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The problem of refolding and reassembling recombinant vicilin subunits
Author(s) -
Chambers Stephen J,
Carr Helen J,
Plumb Geoffrey W,
Lambert Nigel
Publication year - 1990
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740520112
Subject(s) - vicilin , yeast , saccharomyces cerevisiae , sativum , recombinant dna , phaseolus , legumin , biochemistry , biology , storage protein , pisum , chemistry , botany , gene
The reassociation of a storage protein (pea (Pisum sativum L) vicilin) expressed in yeast (Saccharomyces cerevisiae MC16 (ade 2–1, leu 2–3, lys 2–1, his 4–712 FS , SUF 2)) was investigated. The corresponding protein in French, bean (Phaseolus vulgaris L), termed phaseolin, was used as a model to produce a methodology for the refolding of the recombinant protein. Phaseolin was successfully renatured from its dissociated state in 5 M guanidinium chloride. Application of this rationale to yeast‐derived vicilin proved unsuccessful. The nature of the yeast vicilin and its failure to refold and reassemble correctly are discussed together with the further experimental approaches required.