Transformation of barley with antifungal protein genes

Anna-Maria Nuutila, R. Skadsen, B. Jones, H. Kaeppler

    Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review


    The serpins constitute a superfamily of proteins (~40 kDa) found in eukaryotes and some viruses. Most serpins are serine proteinase inhibitors, a few are cysteine proteinase inhibitors, and some are non-inhibitory. They are known to be involved in a large range of physiological processes in mammals - from blood coagulation and complement activation to hormone transport and chromatin folding - but the physiological functions of plant serpins are unknown (1). Serpins are abundant (2-3 mg/g grain) in barley endosperm and are the major antigens in beer (2,3). Active (uncleaved) barley serpins inhibit mammalian serine proteinases of the chymotrypsin family in vitro by forming 1:1 irreversible complexes (1). Inactive (cleaved) serpins are stable proteins resistant to boiling, extreme pH, and protease treatment. Barley serpins form heterodimers with b-amylase, and are assumed to influence beer foam stability and haze formation, and are thus of interest for the malting and brewing industry (3). As a part of a research project continuing to focus on the properties and functions of plant serpins, we have initiated immunomicroscopy studies to localize serpins in barley.
    Original languageEnglish
    Title of host publication2nd European Symposium on Enzymes in Grain Processing, ESEPG-2
    Place of PublicationEspoo
    PublisherVTT Technical Research Centre of Finland
    ISBN (Electronic)951-38-5707-7
    ISBN (Print)951-38-5706-9
    Publication statusPublished - 2000
    MoE publication typeNot Eligible
    EventEuropean Symposium on Enzymes in Grain Processing, ESEGP-2 - Helsinki, Finland
    Duration: 8 Dec 199910 Dec 1999

    Publication series

    SeriesVTT Symposium


    ConferenceEuropean Symposium on Enzymes in Grain Processing, ESEGP-2
    Abbreviated titleESEGP-2


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