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Tobacco ( Nicotiana tabacum cv. Bright Yellow 2) cells as an effective bioreactor for the production of puroindolines
Author(s) -
Sorrentino Angela,
Iannaccone Marco,
Palumbo Daniela,
Capparelli Rosanna,
Porta Raffaele,
Mariniello Loredana
Publication year - 2009
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20080084
Subject(s) - nicotiana tabacum , apoplast , recombinant dna , endosperm , biology , botany , chemistry , biochemistry , cell wall , gene
PINs (puroindolines) are two small proteins so‐called because of the presence of a hydrophobic tryptophan‐rich domain. Associated with wheat ( Triticum aestivum ) starch granules, PINs have been shown to be responsible for the softness of the wheat endosperm. Moreover, they have been proved to possess bactericidal and antifungal properties, together with the capacity to form very stable foams. All these features make PINs very attractive for medical, pharmaceutical and food‐industrial applications. The aim of the present study was to explore a plant molecular‐farming approach for producing a recombinant PIN. Three specific recombinant constructs, aimed at expression in the apoplast and chloroplast compartments, were prepared and used for transformation of tobacco ( Nicotiana tabacum cv. Bright Yellow 2) cells. Recombinant PINB (puroindoline B) targeted to the chloroplast was obtained as 0.35% of BY‐2‐cell total soluble proteins. Antimicrobial‐activity experiments demonstrated that, at the minimum inhibitory concentration, recombinant PINB is responsible for about 91% growth inhibition of Escherichia coli .