The effect of meat cooking on protein aggregation was measured in pig M. Longissimus dorsi. Muscles were aged 4 days in air and then cooked at 100 degrees C for 10 or 30 min. Meat was ground in a KCl solution and the whole extract was delipidated with a mixture of butanol and di-isopropyl ether in a 40:60 v/v ratio. Protein aggregation induced by cooking was evaluated with a laser granulometer, which enabled reliable and reproducible characterisation of particle size distributions, and particle shape distributions using automated imaging techniques. Cooking significantly decreased the level of big particles, while the number of small particles remained stable. Cooking also affected the form and size of the particles. In order to better understand the mechanisms implicated in the aggregation process the level of protein oxidation and the protein surface hydrophobicity were evaluated in parallel with the granulometry measurements. Significant correlations were observed between the granulometry parameters and some of the protein oxidation indices. The protein surface hydrophobicity was also correlated with the granulometry parameters demonstrating the impact of thermal denaturation on the aggregation process.