Burkholderia lata BL02 Galactolipase as an Important Biocatalyst for Plant Biomass Deconstruction and Sugar Ester Synthesis
TL;DR
Findings support the role of galactolipases as accessory enzymes and highlight their potential application in integrated and sustainable biorefinery processes.
Abstract
The transition toward sustainable biorefinery processes requires efficient strategies for lignocellulosic biomass deconstruction and valorization. In this study, an integrated enzymatic system combining fungal holocellulases and laccases with a bacterial galactolipase was developed and evaluated. The consortium, composed of Trametes hirsuta GMA-01, Mycothermus thermophilus CBS 619.91, and Burkholderia lata BL02, was produced using agro-industrial substrates and applied to the hydrolysis of different lignocellulosic biomasses. The incorporation of galactolipase activity enhanced the saccharification yields for leaf-derived substrates, reaching up to 292.0 mg/g for spinach leaves and 236.0 mg/g for corn straw, compared to fungal systems alone. This effect is associated with the selective hydrolysis of membrane-associated galactolipids, improving substrate accessibility to holocellulolytic enzymes. Proteomic analysis confirmed the partial identification of the BL02 enzyme as an ester hydrolase, while structural modeling based on homologous Burkholderia lipases provided preliminary insights into features that may be compatible with the accommodation of bulky polar substrates. In addition, the enzyme catalyzed the synthesis of sugar fatty acid esters with conversion yields above 50% for glucose and xylose in binary solvent systems. These findings support the role of galactolipases as accessory enzymes and highlight their potential application in integrated and sustainable biorefinery processes.