The influence of biochar (biomass-derived black carbon) on crop growth and nutrient uptake varies based on the rate of biochar applied with fertilisers. We investigated the effect of deep-banded oil mallee biochar at different rates (0, 1.5, 3.0, and 6 t/ha) with 2 types of fertiliser (non-inoculated MultiMAPS® at 30 or 55 kg/ha; inoculated Western Mineral Fertiliser at 100 kg/ha) on wheat growth at a farmer’s field in a low rainfall area of Western Australia. Wheat yield increased significantly when biochar was applied with inoculated fertiliser and 30 kg/ha non-inoculated fertiliser. Mycorrhizal colonisation in wheat roots increased significantly with biochar application with inoculated mineral fertiliser. Mycorrhizal hyphae may have improved water supply to reduce drought stress in these treatments by extending crop exploration of water from the wide inter-rows. Grain yield increases were due to better grain survival and grain fill with reduced drought stress. Early stage phosphorus uptake was not improved by mycorrhizal colonisation—phosphorus supply from the soil and applied fertiliser was already adequate. The residual effect of biochar and mineral fertilisers was assessed using a mycorrhizal bioassay for soil collected from the field trial 2 years after application of biochar. Biochar and both fertilisers increased mycorrhizal colonisation in clover bioassay plants. Deep-banded biochar provided suitable conditions for mycorrhizal fungi to colonise plant roots.

Sucrose and Percoll density gradient centrifugation were used to separate organelles from the central zone tissue of cowpea (Vigna unguiculata L. Walp. cv Vita 3: Bradyrhizobium strain CB 756) nodules. Enzyme activity analysis has shown that both plastids and mitochondria have a full complement of enzymes for de novo purine synthesis. In vitro activities of individual component enzymes (glycinamide ribonucleotide synthetase, EC 6.3.4.13; glycinamide ribonucleotide transformylase, EC 2.1.2.2; aminoimidazole ribonucleotide synthetase, EC 6.3.3.1; aminoimidazole carboxamide ribonucleotide transformylase, EC 6.3.2.6; and adenylosuccinate-AMP lyase, EC 4.3.2.2) as well as of the whole purine pathway (from ribose-5-phosphate to inosine monophosphate) were similar in the two organelles. No significant cytosolic or bacteroidal activity of any of the purine pathway enzymes was detected on assay. These findings are contrary to earlier studies (M.J. Boland, K.R. Schubert [1983] Arch Biochem Biophys 220: 179–187; B.J. Shelp C.A. Atkins, P.J. Storer, D.T. Canvin [1983] Arch Biochem Biophys 224: 429–441) that concluded that enhanced expression of purine synthesis in nodules of ureide-forming species is localized to plastids. Significantly increased recovery of activity of key pathway enzymes (particularly of labile aminoimidazole ribonucleotide synthetase) coupled with improved assay methods and the use of Percoll in addition to sucrose for gradient centrifugation have together contributed to much higher reaction rates and more definitive analyses of particulate fractions.