Aug 2026· Catalysts· Vol 16, pp. 720· 0 citations· 52 references
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.
Lignocellulosic biomass deconstruction requires robust biocatalysts capable of operating under demanding industrial conditions. The thermophilic fungus Myceliophthorathermophila is a promising biotechnological platform for cellulase production and lignocellulose valorization because of its naturally thermostable CAZyme repertoire. Extensive knowledge has accumulated across diverse research fields, alongside its taxonomic reclassification as Thermothelomyces thermophila, emphasizing the need to integrate findings across research contexts. This review synthesizes knowledge generated using publicly available M. thermophila strains, retaining the historically prevalent name M. thermophila to facilitate cross-disciplinary comparison. Emphasis is placed on the C1 strain, whose longstanding use as a production platform provides a foundation for current advances in strain engineering and protein production. We provide a genetics-focused perspective on this biotechnological platform, integrating advances in genetic engineering, transcriptional regulation, and protein production. We discuss CRISPR systems applied to M. thermophila, strategies to improve protein production through extracellular protease elimination, optimization of secretion and unfolded protein response pathways, carrier proteins, and synthetic expression systems. We further summarize the transcriptional regulation of cellulase expression, the repertoire of characterized thermostable cellulases, and opportunities for protein engineering. Collectively, these advances position M. thermophila as a versatile biotechnological platform for producing industrial enzymes and other value-added bioproducts for biorefinery applications.
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