larger than those developed for Ca-dep alpha-LA. The addition of cysteine, a low-molecular-mass free thiol, resulted in increased aggregation of both Ca-sat and Ca-dep alpha-LA. Comparisons of SDS-PAGE run under reducing and nonreducing conditions showed that the formed cross-links were primarily disulfide bonds, but Western blots also showed small contributions from dityrosine cross-link formation. The aggregation kinetics related to monomer loss during heat treatment were determined by RP-UPLC and showed that the addition of cysteine increased the rate of aggregation. The activation energies for Ca-dep alpha-LA with 0.35 and 0.7 mM cysteine were found to be 59 +/- 1 and 46 +/- 4 kJ/mol, respectively, which showed that less energy was needed for the enhanced thermal aggregation of alpha-LA when the cysteine concentration was increased. This study showed that it was possible to control the aggregation size of alpha-LA by manipulating the incubation temperature and the cysteine concentration.

AB - The effect of free cysteine (in different concentrations) on the thermal aggregation of calcium-saturated (Ca-sat) and -depleted (Ca-dep) alpha-lactalbumin (alpha-LA) was investigated at 25, 50, and 70 degrees C. The temperatures chosen were below the denaturation temperature (T-d) of Ca-dep and Ca-sat alpha-LA (25 degrees C), above the T-d of Ca-dep alpha-LA and below that of Ca-sat alpha-LA (50 degrees C), and above the T-d of Ca-sat alpha-LA (70 degrees C). Size-exclusion chromatography coupled to multiangle light scattering showed that no aggregation or only minor aggregation was obtained at the investigated temperatures for both Ca-dep and Casat alpha-LA even at extended holding times. Aggregates of Ca-sat alpha-LA were larger than those developed for Ca-dep alpha-LA. The addition of cysteine, a low-molecular-mass free thiol, resulted in increased aggregation of both Ca-sat and Ca-dep alpha-LA. Comparisons of SDS-PAGE run under reducing and nonreducing conditions showed that the formed cross-links were primarily disulfide bonds, but Western blots also showed small contributions from dityrosine cross-link formation. The aggregation kinetics related to monomer loss during heat treatment were determined by RP-UPLC and showed that the addition of cysteine increased the rate of aggregation. The activation energies for Ca-dep alpha-LA with 0.35 and 0.7 mM cysteine were found to be 59 +/- 1 and 46 +/- 4 kJ/mol, respectively, which showed that less energy was needed for the enhanced thermal aggregation of alpha-LA when the cysteine concentration was increased. This study showed that it was possible to control the aggregation size of alpha-LA by manipulating the incubation temperature and the cysteine concentration.

KW - alpha-lactalbumin

KW - calcium

KW - cysteine

KW - aggregation

KW - thiol-disulfide exchange

KW - kinetics

U2 - 10.1021/acs.jafc.8b01172

DO - 10.1021/acs.jafc.8b01172

M3 - Journal article

C2 - 29916707

VL - 66

SP - 7110

EP - 7120

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 27

ER -

ID: 200819976