TY - JOUR
T1 - Functional screening pipeline to uncover laccase-like multicopper oxidase enzymes that transform industrial lignins
AU - Sharan, Anupama A.
AU - Bellemare, Annie
AU - DiFalco, Marcos
AU - Tsang, Adrian
AU - Vuong, Thu V.
AU - Edwards, Elizabeth A.
AU - Master, Emma R.
N1 - Funding Information:
The authors would like to acknowledge Mathieu Lavallee from Concordia University for support with heterologous production of multicopper oxidase enzymes presented in the study and Matthew Mascioni from the University of Toronto for development of R scripts used in ToF-SIMS data analysis. This work was supported by Genome Canada for the LSARP project “SYNBIOMICS – Functional genomics and techno-economic models for advanced biopolymer synthesis” (grant number 10405) and the NSERC CREATE for BioZone (grant number 528163).
Publisher Copyright:
© 2023
PY - 2024/2
Y1 - 2024/2
N2 - Laccase-like multicopper oxidases are recognized for their potential to alter the reactivity of lignins for application in value-added products. Typically, model compounds are employed to discover such enzymes; however, they do not represent the complexity of industrial lignin substrates. In this work, a screening pipeline was developed to test enzymes simultaneously on model compounds and industrial lignins. A total of 12 lignin-active fungal multicopper oxidases were discovered, including 9 enzymes active under alkaline conditions (pH 11.0). Principal component analysis revealed the poor ability of model compounds to predict enzyme performance on industrial lignins. Additionally, sequence similarity analyses grouped these enzymes with Auxiliary Activity-1 sub-families with few previously characterized members, underscoring their taxonomic novelty. Correlation between the lignin-activity of these enzymes and their taxonomic origin, however, was not observed. These are critical insights to bridge the gap between enzyme discovery and application for industrial lignin valorization.
AB - Laccase-like multicopper oxidases are recognized for their potential to alter the reactivity of lignins for application in value-added products. Typically, model compounds are employed to discover such enzymes; however, they do not represent the complexity of industrial lignin substrates. In this work, a screening pipeline was developed to test enzymes simultaneously on model compounds and industrial lignins. A total of 12 lignin-active fungal multicopper oxidases were discovered, including 9 enzymes active under alkaline conditions (pH 11.0). Principal component analysis revealed the poor ability of model compounds to predict enzyme performance on industrial lignins. Additionally, sequence similarity analyses grouped these enzymes with Auxiliary Activity-1 sub-families with few previously characterized members, underscoring their taxonomic novelty. Correlation between the lignin-activity of these enzymes and their taxonomic origin, however, was not observed. These are critical insights to bridge the gap between enzyme discovery and application for industrial lignin valorization.
KW - Kraft lignin
KW - Laccase
KW - Lignin-active enzymes
KW - Organosolv lignin
KW - ToF-SIMS
UR - http://www.scopus.com/inward/record.url?scp=85178102479&partnerID=8YFLogxK
U2 - 10.1016/j.biortech.2023.130084
DO - 10.1016/j.biortech.2023.130084
M3 - Article
C2 - 38000639
AN - SCOPUS:85178102479
SN - 0960-8524
VL - 393
JO - Bioresource Technology
JF - Bioresource Technology
M1 - 130084
ER -
