The purpose of this research was to determine the effects of heating (including heating to ultra-high temperatures) homogenized ultrafiltered whole and skim milks on whey protein denaturation and milk's subsequent rennet coagulation properties: coagulation time, curd firmness, and microstructure. Whole and skim milk samples were ultrafiltered using a spiral wound ultrafiltration membrane system. Samples were preheated to 72°C for 58 s, held for 8 s then heated to 72, 89, 106, 123, or 140°C for more than 97 sand held for 4 s. The milk was then cooled to 60°C and homogenized, further cooled to 30°C, packaged into 120 ml sterile containers, and refrigerated overnight. Rennet coagulation time and curd firmness were monitored using a Formagraph . Milk and gel samples were fixed in 2.5% glutaraldehyde solution and examined by electron microscopy. Whey protein denaturation was determined by precipitating casein at pH 4.6 with .lN HCl and measuring protein content in the filtrate by the Kjeldahl procedure. Rennet coagulation time of milk increased as processing temperature was increased. Gel strength decreased with an increase in processing temperature. Ultrafiltration shortened rennet coagulation time and increased gel firmness. Ultra-high- temperature- heated whole and skim milks did not coagulate upon addition of rennet, but their concentrated counterparts did. Rennet coagulation of the concentrated milks was delayed by heating. Samples treated with ultra-high-temperature formed only a weak gel. The casein micelles in milk increased in size as a function of increasing processing temperature and concentration by ultrafiltration. Additional protein material adhered to the casein micelles after high-temperature processing and was especially noticeable in the samples treated with ultra-high-temperature. Whey protein denaturation increased as a function of increased heating temperature. The heated concentrated milks had higher levels of protein denaturation than the heated unconcentrated ones.