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Poly(lactic acid) Degradation by Recombinant Cutinases from Aspergillus nidulans
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Researchers identified three cutinase enzymes from the fungus Aspergillus nidulans capable of degrading poly(lactic acid), with the top performer ANCUT1 releasing up to 25.86 mM lactic acid and achieving a 46% weight reduction, demonstrating strong enzymatic potential for breaking down biodegradable plastic packaging waste.
Poly(lactic-acid) (PLA) is a biodegradable polymer widely used as a packaging material. Its monomer, lactic acid, and its derivatives have been used in the food, cosmetic, and chemical industries. The accumulation of PLA residues leads to the development of green degrading methodologies, such as enzymatic degradation. This work evaluates the potential use of three cutinolytic enzymes codified in the Aspergillus nidulans genome to achieve this goal. The results are compared with those obtained with proteinase K from Tritirachium album, which has been reported as a PLA-hydrolyzing enzyme. The results show that all three cutinases act on the polymer, but ANCUT 1 releases the highest amount of lactic acid (25.86 mM). Different reaction conditions assayed later led to double the released lactic acid. A decrease in weight (45.96%) was also observed. The enzyme showed activity both on poly L lactic acid and on poly D lactic acid. Therefore, this cutinase offers the potential to rapidly degrade these package residues, and preliminary data show that this is feasible.
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