Engineering Lignin-Binding Catabolic Nanocompartments for Enhanced Biomass Degradation

Author

• Gwyneth Mary GeigerFollow

Publication Date

Summer 7-28-2026

Abstract

Controlled burning is an efficient way to eliminate lignocellulosic biomass; however, it has a risk of causing unintentional wildfires. Lignin is a naturally occurring organic polymer that is notoriously difficult to degrade. Current lignin depolymerization methods often rely on harsh chemicals, high-energy inputs, or inefficient biological processes. We created a recombinant fusion elastin-like polypeptide (ELP) based system that combines the ELP, a lignin-binding domain, and a small laccase. This fusion protein is called SLAC1.LB2-80. The lignin-binding domain binds to lignin, increasing enzyme-substrate interactions and improving catalytic efficiency. We hypothesize that the fusion protein, which undergoes reversible phase separation, can assemble around lignin to form dynamic coacervate compartments that enhance the efficiency of laccase degradation. Here, we present the expression of the fusion protein, characterize its phase behavior, and study its interactions with lignin. Additionally, we covalently attach the mediator TEMPO to our lignin-binding peptide LB2-80 and study its interactions with lignin, combined with the SLAC1.LB2-80 fusion protein.

Language

English

Keywords

lignin transformation, Enzymatic degradation, catalytic coacervates, Fusion Protein, Elastin-like polypeptide, liquid-liquid phase separation

Document Type

Thesis

Degree Name

Biomedical Engineering

Level of Degree

Masters

Department Name

Biomedical Engineering

First Committee Member (Chair)

Gabriel P. López

Second Committee Member

Nick Carroll

Third Committee Member

Telmo Díez Pérez

Fourth Committee Member

David Peabody

Recommended Citation

Geiger, Gwyneth Mary. "Engineering Lignin-Binding Catabolic Nanocompartments for Enhanced Biomass Degradation." (2026). https://digitalrepository.unm.edu/bme_etds/55