Effect of Protein Hydrolysates on Pancreatic Cancer Cells

Effect of Fish Protein Hydrolysates on Pancreatic Cancer Cells Carlo G. Ossum1, Lisa Lystbæk Andersen2, Henrik Hauch Nielsen2, Else K. Hoffmann1, and Flemming Jessen2 1University of Copenhagen, Department of Biology, Denmark, 2Technical University of Denmark (DTU), National Food Institute, Denmark Corresponding author: Carlo G. Ossum ([email protected]) A large number of bioactive peptides have been identified in and isolated from various food sources. Milk seems to be a particularly rich source but also different fish species have been found to yield bioactive peptides. Bioactive peptides, usually consisting of 3 to 20 amino acids, can be released from proteins upon degradation by proteolytic enzymes, e.g. in the intestinal tract. The numerous described bioactivities include antihypertensive, anticancerous, antimicrobial, and immunomodulating effects. Here, we investigate the effect of fish protein hydrolysates obtained by enzymatic hydrolysis on cancer cell proliferation. Skin and belly flap muscle from trout were hydrolysed with the unspecific proteases Alcalase, Neutrase, or UE1 (all from Novozymes, Bagsværd, Denmark) to a hydrolysis degree of 1-15%. The hydrolysates were tested for biological activities affecting cell proliferation and ability to modulate caspase activity in pancreatic cancer cells COLO357 and BxPC-3 in vitro. A number of the hydrolysates showed caspase promoting activity; in particular products containing muscle tissue, i.e. belly flap, were able to stimulate caspase activity. Selected hydrolysis products were further fractionated by ultrafiltration into molecular sizes above and below 5 kDa and their activity and dose-dependence was tested.