Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

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Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size. / Madsen, Mikkel; Westh, Peter; Khan, Sanaullah; Ipsen, Richard; Almdal, Kristoffer; Aachmann, Finn L.; Svensson, Birte.

In: Biomacromolecules, Vol. 22, No. 2, 2021, p. 649-660.

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

Harvard

Madsen, M, Westh, P, Khan, S, Ipsen, R, Almdal, K, Aachmann, FL & Svensson, B 2021, 'Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size', Biomacromolecules, vol. 22, no. 2, pp. 649-660. https://doi.org/10.1021/acs.biomac.0c01485

APA

Madsen, M., Westh, P., Khan, S., Ipsen, R., Almdal, K., Aachmann, F. L., & Svensson, B. (2021). Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size. Biomacromolecules, 22(2), 649-660. https://doi.org/10.1021/acs.biomac.0c01485

Vancouver

Madsen M, Westh P, Khan S, Ipsen R, Almdal K, Aachmann FL et al. Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size. Biomacromolecules. 2021;22(2):649-660. https://doi.org/10.1021/acs.biomac.0c01485

Author

Madsen, Mikkel ; Westh, Peter ; Khan, Sanaullah ; Ipsen, Richard ; Almdal, Kristoffer ; Aachmann, Finn L. ; Svensson, Birte. / Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size. In: Biomacromolecules. 2021 ; Vol. 22, No. 2. pp. 649-660.

Bibtex

@article{c2a9483ff6f94841be9510e8da863139,
title = "Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size",
abstract = "Alginates, serving as hydrocolloids in the food and pharma industries, form particles at pH < 4.5 with positively charged proteins, such as β-lactoglobulin (β-Lg). Alginates are linear anionic polysaccharides composed of 1,4-linked β-d-mannuronate (M) and α-l-guluronate (G) residues. The impact of M and G contents and pH is investigated to correlate with the formation and size of β-Lg alginate complexes under relevant ionic strength. It is concluded, using three alginates of M/G ratios 0.6, 1.1, and 1.8 and similar molecular mass, that β-Lg binding capacity is higher at pH 4.0 than at pH 2.65 and for high M content. By contrast, the largest particles are obtained at pH 2.65 and with high G content. At pH 4.0 and 2.65, the stoichiometry was 28-48 and 3-10 β-Lg molecules bound per alginate, respectively, increasing with higher M content. The findings will contribute to the design of formation of the desired alginate-protein particles in the acidic pH range.",
author = "Mikkel Madsen and Peter Westh and Sanaullah Khan and Richard Ipsen and Kristoffer Almdal and Aachmann, {Finn L.} and Birte Svensson",
year = "2021",
doi = "10.1021/acs.biomac.0c01485",
language = "English",
volume = "22",
pages = "649--660",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "2",

}

RIS

TY - JOUR

T1 - Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

AU - Madsen, Mikkel

AU - Westh, Peter

AU - Khan, Sanaullah

AU - Ipsen, Richard

AU - Almdal, Kristoffer

AU - Aachmann, Finn L.

AU - Svensson, Birte

PY - 2021

Y1 - 2021

N2 - Alginates, serving as hydrocolloids in the food and pharma industries, form particles at pH < 4.5 with positively charged proteins, such as β-lactoglobulin (β-Lg). Alginates are linear anionic polysaccharides composed of 1,4-linked β-d-mannuronate (M) and α-l-guluronate (G) residues. The impact of M and G contents and pH is investigated to correlate with the formation and size of β-Lg alginate complexes under relevant ionic strength. It is concluded, using three alginates of M/G ratios 0.6, 1.1, and 1.8 and similar molecular mass, that β-Lg binding capacity is higher at pH 4.0 than at pH 2.65 and for high M content. By contrast, the largest particles are obtained at pH 2.65 and with high G content. At pH 4.0 and 2.65, the stoichiometry was 28-48 and 3-10 β-Lg molecules bound per alginate, respectively, increasing with higher M content. The findings will contribute to the design of formation of the desired alginate-protein particles in the acidic pH range.

AB - Alginates, serving as hydrocolloids in the food and pharma industries, form particles at pH < 4.5 with positively charged proteins, such as β-lactoglobulin (β-Lg). Alginates are linear anionic polysaccharides composed of 1,4-linked β-d-mannuronate (M) and α-l-guluronate (G) residues. The impact of M and G contents and pH is investigated to correlate with the formation and size of β-Lg alginate complexes under relevant ionic strength. It is concluded, using three alginates of M/G ratios 0.6, 1.1, and 1.8 and similar molecular mass, that β-Lg binding capacity is higher at pH 4.0 than at pH 2.65 and for high M content. By contrast, the largest particles are obtained at pH 2.65 and with high G content. At pH 4.0 and 2.65, the stoichiometry was 28-48 and 3-10 β-Lg molecules bound per alginate, respectively, increasing with higher M content. The findings will contribute to the design of formation of the desired alginate-protein particles in the acidic pH range.

U2 - 10.1021/acs.biomac.0c01485

DO - 10.1021/acs.biomac.0c01485

M3 - Journal article

C2 - 33417429

AN - SCOPUS:85099655321

VL - 22

SP - 649

EP - 660

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 2

ER -

ID: 257285569