Biorefinery of Lignocellulosic Biomass, 2nd Edition

A special issue of Fermentation (ISSN 2311-5637). This special issue belongs to the section "Industrial Fermentation".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 593

Special Issue Editor


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Guest Editor
State Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong University, Jinan, China
Interests: cellulase; saccharification; filamentous fungus; strain improvement; fermentation
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Special Issue Information

Dear Colleagues,

Lignocellulosic biomass is the most abundant and renewable material worldwide, thus making it a viable alternative to fossil fuels. Recent economic, energy, and even social–political factors have boosted the integral valorization of lignocellulosic biomass to facilitate moving from today’s fossil-based economy toward a bio-based economy. Biorefinery is the sustainable utilization of lignocellulosic biomass in a spectrum of commercial products, including biofuels and platform chemicals, to guarantee the highest profitability. However, there are still significant barriers in pretreatment, hydrolysis, and fermentation and its down-streaming processes, which have made commercialization difficult. The potent strains for the production of efficient enzymes and value-added byproducts are far from being thoroughly exploited. Optimization of feedstock pretreatment, enzymatic saccharification, and sugar fermentation, together with integrated bioprocesses, remain the key to a biorefineries-based circular bioeconomy. Thus, a multidisciplinary approach to the valorization of lignocellulosic biomass would substantially accelerate progress in modern biorefineries and facilitate achieving commercial sustainability.

The present Special Issue aims to collect and publish both recent research results and review papers in the area of biorefineries based on lignocellulose for the production of biofuels and value-added byproducts. Actual studies addressing challenges in pretreatment, saccharification, fermentation, and integrated bioprocesses are of interest, but recent advances in the development of novel enzymes and microbial strains are also welcomed. If you would like to submit a review article, please contact one of the editors to discuss the relevance of the topic before writing your submission.

Prof. Dr. Yaohua Zhong
Guest Editor

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Keywords

  • biorefinery
  • lignocellulosics
  • biofuels
  • value-added biochemicals
  • integrated bioprocess
  • pretreatment
  • cellulases
  • enzymatic hydrolysis
  • fermentable sugars
  • strain improvement

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Research

16 pages, 2948 KiB  
Article
High-Level Expression of β-Glucosidase in Aspergillus niger ATCC 20611 Using the Trichoderma reesei Promoter Pcdna1 to Enhance Cellulose Degradation
by Jingjing Chang, Juan Wang, Zhihong Li, Lu Wang, Peng Lu, Yaohua Zhong and Hong Liu
Fermentation 2024, 10(9), 461; https://doi.org/10.3390/fermentation10090461 - 5 Sep 2024
Viewed by 301
Abstract
β-glucosidase is a key component of cellulase for its function in hydrolyzing cellobiose to glucose in the final step of cellulose degradation. The high-level expression of β-glucosidase is essential for cellulose conversion. Aspergillus niger ATCC 20611 has the potential for efficient protein expression [...] Read more.
β-glucosidase is a key component of cellulase for its function in hydrolyzing cellobiose to glucose in the final step of cellulose degradation. The high-level expression of β-glucosidase is essential for cellulose conversion. Aspergillus niger ATCC 20611 has the potential for efficient protein expression because of its ability to secret enzymes for the industrial production of fructooligosaccharides, but it lacks robust promoters for high-level protein expression. Here, the development of A. niger 20611 as a powerful protein expression system exploited the conserved constitutive promoter Pgpd1 of the glyceraldehyde-3-phosphate dehydrogenase-encoding gene from Trichoerma reesei to drive the expression of the enhanced green fluorescent protein in A. niger ATCC 20611. The mycelium of the transformant AGE9 exhibited intense fluorescence. Then, the promotor Pgpd1 was used to drive the expression of β-glucosidase and the enzyme activity of transformants AGB1 and AGB33 were 1.02 and 0.51 U/mL, respectively. These results demonstrate that the promotor Pgpd1 from T. reesei was applicable for A. niger ATCC 20611. Furthermore, the T. reesei-specific robust promoter Pcdna1 was used to drive the expression of β-glucosidase. The β-glucosidase exhibited a high-level expression with a yield of 15.2 U/mL, which was over 13.9 times higher than that driven by the promoter Pgpd1. The β-glucosidase was thermally stable and accounted for 85% of the total extracellular proteins. Subsequently, the fermentation broth including β-glucosidase was directly added to the cellulase mixture of T. reesei for saccharification of the acid-treated corncob residues and the delignified corncob residues, which increased the saccharification efficiency by 26.21% and 29.51%, respectively. Thus, β-glucosidase exhibited a high level of expression in A. niger ATCC 20611 and enhanced cellulose degradation by addition in vitro. In addition, the robust promoter Pcdna1 of T. reesei could drive the high-level expression of protein in A. niger ATCC 20611. These results demonstrate that the promoters in filamentous fungi could be employed across species in A. niger ATCC 20611 and further facilitated the efficient expression of β-glucosidase to optimize cellulases for efficient cellulose transformation. Full article
(This article belongs to the Special Issue Biorefinery of Lignocellulosic Biomass, 2nd Edition)
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