Conformational stability of the potato serine protease ihibitor group

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)

Abstract

The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at least one stable intermediate is present. Additionally, the occurrence of aggregation, especially at low scan rates, increases the apparent cooperativity of the unfolding and makes the system kinetically rather than thermodynamically controlled. Aggregate formation seems to occur via a specific mechanism of which PSPI in a tetrameric form is the end product and which may involve disulfide interchanges.
Original languageEnglish
Pages (from-to)3191-3196
JournalJournal of Agricultural and Food Chemistry
Volume53
Issue number8
DOIs
Publication statusPublished - 2005

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Serine Proteinase Inhibitors
Serine Proteases
serine proteinases
Solanum tuberosum
proteinase inhibitors
potatoes
fluorescence emission spectroscopy
Hot Temperature
Guanidine
Fluorescence spectroscopy
Interchanges
circular dichroism spectroscopy
Protease Inhibitors
heat
Disulfides
Fluorescence Spectrometry
Agglomeration
sulfides
Spectrum Analysis
tubers

Keywords

  • differential scanning calorimetry
  • molten-globule state
  • circular-dichroism
  • alpha-lactalbumin
  • side-chains
  • cv elkana
  • proteins
  • form

Cite this

@article{3b4159d42a754099ac6474aad4306377,
title = "Conformational stability of the potato serine protease ihibitor group",
abstract = "The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at least one stable intermediate is present. Additionally, the occurrence of aggregation, especially at low scan rates, increases the apparent cooperativity of the unfolding and makes the system kinetically rather than thermodynamically controlled. Aggregate formation seems to occur via a specific mechanism of which PSPI in a tetrameric form is the end product and which may involve disulfide interchanges.",
keywords = "differential scanning calorimetry, molten-globule state, circular-dichroism, alpha-lactalbumin, side-chains, cv elkana, proteins, form",
author = "L.A.M. Pouvreau and H. Gruppen and {van Koningsveld}, G.A. and {van den Broek}, L.A.M. and A.G.J. Voragen",
year = "2005",
doi = "10.1021/jf048353v",
language = "English",
volume = "53",
pages = "3191--3196",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "8",

}

Conformational stability of the potato serine protease ihibitor group. / Pouvreau, L.A.M.; Gruppen, H.; van Koningsveld, G.A.; van den Broek, L.A.M.; Voragen, A.G.J.

In: Journal of Agricultural and Food Chemistry, Vol. 53, No. 8, 2005, p. 3191-3196.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Conformational stability of the potato serine protease ihibitor group

AU - Pouvreau, L.A.M.

AU - Gruppen, H.

AU - van Koningsveld, G.A.

AU - van den Broek, L.A.M.

AU - Voragen, A.G.J.

PY - 2005

Y1 - 2005

N2 - The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at least one stable intermediate is present. Additionally, the occurrence of aggregation, especially at low scan rates, increases the apparent cooperativity of the unfolding and makes the system kinetically rather than thermodynamically controlled. Aggregate formation seems to occur via a specific mechanism of which PSPI in a tetrameric form is the end product and which may involve disulfide interchanges.

AB - The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at least one stable intermediate is present. Additionally, the occurrence of aggregation, especially at low scan rates, increases the apparent cooperativity of the unfolding and makes the system kinetically rather than thermodynamically controlled. Aggregate formation seems to occur via a specific mechanism of which PSPI in a tetrameric form is the end product and which may involve disulfide interchanges.

KW - differential scanning calorimetry

KW - molten-globule state

KW - circular-dichroism

KW - alpha-lactalbumin

KW - side-chains

KW - cv elkana

KW - proteins

KW - form

U2 - 10.1021/jf048353v

DO - 10.1021/jf048353v

M3 - Article

VL - 53

SP - 3191

EP - 3196

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 8

ER -