October 7, 2011

High molecular weight coffee melanoidins are inhibitors for matrix metalloproteases

L M De Marco et al, High molecular weight coffee melanoidins are inhibitors for matrix metalloproteases, Journal of Agricultural and Food Chemistry, 2011, published online ahead of print.


High-molecular (above 10 kDa) melanoidins isolated from coffee beans of varying roasting degree were found to be efficient inhibitors for the zinc-containing matrix metalloproteases MMP-1, MMP-2 and MMP-9 with IC50 values ranging 0.2 and 1.1 mg/ml in vitro. Inhibitory potential increased with roasting degree. No or only slight inhibition of other zinc-containing peptidases closely related to MMPs, namely Clostridium histolyticum collagenase and angiotensin converting enzyme, was found, indicating specific structural features of melanoidins to be responsible for the interaction with MMPs. A continuous increase on the apparent molecular weight of melanoidins as well as incorporation of phenolic substances into the melanoidin structure with progress of roasting was observed, concomitant with a significant increase in the carbon/nitrogen of the melanoidins. This suggests that the melanoidins are mainly formed by incorporation of carbohydrates and phenolic compounds onto a proteinaceous backbone. As MMP-1, MMP-2 and MMP-9 play a pivotal role in pathogenesis of colorectal cancer, studies on possible physiological effects of melanoidins are mandatory.

Modtag nyhedsbrev

Ja tak, jeg vil gerne modtage nyhedsbrev, når der er noget nyt om kaffe og helbred.