Ultrafiltration resulted in excellent purity and high yield of collagen for both the germ and endosperm extracts. Filtration using a 100 kDa molecular weight cut off (MWCO) membrane resulted in complete retention of collagen, whereas the 300 kDa MWCO membrane showed significant loss of collagen throughout the filtration. For the 100 kDa membrane, no significant difference in the sieving of either the host cell proteins, GFP or rhCollagen occurred under different conditions of crossflow rate and TMP; however, a significant increase in the permeate flux was observed at higher crossflow and TMP. Additionally, increasing the pH resulted in a significant decrease in the sieving of host cell proteins while pH had no effect on GFP sieving. Filtrations performed in concentration mode were able to achieve collagen concentrations as high as 1 mg/ml without any observed sieving. These results indicate that ultrafiltration can be used to obtain a high purity when separating large proteins from corn extracts.&'
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