High molecular weight coffee melanoidins are inhibitors for matrix metalloproteases.

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 IC(50) values ranging between 0.2 and 1.1 mg/mL in vitro. The 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.

Imobilização da pancreatina em carvão ativado e em alumina para o preparo de hidrolisados de soro de leite / Immobilization of pancreatin in activated carbon and in alumina for preparing whey hydrolysates

Tendo como objetivo a redução de custos do processo de fabricação de hidrolisados protéicos, estudou-se neste trabalho a imobilização da pancreatina, por adsorção, em carvão ativado e em alumina. Para isso, foram testadas diferentes condições de imobilização (30, 60 e 90min a 25°C, e 12h a 5°C). Para verificar a taxa de imobilização, determinou-se indiretamente a enzima não adsorvida nos suportes. Ao se utilizar o carvão ativado, não foi observada diferença significativa entre as condições testadas, tendo-se obtido 100% de imobilização enzimática. Para a alumina, a melhor condição foi a de 90min, na qual se obteve 37% de imobilização. A medida do grau de exposição da fenilalanina, pela espectrofotometria derivada segunda, foi empregada para a determinação da estabilidade operacional da enzima, tendo sido mostrado que a imobilização em carvão ativado e em alumina permitiu a reutilização da pancreatina por até 5 vezes e 2 vezes, respectivamente.

Immobilization of pancreatin in activated carbon and in alumina was studied for producing protein hydrolysates, in order to reduce the process costs. Different immobilization conditions were tested (30, 60 and 90min at 25°C, and 12h at 5°C). For estimating the immobilization rate the amount of the non-adsorbed enzyme on the supports was indirectly determined. When activated carbon was used, no significant difference was observed among the tested conditions, obtaining 100% of enzymatic immobilization. In case of alumina, the best condition showed to be the 90min treatment which produced 37% of immobilization. The evaluation of the degree of exposition of phenylalanine, by second derivative spectrophotometry, was used for the determination of the enzyme operational stability, and showed that the immobilization in activated carbon and in alumina allowed the reusability of the pancreatin for 5 times and 2 times, respectively.