Structural characterization of potato protease inhibitor I (Cv. Bintje) after expression in Pichia pastoris

L.A.M. van den Broek, L.A.M. Pouvreau, G. Lommerse, B. Schipper, G.A. van Koningsveld, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

11 Citations (Scopus)

Abstract

In the present study the structural properties of potato protease inhibitor 1 (PI-1) were studied as a function of temperature to elucidate its precipitation mechanism upon heating. A cDNA coding for PI-1 from cv. Bintje was cloned and expressed in Pichia pastoris. Using the recombinant PI-1 it was suggested that PI-1 behaves as a hexameric protein rather than as a pentamer, as previously proposed in the literature. The recombinant protein seems either to have a predominantly unordered structure or to belong to the -II proteins. Differential scanning calorimetry analysis of PI-1 revealed that its thermal unfolding occurs via one endothermic transition in which the hexameric PI-1 probably unfolds, having a dimer instead of a monomer as cooperative unit. The transition temperature for the recombinant PI-1 was 88 C. Similar results were obtained for a partially purified pool of native PI-1 from cv. Bintje
Original languageEnglish
Pages (from-to)4928-4934
JournalJournal of Agricultural and Food Chemistry
Volume52
DOIs
Publication statusPublished - 2004

Keywords

  • circular-dichroism
  • stability
  • proteins
  • chymotrypsin
  • tubers
  • solubility
  • elkana

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