Identification of fungal lignocellulose-degrading biocatalysts secreted by Phanerochaete chrysosporium via activity-based protein profiling

Schmerling, Christian; Sewald, Leonard; Heilmann, Geronimo; Witfeld, Frederick; Begerow, Dominik; Jensen, Kenneth; Bräsen, Christopher; Kaschani, Farnusch; Overkleeft, Herman S.; Siebers, Bettina; Kaiser, Markus

doi:10.1038/s42003-022-04141-x

Cited by 5 publications

(3 citation statements)

References 93 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The isolated fungus was identified as Phanerochaete chrysosporium. According to other studies, P. chrysosporium has been isolated from decayed woods (Hervé et al 2016;Schmerling et al 2022). Based on previous investigations, the potential of white-rot fungus P. chrysosporium to create ligninolytic enzymes such as manganese peroxidases (MnPs) and lignin peroxidases (LiPs) was documented (Singh and Chen 2008;van der Made et al 2023).…”

Section: Resultsmentioning

confidence: 99%

Nanoparticles enhanced ligninolytic enzymes activity of rotten wood fungus Phanerochaete chrysosporium

Al-Rajhi,

Alharbi,

Alsalamah

et al. 2024

BioRes

View full text Add to dashboard Cite

White-rot fungi are vital microorganisms that can decay lignocellulosic biomass. This study investigated the ability of white-rot fungus found on rotten wood to produce ligninolytic enzymes and their enhancement using nanoparticles (NPs). Phanerochaete chrysosporium was isolated from decayed wood. Its ability to produce ligninolytic enzymes, namely CMCase, FPase, Laccase, and MnPase, was recorded. The enzymes’ productivity was enhanced via utilization of the surfactant polysorbate 80 with optimum concentration 0.20 mL/L for maximum CMCase (201.33 ± 2.31 U/mL) and FPase (66.33 ± 0.58 U/mL), whereas the corresponding value was 0.15 mL/L for laccase and MnPase production. Mn2O3NPs and CuONPs enhanced the enzymes’ productivity but with different levels according to their concentrations, where the maximum productivity of CMCase (220.67 ± 2.31 U/mL) and (FPase 74.63 ± 3.51 U/mL) were at 50 ppm, but MnPase (0.52 ± 0.01 U/mL) and laccase (2.88 ± 0.01U/mL) were at 25 ppm and 75 ppm of CuONPs, respectively. Mn2O3NPs at 75 ppm enhanced the productivity of CMCase (219.33 ± 1.15 U/mL) and FPase (74.63 ± 3.51U/mL); but at 25 ppm and 75 ppm enhanced the productivity of laccase (2.40 ± 0.04U/mL) and MnPase (0.73 ± 0.03 U/mL), respectively. Thus, NPs were found to play a vital role in improving the productivity of ligninolytic enzymes.

show abstract

Section: Resultsmentioning

confidence: 99%

Nanoparticles enhanced ligninolytic enzymes activity of rotten wood fungus Phanerochaete chrysosporium

Al-Rajhi,

Alharbi,

Alsalamah

et al. 2024

BioRes

View full text Add to dashboard Cite

show abstract

“…ABPP is based on small-molecule probes, which bind specifically to enzyme active sites and ‘tag’ them with different reporter molecules [ 77–83 ]. The strength of ABPP as an enzyme discovery tool lies in direct identification of novel enzymes, which have no sequence similarity to known biocatalysts [ 84 , 85 ]. In the field of drug discovery, the application of ABPP was highly successful in recent years [ 86 ].…”

Section: Discovery Of Extremophilic Enzymes For Polyester Recyclingmentioning

confidence: 99%

Harnessing extremophilic carboxylesterases for applications in polyester depolymerisation and plastic waste recycling

