Purification, cloning and characterisation of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense

Gusakov, Alexander V.; Sinitsyn, A. P.; Salanovich, T. N.; Bukhtojarov, F. E.; Марков, А. В.; Ustinov, Boris B.; Zeijl, Cora van; Punt, Peter J.; Burlingame, Richard P.

doi:10.1016/j.enzmictec.2004.03.025

Cited by 77 publications

(50 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Saha (2004) reported pH range 4.0-7.0 optimum for activity of CMCase from M. circinelloides. Cellulases produced from Chrysosporium lucknowense and A. fumigatus were found stable at pH 5.0 (Gusakov et al 2005;Sherief et al 2010).…”

Section: Characterization Of Cellulasesmentioning

confidence: 97%

Enzymatic saccharification of pretreated rice straw by cellulases from Aspergillus niger BK01

et al. 2017

View full text Add to dashboard Cite

Alkali-assisted acid pretreated rice straw was saccharified using cellulase from Aspergillus niger BK01. The cellulase production by the fungus was enhanced by parametric optimization using solid-state fermentation conditions. Maximum cellulase production (12.0 U/gds of carboxymethyl cellulase, CMCase) was achieved in 96 h, using 6.0% substrate concentration, 7.5% inoculum concentration, 1:2 solid to liquid ratio, at pH 5.5, and temperature 28°C, by supplementation of the fermentation medium with 0.1% carboxymethylcellulose and 0.1% ammonium nitrate. Characterization of crude cellulases showed that highest CMCase activity was observed at pH 4.8 and temperature 40°C. The CMCase was stable from pH 4.8-5.5 and at a temperature range of 35-50°C. The pretreated biomass was subjected to hydrolysis with the fungal cellulases. The saccharification optimization studies showed that 2% (v/v) enzyme concentration and hydrolysis time of 2.5 h were optimum for maximum yield, i.e, 23.78% sugars and 35.96% saccharification value.

show abstract

Section: Characterization Of Cellulasesmentioning

confidence: 97%

Enzymatic saccharification of pretreated rice straw by cellulases from Aspergillus niger BK01

et al. 2017

View full text Add to dashboard Cite

show abstract

“…In 2007, mixtures of thermostable enzymes, including cellulases from Thermoascus auranticus, Thrichoderma reseei, Acremonium thermophilum and Thermoascus auranticus, have been produced by ROAL, Finland (Viikari et al, 2007). Multienzyme mixtures were also reconstituted using purified Chrysosporium lucknowense enzymes (Gusakov et al, 2005). Despite the noticeable advantages of thermostable enzymes, cultivation of thermophiles and hyperthermophyles requires special and expensive media, and it is hampered by the low specific growth rates and product inhibition (Krahe et al, 1996;Schiraldi et al, 2002;Turner et al, 2007).…”

Section: Enzymes For the Cellulose Liquefaction: Thermophilic Enzymesmentioning

confidence: 99%

Hydrolysis of Lignocellulosic Biomass: Current Status of Processes and Technologies and Future Perspectives

Verardi¹,

De²,

Ricca³

et al. 2012

Bioethanol

View full text Add to dashboard Cite

“…Hydrolysis at higher temperatures with increased enzyme activity could reduce the costs associated with producing ethanol from biomass by reducing reaction time and required enzyme loading. Much work has been done to improve the thermostability of cellulases and other hydrolytic enzymes at temperatures above 508C (Ai and Wilson, 2002;Gusakov et al, 2005;Voutilainen et al, 2007). In a conversion plant employing a separate hydrolysis and fermentation scheme, each step can operate at its optimum temperature, making enzymes active at 508C or higher important for efficient hydrolysis (Tengborg et al, 2001).…”

Section: Hydrolytic Activitymentioning

confidence: 99%

An optimized microplate assay system for quantitative evaluation of plant cell wall–degrading enzyme activity of fungal culture extracts

King

Donnelly

Bergstrom

et al. 2008

Biotech & Bioengineering

138

102

View full text Add to dashboard Cite

Developing enzyme cocktails for cellulosic biomass hydrolysis complementary to current cellulase systems is a critical step needed for economically viable biofuels production. Recent genomic analysis indicates that some plant pathogenic fungi are likely a largely untapped resource in which to prospect for novel hydrolytic enzymes for biomass conversion. In order to develop high throughput screening assays for enzyme bioprospecting, a standardized microplate assay was developed for rapid analysis of polysaccharide hydrolysis by fungal extracts, incorporating biomass substrates. Fungi were grown for 10 days on cellulose-or switchgrass-containing media to produce enzyme extracts for analysis. Reducing sugar released from filter paper, Avicel, corn stalk, switchgrass, carboxymethylcellulose, and arabinoxylan was quantified using a miniaturized colorimetric assay based on 3,5-dinitrosalicylic acid. Significant interactions were identified among fungal species, growth media composition, assay substrate, and temperature. Within a small sampling of plant pathogenic fungi, some extracts had crude activities comparable to or greater than T. reesei, particularly when assayed at lower temperatures and on biomass substrates. This microplate assay system should prove useful for high-throughput bioprospecting for new sources of novel enzymes for biofuel production.

show abstract

Purification, cloning and characterisation of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense

Cited by 77 publications

References 40 publications

Enzymatic saccharification of pretreated rice straw by cellulases from Aspergillus niger BK01

Enzymatic saccharification of pretreated rice straw by cellulases from Aspergillus niger BK01

Hydrolysis of Lignocellulosic Biomass: Current Status of Processes and Technologies and Future Perspectives

An optimized microplate assay system for quantitative evaluation of plant cell wall–degrading enzyme activity of fungal culture extracts

Contact Info

Product

Resources

About