Román-Morales's Lab. Progress Results

Use of Enzymes to Degrade Dichloro-diphenyl-trichloroethane (DDT):

Agricultural products have been affected by the excessive use of pesticides. Dichloro-diphenyl-trichloroethane (DDT) is the activate ingredient used in insecticide commercial products like Chlorophenothane®, Guesarol®, and Digmar®. Excessive use of this pesticide brought negative physiological effects such as cancer, seizures, vomits, tremors (in humans) and effects on the nervous system, kidney, liver, and immune system (in animals). It was banned in most continents due to its toxicity and degradation chain involving dichloro-diphenyl-dichloroethane (DDD) and dichloro-diphenyl-dichloroethylene (DDE), which are products of high toxicity. Microorganisms have been frequently used as a method for the degradation of DDT and other pesticides in soil. Domínguez et. al. showed that the use of White-rot fungi in soil accelerates the degradation of DDT. He suggests that the accelerated degradation is due to enzymatic ligninolytic activity, specifically Laccase and peroxidases.  This project proposal focuses on developing a method to increase the degradation of DDT, and their related products, by taking advantage and enhancing the ligninolytic activity of enzymes such as, horseradish peroxidase and Laccase.  The degradation process of DDT, when exposed to Laccase and/or Horseradish Peroxidase, will be analyzed by following the change in absorbance of its maximum absorption band in Ultraviolet-Visible Spectroscopy (UV-VIS) and correlating it to its change in concentration during the process. The expected outcomes are that the enzymes will degrade the pesticide without the need of a host and that it will be functional on other pesticides. The longterm goal is to use enzymes as a method to increase the degradation of DDT in soil and provide a safe & ecofriendly solution to the agricultural station.