Team:UC Davis/Data/Cutinase Activity

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Cutinase Activity

As of now, through our p-nitrophenyl butyrate assays we have gathered enough data to determine that our LC-Cutinase part (BBa_K936000) exhibits its intended function as an esterase. Unfortunately it has been much more difficult to characterize than expected as we have been unable to purify the protein successfully.

References

1. Silva C, et al. 2011. Engineered Thermobifida fusca cutinase with increased activity on polyester substrates. Biotechnol. J. 6:1230–1239.
2. S. Sulaiman, S. Yamato, E. Kanaya, J. Kim, Y. Koga, K. Takano, S. Kanaya. "Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach." Applied and Environment Microbiology, vol. 78 no. 5, pp. 1556-1562, March 2012.
3. Ö. Faiz et al. Determination and characterization of thermostable esterolytic activity from a novel thermophilic bacterium Anoxybacillus gonensis J. Biochem. Mol. Biol., 40 (2007), pp. 588–594

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