Enzymatic Hydrolysis of Triacetin and L-Lactide in Emulsified Microparticles Within a Cellulose Hydrogel Dispersion

Triacetin (TA) is a solvent commonly used in pharmaceutical and food applications, and as a plasticizer in bioplastics such as poly(lactic acid) (PLA) and cellulose acetate (CA). L-lactide is the monomer used in the ring-opening polymerization of PLA. The structure of TA emulsions stabilized by a cellulose hydrogel (CH) was imaged in this study. The emulsions were prepared by mechanical homogenization or a two-step process with subsequent high-pressure homogenization (HPH). The two-step process yielded smaller TA droplets and a more homogeneous CH dispersion. The images demonstrate that emulsion stabilization is due to CH particles adsorbed at the TA-water interface. The ester hydrolysis of TA and a lactide/TA solution by two industrially important lipases, from Candida rugosa (CRL) and Burkholderia cepacia (BCL), was investigated, assessing the effect of CH as an emulsion stabilizer. Mechanically homogenized TA emulsions were effectively hydrolyzed. Lactide was found to inhibit the enzymatic hydrolysis of TA. This inhibition was mitigated by CH for CRL-catalyzed hydrolysis but not for BCL catalysis. These results indicate a synergistic effect of CH stabilization on the interfacial activation of CRL. Thise effect may also be relevant for the biodegradation of bio-derived plastics and their fibrous cellulose composites.