Rhizobium bacteria was isolated from the root nodules of Medicago sativa plants and, based on morphological and some biochemical properties, it was characterized as Sinorhizobium meliloti. We studied the ability of this isolate, as well as that of Agrobacterium rhizogenes R1601, to produce the auxin  indole acetic acid (IAA). For purposes of control, both isolates, in the absence of tryptophan-L, were similarly tested. The identification of IAA was achieved by checking the colour reactions with Salkowski’s reagent. Low amounts (23, 69 and 26,77 µɡ/ml) of IAA were produced by S.meliloti and A.rhizogenes after 24 and 72 hours of incubation, respectively. S.meliloti was distinguished by the high production of this auxin (612µg/ml) when adding 0.1% tryptophan to the growth medium (YEM), as compared to the amount of its production by the other bacteria. Therefore, this isolation was used to determine the highest production of IAA at optimal conditions, which reached to 553,550 and 610,662 µg/ml in liquid YEM medium supported with tryptophan-L (both at 0.5 and 1.0%)  and a medium supported with glucose and lactose sugar (10%), after 72 hours of incubation, respectively. The 72-hour incubation period was better than that of 24-hour in obtaining an additional amount of IAA, which ranged between 0.6 and 0.7g/l. A spot of IAA produced by rhizobium bacteria was created corresponding to the standard spot of IAA in the thin layer chromatography (TLC) detection experiment.

The present research aimed to isolate and purify Alkaline phosphatase enzyme from crude protein extract (Lysate supernatant) of Escherichia coli, by using different biotechnologies. To proceed, the following steps were taken: Firstly, The verification of the existence of enzyme in bacteria, the bacteria were diagnosed by using the API 20 stripe that consists of (20) items. the enzyme was isolated to ensure its availability in bacteria within the logarithmic phase and this was done through proliferating them for 18 hours in a nutrient agar. It had been detected that the enzyme was intracellular because of the occurrence of enzyme activity in the lysate supernatant without occurring it in the cell free culture supernatant. Secondly, Enzyme purification, the enzyme had been purified through three stages: precipitation of protein by ammonium sulphate, dialysis and finally, the protein extract was passed through column chromatography by using Sephadex G-100 gel, the estimated enzyme activity after this step was 22.0 in comparison with its activity before the purification processes (crude protein extract). The approximate molecular weight of alkaline phosphatase was 81.000 Dalton estimated by using gel filtration technique.