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 and Marcos J. C. Alcocer
Biochimica et Biophysica Acta (BBA) - Proteins & ProteomicsVolume 1698, Issue 2 , 6 May 2004, Pages 203-212
2004
บทคัดย่อ
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.