Document Type
Article
Rights
Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence
Disciplines
1. NATURAL SCIENCES, Biochemistry and molecular biology, Biochemical research methods, Bioremediation, 2.9 INDUSTRIAL BIOTECHNOLOGY, Biocatalysis, Bioplastics
Abstract
An extracellular lipase from Amycolatopsis mediteranei (AML) with potential applications in process biotechnology was recently cloned and examined in this laboratory. In the present study, the 3D structure of AML was elucidated by comparative modelling. AML lacked the ‘lid’ structure observed in most true lipases and shared similarities with plastic degrading enzymes. Modelling and substrate specificity studies showed that AML was a cutinase with a relatively exposed active site and specificity for medium chain fatty acyl moieties.
AML rapidly hydrolysed the aliphatic plastics poly(ε-caprolactone) and poly(1,4-butylene succinate) extended with 1,6-diisocyanatohexane under mild conditions. These plastics are known to be slow to degrade in landfill. Poly(L-lactic acid) was not hydrolysed by AML, nor was the aromatic plastic Polyethylene Terephthalate (PET). The specificity of AML is partly explained by active site topology and analysis reveals that minor changes in the active site region can have large effects on substrate preference. These findings show that extracellular Amycolatopsis enzymes are capable of degrading a wider range of plastics than is generally recognised. The potential for application of AML in the bioremediation of plastics is discussed.
DOI
https://doi.org/10.1016/j.csbj.2021.01.019
Recommended Citation
Tan, Y., Kinsella G.K., Henehan G.T., Ryan B.J. (2021). An extracellular lipase from Amycolatopsis mediterannei is a cutinase with plastic degrading activity. Computational and Structural Biotechnology Journal, 19, 869-879.
Funder
DIT/TU Dublin
Publication Details
Tan, Y., Kinsella G.K., Henehan G.T., Ryan B.J. (2021). An extracellular lipase from Amycolatopsis mediterannei is a cutinase with plastic degrading activity. Computational and Structural Biotechnology Journal, 19, 869-879.
doi:10.1016/j.csbj.2021.01.019