Williams

Khusnutdinova

et al. 2023

Essays in Biochemistry

View full text Add to dashboard Cite

The steady growth in industrial production of synthetic plastics and their limited recycling have resulted in severe environmental pollution and contribute to global warming and oil depletion. Currently, there is an urgent need to develop efficient plastic recycling technologies to prevent further environmental pollution and recover chemical feedstocks for polymer re-synthesis and upcycling in a circular economy. Enzymatic depolymerization of synthetic polyesters by microbial carboxylesterases provides an attractive addition to existing mechanical and chemical recycling technologies due to enzyme specificity, low energy consumption, and mild reaction conditions. Carboxylesterases constitute a diverse group of serine-dependent hydrolases catalysing the cleavage and formation of ester bonds. However, the stability and hydrolytic activity of identified natural esterases towards synthetic polyesters are usually insufficient for applications in industrial polyester recycling. This necessitates further efforts on the discovery of robust enzymes, as well as protein engineering of natural enzymes for enhanced activity and stability. In this essay, we discuss the current knowledge of microbial carboxylesterases that degrade polyesters (polyesterases) with focus on polyethylene terephthalate (PET), which is one of the five major synthetic polymers. Then, we briefly review the recent progress in the discovery and protein engineering of microbial polyesterases, as well as developing enzyme cocktails and secreted protein expression for applications in the depolymerisation of polyester blends and mixed plastics. Future research aimed at the discovery of novel polyesterases from extreme environments and protein engineering for improved performance will aid developing efficient polyester recycling technologies for the circular plastics economy.

show abstract

“…ABPP has been successfully applied to study a wide range of biological processes and diseases, making it a valuable tool for both basic research and drug discovery. Recent advances in proteomics have expanded the scope of ABPP, enabling its application in a variety of areas, from the study of different enzyme classes, such as kinases, 5 proteases, 6 glycosidases, 7 phosphatases, 8 and oxidoreductases, 9 to cell imaging 10 (Figure 1). ABPP has significantly enhanced our understanding of enzyme activity in various physiological and pathological processes on a proteome-wide scale.…”

mentioning

confidence: 99%

Mapping the Evolution of Activity-Based Protein Profiling: A Bibliometric Review

Porta¹

2023

Adv Pharm Bull

View full text Add to dashboard Cite

Activity-based protein profiling (ABPP) is a chemoproteomic approach that employs small-molecule probes to directly evaluate protein functionality within complex proteomes. This technology has proven to be a potent strategy for mapping ligandable sites in organisms and has significantly impacted drug discovery processes by enabling the development of highly selective small-molecule inhibitors and the identification of new therapeutic molecular targets. Despite being nearly a quarter of a century old as a chemoproteomic tool, ABPP has yet to undergo a bibliometric analysis. In order to gauge its scholarly impact and evolution, a bibliometric analysis was performed, comparing all 1,919 reported articles with the articles published in the last five years. Through a comprehensive data analysis, including a 5-step workflow, the most influential articles were identified, and their bibliometric parameters were determined. The 1,919 analyzed articles span from 1999 to 2022, providing a comprehensive overview of the historical and current state of ABPP research. This analysis presents, for the first time, the characteristics of the most influential ABPP articles, offering valuable insight into the research conducted in this field and its potential future directions. The findings underscore the crucial role of ABPP in drug discovery and novel therapeutic target identification, as well as the need for continued advancements in the development of novel chemical probes and proteomic technologies to further expand the utility of ABPP.

show abstract

Identification of fungal lignocellulose-degrading biocatalysts secreted by Phanerochaete chrysosporium via activity-based protein profiling

Cited by 5 publications

References 93 publications

Nanoparticles enhanced ligninolytic enzymes activity of rotten wood fungus Phanerochaete chrysosporium

Nanoparticles enhanced ligninolytic enzymes activity of rotten wood fungus Phanerochaete chrysosporium

Harnessing extremophilic carboxylesterases for applications in polyester depolymerisation and plastic waste recycling

Mapping the Evolution of Activity-Based Protein Profiling: A Bibliometric Review

Contact Info

Product

Resources

About