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An examination of the quinic acid utilization genes in Aspergillus niger reveals the involvement of two pH-dependent permeases

Author(s): Sgro M; Reid ID; Arentshorst M; Ram AFJ; Tsang A;

Many microorganisms are able to use plant-derived aromatic and cyclic compounds like the common plant secondary metabolite quinic acid as carbon and energy sources. In fungi, three enzymatic steps convert quinic acid into the common intermediate protocatech...

Article GUID: 40853219
Global survey of secondary metabolism in em Aspergillus niger /em via activation of specific transcription factors

Author(s): Semper C; Pham TTM; Ram S; Palys S; Evdokias G; Ouedraogo JP; Moisan MC; Geoffrion N; Reid I; Di Falco M; Bailey Z; Tsang A; Benoit-Gelber I...

Genomics analysis confirmed the status of filamentous fungi as a rich source of novel secondary metabolites; however, the discovery of these compounds is hampered by the cryptic nature of their bio...

Article GUID: 40852424
Fortifying the Rasamsonia emersonii secretome with recombinant cellobiohydrolase (GH7) for efficient biomass saccharification

Author(s): Raheja Y; Singh V; Gaur VK; Sharma G; Tsang A; Chadha BS;

GH7 cellobiohydrolases (CBH1s) are essential for depolymerizing crystalline cellulose, yet the hypercellulolytic thermophile Rasamsonia emersonii secretes them only in low amounts, leaving a gap in its native enzyme cocktail. To see whether a cognate CBH1 c...

Article GUID: 40622460
Heterologous Expression of Thermostable Endoglucanases from Rasamsonia emersonii: A Paradigm Shift in Biomass Hydrolysis

Author(s): Raheja Y; Singh V; Gaur VK; Tsang A; Chadha BS;

In this study, two thermostable endoglucanases (Rem_GH5EG and Rem_GH7EG) from Rasamsonia emersonii were heterologously expressed in Pichia pastoris and characterized to evaluate their potential for industrial biomass saccharification. Rem_GH5EG demonstrated...

Article GUID: 40418313
Title:Heterologous Expression of Thermostable Endoglucanases from Rasamsonia emersonii: A Paradigm Shift in Biomass Hydrolysis
Authors:Raheja Y,  Singh V,  Gaur VK,  Tsang A,  Chadha BS, 
Link:https://pubmed.ncbi.nlm.nih.gov/40418313/
DOI:10.1007/s12010-025-05258-5
Category:
PMID:40418313
Dept Affiliation: GENOMICS
1 Department of Microbiology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.
2 School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology, Ulsan, 44919, Republic of Korea.
3 Amity Institute of Biotechnology, Amity University Uttar Pradesh, Noida, India.
4 Center for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, QC, H4B 1R6, Canada.
5 Department of Microbiology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. chadhabs@yahoo.com.

Description:

In this study, two thermostable endoglucanases (Rem_GH5EG and Rem_GH7EG) from Rasamsonia emersonii were heterologously expressed in Pichia pastoris and characterized to evaluate their potential for industrial biomass saccharification. Rem_GH5EG demonstrated markedly superior catalytic efficiency toward barley ß-glucan (kcat/Km = 6.3 × 10-3/mg mL/min), while Rem_GH7EG exhibited a preference for carboxymethyl cellulose (kcat/Km = 1.17 × 10-3/mg mL/min). Notably, Rem_GH5EG showed optimal activity at 90 °C with a half-life (t1/2) of 2 h, whereas Rem_GH7EG was active at 70 °C with a half-life (t1/2) of 1 h, highlighting its suitability for high-temperature hydrolysis processes. Moreover, pre-conditioning of steam and acid pretreated unwashed rice straw slurry with Rem_GH5EG at 90 °C effectively reduced viscosity-related mass transfer limitations, thereby enhancing the hydrolytic efficiency of benchmark cellulase. These findings underscore the industrial relevance of Rem_GH5EG as the more promising candidate for developing efficient enzyme cocktails for biomass saccharification.