Category
Poster - Basic
Description
Increased production of fluorinated drugs and agrochemicals over the last few decades has resulted in many concerns over the disposition of fluorinated waste products in the environment. The functional attraction to these compounds arises due to the difficulty in breaking C-F bonds, enhancing stability, and therefore the utility, of these compounds for their desired use. It is this stability that has prompted the concern over the persistent nature of these compounds in the environment. Effective strategies for degrading fluorinated aromatic waste have been developed, however excessive cost of reagents and impractical logistics for use justify the search for novel and inexpensive approaches to the degradation of these environmental waste products. The work described in this study proposes a systematic approach to the identification of readily available and low-cost catalytic systems for degrading fluorinated phenolic derivatives. Through the use of a library screening method, several plant-based peroxidase catalysts have been identified with the ability to degrade mono and polyfluorinated phenolic compounds. Several of the samples identified have activities that equal or exceed that of horseradish peroxidase, which is the prototypic peroxidase enzyme used in nearly all biotechnological applications involving peroxidases. The much higher abundance of peroxidase enzyme in skin of pumpkins, butternut squash, acorn squash, yellow squash, spaghetti squash and zucchini, relative to horseradish root, suggests that these novel peroxidase enzymes may be a more cost effective and readily accessible catalyst for this type of waste treatment. Ultimately, an understanding of the kinetic properties of the enzymes identified in this study may direct future efforts aimed at developing more effective treatment strategies for these and other classes of environmental toxins, which is a long-range goal of this research.
Structural Comparison of Fluoro-phenolic Compound Degradation with Peroxidase Enzymes
Poster - Basic
Increased production of fluorinated drugs and agrochemicals over the last few decades has resulted in many concerns over the disposition of fluorinated waste products in the environment. The functional attraction to these compounds arises due to the difficulty in breaking C-F bonds, enhancing stability, and therefore the utility, of these compounds for their desired use. It is this stability that has prompted the concern over the persistent nature of these compounds in the environment. Effective strategies for degrading fluorinated aromatic waste have been developed, however excessive cost of reagents and impractical logistics for use justify the search for novel and inexpensive approaches to the degradation of these environmental waste products. The work described in this study proposes a systematic approach to the identification of readily available and low-cost catalytic systems for degrading fluorinated phenolic derivatives. Through the use of a library screening method, several plant-based peroxidase catalysts have been identified with the ability to degrade mono and polyfluorinated phenolic compounds. Several of the samples identified have activities that equal or exceed that of horseradish peroxidase, which is the prototypic peroxidase enzyme used in nearly all biotechnological applications involving peroxidases. The much higher abundance of peroxidase enzyme in skin of pumpkins, butternut squash, acorn squash, yellow squash, spaghetti squash and zucchini, relative to horseradish root, suggests that these novel peroxidase enzymes may be a more cost effective and readily accessible catalyst for this type of waste treatment. Ultimately, an understanding of the kinetic properties of the enzymes identified in this study may direct future efforts aimed at developing more effective treatment strategies for these and other classes of environmental toxins, which is a long-range goal of this research.
Comments
Undergraduate