Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure. / Marciniak, Alice; Suwal, Shyam; Brisson, Guillaume; Britten, Michel; Pouliot, Yves; Doyen, Alain.

In: Food Chemistry, Vol. 275, 2019, p. 193-196.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Marciniak, A, Suwal, S, Brisson, G, Britten, M, Pouliot, Y & Doyen, A 2019, 'Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure', Food Chemistry, vol. 275, pp. 193-196. https://doi.org/10.1016/j.foodchem.2018.09.110

APA

Marciniak, A., Suwal, S., Brisson, G., Britten, M., Pouliot, Y., & Doyen, A. (2019). Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure. Food Chemistry, 275, 193-196. https://doi.org/10.1016/j.foodchem.2018.09.110

Vancouver

Marciniak A, Suwal S, Brisson G, Britten M, Pouliot Y, Doyen A. Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure. Food Chemistry. 2019;275:193-196. https://doi.org/10.1016/j.foodchem.2018.09.110

Author

Marciniak, Alice ; Suwal, Shyam ; Brisson, Guillaume ; Britten, Michel ; Pouliot, Yves ; Doyen, Alain. / Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure. In: Food Chemistry. 2019 ; Vol. 275. pp. 193-196.

Bibtex

@article{c7a3258384af4422be7b7fe956c4d93d,
title = "Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure",
abstract = "Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6. Specifically, we studied the effect of different concentration of CN on α-la purity and recovery. Model solutions of α-la, β-lg and CN (from 0 to 5 mg/mL) were pressurized (600 MPa–5 min). After acidification and centrifugation of pressure-treated solutions, purity of α-la was increased up to 78% with a recovery of 88% for solution without CN. In contrast with our initial hypothesis, the presence of CN decreased β-lg pressure-induced aggregation and co-precipitation upon acidification and significantly reduced purity (∼71%). Therefore, our results suggest a chaperone-like activity of CN on β-lg pressure-induced aggregation which needs further investigation.",
keywords = "Alpha-lactalbumin purification, High hydrostatic pressure, Protein aggregation, Whey protein fractionation",
author = "Alice Marciniak and Shyam Suwal and Guillaume Brisson and Michel Britten and Yves Pouliot and Alain Doyen",
year = "2019",
doi = "10.1016/j.foodchem.2018.09.110",
language = "English",
volume = "275",
pages = "193--196",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure

AU - Marciniak, Alice

AU - Suwal, Shyam

AU - Brisson, Guillaume

AU - Britten, Michel

AU - Pouliot, Yves

AU - Doyen, Alain

PY - 2019

Y1 - 2019

N2 - Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6. Specifically, we studied the effect of different concentration of CN on α-la purity and recovery. Model solutions of α-la, β-lg and CN (from 0 to 5 mg/mL) were pressurized (600 MPa–5 min). After acidification and centrifugation of pressure-treated solutions, purity of α-la was increased up to 78% with a recovery of 88% for solution without CN. In contrast with our initial hypothesis, the presence of CN decreased β-lg pressure-induced aggregation and co-precipitation upon acidification and significantly reduced purity (∼71%). Therefore, our results suggest a chaperone-like activity of CN on β-lg pressure-induced aggregation which needs further investigation.

AB - Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6. Specifically, we studied the effect of different concentration of CN on α-la purity and recovery. Model solutions of α-la, β-lg and CN (from 0 to 5 mg/mL) were pressurized (600 MPa–5 min). After acidification and centrifugation of pressure-treated solutions, purity of α-la was increased up to 78% with a recovery of 88% for solution without CN. In contrast with our initial hypothesis, the presence of CN decreased β-lg pressure-induced aggregation and co-precipitation upon acidification and significantly reduced purity (∼71%). Therefore, our results suggest a chaperone-like activity of CN on β-lg pressure-induced aggregation which needs further investigation.

KW - Alpha-lactalbumin purification

KW - High hydrostatic pressure

KW - Protein aggregation

KW - Whey protein fractionation

U2 - 10.1016/j.foodchem.2018.09.110

DO - 10.1016/j.foodchem.2018.09.110

M3 - Journal article

C2 - 30724187

VL - 275

SP - 193

EP - 196

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

ER -

ID: 204113852