Cellulase production by Neurospora crassa on wheat straw

Romero, M.D.; Aguado, J.; González, Leandro; Ladero, Miguel

doi:10.1016/s0141-0229(99)00035-6

Cited by 116 publications

(50 citation statements)

References 14 publications

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“…Neurospora crassa produced 0.23 UmL −1 of FPase when it was cultivated in liquid medium with 1% wheat straw as carbon source [41]. On the other hand, higher FPase production, 5 U.mL −1 , was reported by Yamanobe [27] using A. cellulolyticus strain grown in a liquid medium with 4% of cellulose powder as carbon source.…”

Section: Enzymes Productionmentioning

confidence: 90%

Cellulases and Hemicellulases from Endophytic Acremonium Species and Its Application on Sugarcane Bagasse Hydrolysis

Almeida

Guimarães

Bischoff

et al. 2011

Appl Biochem Biotechnol

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The aim of this work was to have cellulase activity and hemicellulase activity screenings of endophyte Acremonium species (Acremonium zeae EA0802 and Acremonium sp. EA0810). Both fungi were cultivated in submerged culture (SC) containing L -arabinose, D -xylose, oat spelt xylan, sugarcane bagasse, or corn straw as carbon source. In solid-state fermentation, it was tested as carbon source sugarcane bagasse or corn straw. The highest FPase, endoglucanase, and xylanase activities were produced by Acremonium sp. EA0810 cultivated in SC containing sugarcane bagasse as a carbon source. The highest β-glucosidase activity was produced by Acremonium sp. EA0810 cultivated in SC using D -xylose as carbon source. A. zeae EA0802 has highest α-arabinofuranosidase and α-galactosidase activities in SC using xylan as a carbon source. FPase, endoglucanase, β-glucosidase, and xylanase from Acremonium sp. EA0810 has optimum pH and temperatures of 6.0, 55 °C; 5.0, 70 °C; 4.5, 60 °C; and 6.5, 50 °C, respectively. α-Arabinofuranosidase and α-galactosidase from A. zeae EA0802 has optimum pH and temperatures of 5.0, 60 °C and 4.5, 45 °C, respectively. It was analyzed the application of Acremonium sp. EA0810 to hydrolyze sugarcane bagasse, and it was achieved 63% of conversion into reducing sugar and 42% of conversion into glucose.

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Section: Enzymes Productionmentioning

confidence: 90%

Cellulases and Hemicellulases from Endophytic Acremonium Species and Its Application on Sugarcane Bagasse Hydrolysis

Almeida

Guimarães

Bischoff

et al. 2011

Appl Biochem Biotechnol

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“…Many N. crassa isolates have been recovered from sugar cane, which is closely related to Miscanthus, an attractive crop for biofuel production (6)(7)(8). Although it was shown to degrade cellulose Ͼ30 years ago (9,10), relatively little has been reported on plant biomass utilization by N. crassa. The N. crassa genome is predicted to contain twice as many cellulases as H. jecorina (11), as well as many hemicellulases and other enzymes involved in plant biomass degradation.…”

mentioning

confidence: 99%

Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa

Tian

Beeson

Iavarone

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

286

347

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The filamentous fungus Neurospora crassa is a model laboratory organism, but in nature is commonly found growing on dead plant material, particularly grasses. Using functional genomics resources available for N. crassa, which include a near-full genome deletion strain set and whole genome microarrays, we undertook a systemwide analysis of plant cell wall and cellulose degradation. We identified approximately 770 genes that showed expression differences when N. crassa was cultured on ground Miscanthus stems as a sole carbon source. An overlap set of 114 genes was identified from expression analysis of N. crassa grown on pure cellulose. Functional annotation of up-regulated genes showed enrichment for proteins predicted to be involved in plant cell wall degradation, but also many genes encoding proteins of unknown function. As a complement to expression data, the secretome associated with N. crassa growth on Miscanthus and cellulose was determined using a shotgun proteomics approach. Over 50 proteins were identified, including 10 of the 23 predicted N. crassa cellulases. Strains containing deletions in genes encoding 16 proteins detected in both the microarray and mass spectrometry experiments were analyzed for phenotypic changes during growth on crystalline cellulose and for cellulase activity. While growth of some of the deletion strains on cellulose was severely diminished, other deletion strains produced higher levels of extracellular proteins that showed increased cellulase activity. These results show that the powerful tools available in N. crassa allow for a comprehensive system level understanding of plant cell wall degradation mechanisms used by a ubiquitous filamentous fungus.cellulase ͉ secretome ͉ transcriptome

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“…For most cellulose degradation processes, the hydrolysis of cellulose requires the synergetic action of three major enzymes: endo-1,4-β-glucanase (EC3.2.1.4), exoglucanase (EC3.2.1.91), and β-glucosidase [2]. Exoglucanases catalyze the degradation of crystalline cellulose at the ends of the polysaccharide chains, whereas cellulose chains are attacked internally by endoglucanases.…”

mentioning

confidence: 99%

A Novel Cold-Active and Alkali-Stable β-Glucosidase Gene Isolated from the Marine Bacterium Martelella mediterranea

Mao

Hong

Shao

et al. 2010

Appl Biochem Biotechnol

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A β-glucosidase gene designated gluc3m was cloned through construction of a genomic library of Martelella mediterranea 2928. The gluc3m consisted of 2,496 bp and encoded a peptide of 832 amino acids that shared the greatest amino acid similarity (59%) with a β-glucosidase of family 3 glycoside hydrolase from Agrobacterium radiobacter K84. The optimum reaction temperature and pH of Gluc3M were 45 °C and 8.0, respectively. The K (m) and V (max) for p-nitrophenyl-β-D: -glucopyranoside were 0.18 mg/ml and 196.08 µmol/min/mg enzyme, respectively. Gluc3M was found to be highly alkali stable, retaining 80% of its maximum enzymatic activity after treatment with pH 11.0 buffers for 24 h. Furthermore, the activity of Gluc3M improved remarkably in the presence of univalent metal ions, whereas it was inhibited in the presence of divalent ions. Gluc3M also exhibited significant activities toward various substrates including pNPGlu, pNPGal, salicin, and konjac powder. It is important to note that Gluc3M is a cold-active enzyme that showed over 50% of the maximum enzymatic activity at 4 °C. SWISS-MODEL revealed that the amino acids near the conserved domain SDW of Gluc3M contributed to the cold-active ability. Based on these characteristics, Gluc3M has the potential for use in additional studies and for industrial applications.

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Cellulase production by Neurospora crassa on wheat straw

Cited by 116 publications

References 14 publications

Cellulases and Hemicellulases from Endophytic Acremonium Species and Its Application on Sugarcane Bagasse Hydrolysis

Cellulases and Hemicellulases from Endophytic Acremonium Species and Its Application on Sugarcane Bagasse Hydrolysis

Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa

A Novel Cold-Active and Alkali-Stable β-Glucosidase Gene Isolated from the Marine Bacterium Martelella mediterranea

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