Improvement of homologous GH10 xylanase production by deletion of genes with predicted function in the <i>Aspergillus nidulans</i> secretion pathway

Zubieta, Mariane Paludetti; Gerhardt, Jaqueline Aline; Rubio, Marcelo Ventura; Terrasan, César Rafael Fanchini; Persinoti, Gabriela Félix; Antoniel, Everton Paschoal; Contesini, Fabiano Jares; Prade, Rolf A.; Damásio, André

doi:10.1111/1751-7915.13556

Cited by 9 publications

(3 citation statements)

References 44 publications

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“…2 A, the optimum pH for WT and its mutants was 4.0 or 4.5. This result was similar to that of GH10 xylanase obtained from most fungi, such as Penicillium canescens [ 19 ], Trichoderma reesei [ 20 ], and Aspergillus nidulans [ 21 ]. The relative activities of the enzymes did not differ significantly in the same pH environment.…”

Section: Resultssupporting

confidence: 82%

Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries

You

Zha

et al. 2021

Biotechnol Biofuels

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Background Xylanase, an important accessory enzyme that acts in synergy with cellulase, is widely used to degrade lignocellulosic biomass. Thermostable enzymes with good catalytic activity at lower temperatures have great potential for future applications in the feed and fuel industries, which have distinct demands; however, the potential of the enzymes is yet to be researched. Results In this study, a structure-based semi-rational design strategy was applied to enhance the low-temperature catalytic performance of Bispora sp. MEY-1 XYL10C_∆N wild-type (WT). Screening and comparisons were performed for the WT and mutant strains. Compared to the WT, the mutant M53S/F54L/N207G exhibited higher specific activity (2.9-fold; 2090 vs. 710 U/mg) and catalytic efficiency (2.8-fold; 1530 vs. 550 mL/s mg) at 40 °C, and also showed higher thermostability (the melting temperature and temperature of 50% activity loss after 30 min treatment increased by 7.7 °C and 3.5 °C, respectively). Compared with the cellulase-only treatment, combined treatment with M53S/F54L/N207G and cellulase increased the reducing sugar contents from corn stalk, wheat bran, and corn cob by 1.6-, 1.2-, and 1.4-folds, with 1.9, 1.2, and 1.6 as the highest degrees of synergy, respectively. Conclusions This study provides useful insights into the underlying mechanism and methods of xylanase modification for industrial utilization. We identified loop2 as a key functional area affecting the low-temperature catalytic efficiency of GH10 xylanase. The thermostable mutant M53S/F54L/N207G was selected for the highest low-temperature catalytic efficiency and reducing sugar yield in synergy with cellulase in the degradation of different types of lignocellulosic biomass. Graphic Abstract

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Section: Resultssupporting

confidence: 82%

Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries

You

Zha

et al. 2021

Biotechnol Biofuels

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“…Recently, several strategies have been developed to improve protein production by A. nidulans . For instance, when the Hsp40 co-chaperone ydjA gene was knocked out, xylanase XlnE production increased by 171% [ 45 ]. A. nidulans production of cellulase production was improved in the Δ pkaA (protein kinase A) strain [ 46 ].…”

Section: Discussionmentioning

confidence: 99%

Development of an auto-inducible expression system by nitrogen sources switching based on the nitrogen catabolite repression regulation

et al. 2022

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Background The construction of protein expression systems is mainly focused on carbon catabolite repression and quorum-sensing systems. However, each of these regulatory modes has an inherent flaw, which is difficult to overcome. Organisms also prioritize using different nitrogen sources, which is called nitrogen catabolite repression. To date, few gene regulatory systems based on nitrogen catabolite repression have been reported. Results In this study, we constructed a nitrogen switching auto-inducible expression system (NSAES) based on nitrogen catabolite regulation and nitrogen utilization in Aspergillus nidulans. The PniaD promoter that is highly induced by nitrate and inhibition by ammonia was used as the promoter. Glucuronidase was the reporter protein. Glucuronidase expression occurred after ammonium was consumed in an ammonium and nitrate compounding medium, achieving stage auto-switching for cell growth and gene expression. This system maintained a balance between cell growth and protein production to maximize stress products. Expressions of glycosylated and secretory proteins were successfully achieved using this auto-inducible system. Conclusions We described an efficient auto-inducible protein expression system based on nitrogen catabolite regulation. The system could be useful for protein production in the laboratory and industrial applications. Simultaneously, NSAES provides a new auto-inducible expression regulation mode for other filamentous fungi.

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“…Filamentous fungi are important resources for large-scale enzyme production. However, the production level is low and this limitation stimulates the research on gene manipulations [ 65 ]. The heterologous expression is reported as an alternative to increase the production of enzymes.…”

Section: A Nidulans An Ideal Fungus For Exprmentioning

confidence: 99%

Aspergillus nidulans: A Potential Resource of the Production of the Native and Heterologous Enzymes for Industrial Applications

Kumar

2020

International Journal of Microbiology

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Aspergillus nidulans is a filamentous fungus that is a potential resource for industrial enzymes. It is a versatile fungal cell factory that can synthesize various industrial enzymes such as cellulases, β-glucosidases, hemicellulases, laccases, lipases, proteases, β-galactosidases, tannases, keratinase, cutinases, and aryl alcohol oxidase. A. nidulans has shown the potential to utilize low-cost substrates such as wheat bran, rice straw, sugarcane bagasse, rice bran, coir pith, black gram residue, and chicken feathers to produce enzymes cost-effectively. A. nidulans has also been known as a model organism for the production of heterologous enzymes. Several studies reported genetically engineered strains of A. nidulans for the production of different enzymes. Native as well as heterologous enzymes of A. nidulans have been employed for various industrial processes.

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Improvement of homologous GH10 xylanase production by deletion of genes with predicted function in the Aspergillus nidulans secretion pathway

Cited by 9 publications

References 44 publications

Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries

Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries

Development of an auto-inducible expression system by nitrogen sources switching based on the nitrogen catabolite repression regulation

Aspergillus nidulans: A Potential Resource of the Production of the Native and Heterologous Enzymes for Industrial Applications

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