Enzymatic Hydrolysis of Triacetin and L-Lactide in Emulsified Microparticles Within a Cellulose Hydrogel Dispersion
Margarita Antonenko, Gilad Alfassi, Dmitry M. Rein, Yachin Cohen
TL;DR
This study examines how cellulose hydrogel stabilizes emulsions and affects enzyme activity during the breakdown of triacetin and lactide.
Contribution
The study reveals a synergistic effect of cellulose hydrogel on the interfacial activation of Candida rugosa lipase during enzymatic hydrolysis.
Findings
Emulsions prepared with a two-step process had smaller triacetin droplets and a more uniform cellulose hydrogel dispersion.
L-lactide inhibited enzymatic hydrolysis of triacetin, but this was mitigated by cellulose hydrogel for Candida rugosa lipase.
Cellulose hydrogel stabilization enhanced the interfacial activation of Candida rugosa lipase but not Burkholderia cepacia lipase.
Abstract
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.…
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Taxonomy
Topicsbiodegradable polymer synthesis and properties · Nanocomposite Films for Food Packaging · Enzyme Catalysis and Immobilization