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Multi copper oxidase from Micrococcus sp. IITD107, a promising candidate for polypropylene biodegradation
Summary
A novel multi-copper oxidase enzyme from Micrococcus sp. IITD107 achieved approximately 16% degradation of untreated commercial polypropylene strips within 24 hours at 60°C, confirmed by FTIR and SEM showing surface modification and breakdown into alkanes and aldehydes. This is the first report of enzymatic polypropylene degradation without pretreatment, representing a significant advance for bioremediation of one of the most abundant and persistent microplastic polymers in the environment.
Polypropylene (PP) is the second most abundantly used synthetic plastic which poses challenges in degradation due to its structural stability. There are limited reports on enzymatic biodegradation of PP. Here, we report degradation of commercial PP strips without any pre-treatment by a novel multi copper oxidase (MCO) from Micrococcus sp. IITD107. The molecular docking and simulation analysis revealed strong binding of MCO with PP. The purified enzyme and the whole cell lysate from recombinant E. coli expressing MCO, exhibited around 16% and 6.8% decrease (w/w), respectively in PP within 24 h at 60 ˚C. Changes in the functional groups and surface modification of PP were observed by FTIR, NMR and SEM. The biodegradation by-products identified were alkanes, aldehydes, ketones and a few carboxylic acids. This is the first report demonstrating the biodegradation of PP by MCO without any pre-treatment, suggesting this to have a significant role for PP degradation.