Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.).

Two new members of the polyketide synthase (PKS) gene family (RiPKS4 and RiPKS5) were cloned from raspberry fruits (Rubus idaeus L., cv Royalty) and expressed in Escherichia coli. Characterization of the recombinant enzyme products indicated that RiPKS4 is a bifunctional polyketide synthase producing both 4-hydroxybenzalacetone and naringenin chalcone.

Aroma production by tissue cultures.

Although plant tissue cultures have been in use for the past hundred years, adapting them for the production of aroma compounds started only in the 1970s. The use of tissue cultures in aroma production has its advantages, because plant cells, unlike whole plants, are not limited to geographic locations or the seasons. Cell mass can be doubled relatively rapidly and can be induced for the production of compounds in a coordinated manner.

Response of scab-susceptible (McIntosh) and scab-resistant (Liberty) apple tissues to treatment with yeast extract and Venturia inaequalis.

Yeast extract and Venturia inaequalis treated intact scab-susceptible (McIntosh) and scab-resistant (Liberty) apple plants and their organs were analyzed for phenolic metabolites. The major phenolic compounds found in both non-treated and treated leaves were phloridzin and phloretin which accumulated in mM concentrations. Untreated and treated stems and roots contained only phloridzin as the major detectable metabolite during the course of the investigation.

Molecular and biochemical characterization of three aromatic polyketide synthase genes from Rubus idaeus.

Three polyketide synthase genes (PKS1, PKS2, PKS3) from cell suspension cultures of raspberry (Rubus idaeus L. cv. Royalty) were characterized.

Characterization of a new IgE-binding 35-kDa protein from birch pollen with cross-reacting homologues in various plant foods.

The present investigation was undertaken to obtain molecular data of a new immunoglobulin (Ig)E-binding birch pollen protein with a mass of 35 kDa. In a previous study, this protein showed IgE cross-reactivity with 34- and 35-kDa proteins in apples, pears, carrots, bananas and other exotic fruits. Since the protein was N-terminally blocked, it was purified by preparative SDS-PAGE, and multiple proteolytic fragments were subsequently generated by in-gel digestion with the endoproteinases Glu C, Lys C and Clostripain.