The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris.
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.
Lin
Jing
J
School of Biology, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Fido
Roger
R
Shewry
Peter
P
Archer
David B
DB
Alcocer
Marcos J C
MJ
D055516:2S Albumins, Plant; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D002942:Circular Dichroism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006358:Hot Temperature; D008969:Molecular Sequence Data; D010843:Pichia / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010940:Plant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013025:Glycine max / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D055516:2S Albumins, Plant; D052179:Antigens, Plant; D005656:Fungal Proteins; D010940:Plant Proteins