The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris

Jing Lin, Roger Fido, Peter Shewry, David B. Archer, Marcos J.C. Alcocer

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Soybean seeds contain two 2S albumin storage proteins (AL1 and AL3) which may contribute to their industrial processing quality and allergenicity. We show that these proteins (AL1 and AL3) are well expressed by the methylotrophic yeast Pichia pastoris and that one of the secreted proteins (AL3) has a similar conformation and stability to that purified from soybean seeds. Further, we show that the subunits are post-translationally processed within the same loop region as the native protein but with some differences in the precise sites. This internal processing provides useful information on the endoproteolytic activity in P. pastoris. We also show that, similar to many plant allergens, the 2S albumins from soybean are stable to heat and chemical treatments.

Original languageEnglish
Pages (from-to)203-212
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1698
Issue number2
DOIs
StatePublished - 6 May 2004
Externally publishedYes

Keywords

  • 2S albumin
  • Pichia pastoris
  • Plant allergen
  • Proteolytic processing
  • Soybean protein

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