<p style="text-align: justify;"><b>Nutritional Data</b></p>

<p style="text-align: justify;">The levels of proximates (moisture, ash, fat, protein, total dietary fibre, and carbohydrates) were determined in samples of grain, straw, and various processed fractions (<i>e.g.,</i> rice hulls, brown rice, parboiled brown rice, polished rice, rice flour, rice bran, bran oil) from LLRICE62 and LLRICE06 (sprayed and unsprayed with glufosinate ammonium herbicide) and found to be within the normal range reported in the literature for commercial rice varieties. The amino acid and fatty acid profiles of grain from these transgenic varieties were similar to those of non-transgenic control varieties tested at the same time, and comparable to values reported in the scientific literature.</p>

<p style="text-align: justify;">Rice contains a small number of antinutritional factors that are concentrated in the bran fraction and which, except for phytic acid, are subject to heat denaturation (inactivation). These antinutrients include: phytic acid, which is a storage form of phosphorus in plant seeds but also chelates calcium, zinc, iron, and magnesium in the digestive tract of animals thus interfering with absorption of these nutrients; trypsin inhibitor; and lectins, which are a class of proteins with specific binding affinities for particular carbohydrate moieties present on glycoproteins present in cell walls and cell plasma membranes, and have been associated with a range of antinutritive effects and some disease pathologies.</p>

<p style="text-align: justify;">The levels of trypsin inhibitor and lectins in non-transgenic and transgenic LLRICE06 rough grain were reported to be below the limit of detection, and the phytic acid content did not vary significantly between transgenic and non-transgenic varieties.</p>

<p style="text-align: justify;">The lack of any changes to nutritional composition and quality were also confirmed in a 42-day male broiler chicken feeding study.</p>

<p style="text-align: justify;"><b>Toxicity</b></p>

<p style="text-align: justify;">The PAT enzyme does not have the characteristics of a toxin. It is specific for L?phosphinothricin and has no homology to proteins other than to similar PAT encoding genes from other organisms. In summary, no adverse effects were predicted given that the PAT enzyme is a minor constituent of human and animal food</p>

<p style="text-align: justify;"><b>Allergenicity</b></p>

<p style="text-align: justify;">Searches of public amino acid sequence databases did not reveal any homologies between the deduced amino acid sequence of the introduced PAT protein and sequences of known toxins or allergens. The PAT enzyme does not exhibit the characteristics of an allergen. The PAT enzyme is both heat and acid labile, and looses 100% of its activity after cooking for 30 minutes at 75C. The enzyme is also inactivated after 30 minutes at a pH level of 4 or less. Should cooking not destroy the enzyme, it would be subject to oral ingestion by humans and subsequent rapid digestion. It was shown that PAT was degraded within minutes in simulated gastric juices.</p>
