Phenolic Profiles of Ten Australian Faba Bean Varieties.

Although Australia is the largest exporter of faba bean globally, there is limited information available on the levels of bioactive compounds found in current commercial faba bean varieties grown in this country. This study profiled the phenolic acid and flavonoid composition of 10 Australian faba bean varieties, grown at two different locations. Phenolic profiling by HPLC-DAD revealed the most abundant flavonoid to be catechin, followed by rutin.

A proteomic approach to the identification and characterisation of protein composition in wheat germ.

Proteome analyses were carried out on commercial wheat germ of mature grain from the biscuit-making wheat cultivar, Rosella. Wheat germ protein extracts were fractionated by two-dimensional gel electrophoresis across two different immobilised pH gradients: pH 4.0-7.

Genes active in developing wheat endosperm.

This paper describes the construction and characterisation of a cDNA library from wheat endosperm tissue during the early stages of grain filling. Developing wheat endosperm tissue was characterised with respect to standard measures including dry weight, cytological appearance and timing of expression of major sources of mRNA such as the seed storage protein genes. In addition, the full complement of proteins present at mid-endosperm development was examined using 2D-electrophoretic techniques.

The wheat-grain proteome as a basis for more efficient cultivar identification.

The wheat-grain proteome was investigated, as a basis for devising more efficient methods of cultivar identification or discrimination. Australian wheats (Halberd, Cranbrook, CD87 and Katepwa) were used as the basis of this study. These cultivars were selected on the basis of differences in the quality types represented, in terms of dough-processing attributes that can suit one cultivar better than another for specific types of industrial utilisation.

Expression and purification of recombinant human indoleamine 2, 3-dioxygenase.

Indoleamine 2,3-dioxygenase, the first and rate-limiting enzyme in human tryptophan metabolism, has been implicated in the pathogenesis of many diseases. The human enzyme was expressed in Escherichia coli EC538 (pREP4) as a fusion protein to a hexahistidyl tag and purified to homogeneity in terms of electrophoretic and mass spectroscopic analysis, by a combination of phosphocellulose and nickel-agarose affinity chromatography. The yield of the fusion protein was 1.