Effect of pH and heat treatment on the structure and solubility of potato proteins in different preparations

G.A. van Koningsveld; H. Gruppen; H.H.J. de Jongh; G. Wijngaards; M.A.J.S. van Boekel

doi:10.1021/jf010340j

Effect of pH and heat treatment on the structure and solubility of potato proteins in different preparations

G.A. van Koningsveld, H. Gruppen, H.H.J. de Jongh, G. Wijngaards, M.A.J.S. van Boekel

Research output: Contribution to journal › Article › Academic › peer-review

108 Citations (Scopus)

Abstract

The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 °C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.

Original language	English
Pages (from-to)	4889-4997
Journal	Journal of Agricultural and Food Chemistry
Volume	2001
DOIs	https://doi.org/10.1021/jf010340j
Publication status	Published - 2001

Keywords

Differential scanning calorimetry
Patatin
Potato
Protease inhibitor
Solanum tuberosum
Solubility
Structural stability

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10.1021/jf010340j

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title = "Effect of pH and heat treatment on the structure and solubility of potato proteins in different preparations",

abstract = "The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 °C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.",

keywords = "Differential scanning calorimetry, Patatin, Potato, Protease inhibitor, Solanum tuberosum, Solubility, Structural stability",

author = "{van Koningsveld}, G.A. and H. Gruppen and {de Jongh}, H.H.J. and G. Wijngaards and {van Boekel}, M.A.J.S.",

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doi = "10.1021/jf010340j",

language = "English",

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pages = "4889--4997",

journal = "Journal of Agricultural and Food Chemistry",

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publisher = "American Chemical Society",

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TY - JOUR

T1 - Effect of pH and heat treatment on the structure and solubility of potato proteins in different preparations

AU - van Koningsveld, G.A.

AU - Gruppen, H.

AU - de Jongh, H.H.J.

AU - Wijngaards, G.

AU - van Boekel, M.A.J.S.

N1 - PDQ-660

PY - 2001

Y1 - 2001

N2 - The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 °C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.

AB - The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 °C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.

KW - Differential scanning calorimetry

KW - Patatin

KW - Potato

KW - Protease inhibitor

KW - Solanum tuberosum

KW - Solubility

KW - Structural stability

U2 - 10.1021/jf010340j

DO - 10.1021/jf010340j

M3 - Article

SN - 0021-8561

VL - 2001

SP - 4889

EP - 4997

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

ER -

Effect of pH and heat treatment on the structure and solubility of potato proteins in different preparations

Abstract

Keywords

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