Triggering Degradation of Cellulose Acetate by Embedded Enzymes: Accelerated Enzymatic Degradation and Biodegradation under Simulated Composting Conditions.

A green strategy that significantly accelerates the biodegradation rate of cellulose acetate (CA) by triggering deacetylation was demonstrated. Lipase isolated from Candida rugosa was immobilized on CA particles (immobilized lipase (IL)) by a physical entrapment method and further incorporated in CA films. After 40 days of aging in contact with external enzymes (lipase and cellulase), the number-average molecular weight ( M n ) of CA/IL 5% decreased by 88%, while the M n of CA only exhibited a 48% reduction. Fourier transform infrared and nuclear magnetic resonance spectroscopy of CA/IL 5% indicated significant deacetylation, which was further supported by the decrease of the water contact angle from 59 to 16°. These drastic changes were not observed for CA. Similar differences in the degradation rate were observed during aging under simulated composting conditions. After 180 days of simulated composting, traces of CA/IL 5% were barely observable, while large pieces of CA still remained. This could open the door to modified lignocellulose materials with retained biodegradability, also reducing the requirements for the degradation environment as the process is initiated from inside of the material.