Characterization and pulp refining activity of a Paenibacillus campinasensis cellulase expressed in Escherichia coli

Ko, Chun-Han; Tsai, Chien-Chung; Lin, Ping; Chang, Ko-Cheng; Tu, Jenn; Wang, Ya-Nang; Yang, Chenming

doi:10.1016/j.biortech.2010.05.043

Cited by 36 publications

(26 citation statements)

References 32 publications

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“…The pH stability of the CMCase produced by Bacillus sp. strain C1AC5507 over a broad pH range seems to be a common characteristic of many Bacillus CMCases (Ko et al, 2010).…”

Section: Resultsmentioning

confidence: 99%

PRODUCTION AND CHARACTERIZATION OF THERMOPHILIC CARBOXYMETHYL CELLULASE SYNTHESIZED BY Bacillus sp. GROWING ON SUGARCANE BAGASSE IN SUBMERGED FERMENTATION

Padilha

Carvalho

Dias

et al. 2015

Braz. J. Chem. Eng.

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-The production and characterization of cellulase from thermophilic strain Bacillus sp. C1AC5507 was studied. For enzyme production, sugarcane bagasse was used as carbon source. The produced carboxymethyl cellulase (CMCase) had a molecular weight around 55 kDa and its activity varied between 0.14 and 0.37 IU mL -1 in conditions predicted by Response Surface Methodology. The optimum temperature and pH for the CMCase production were 70 °C and 7.0, respectively. The enzyme activity was inhibited mostly by Cu +2 and activated mostly by Co +2 , Mn 2+ , Ca +2 and Fe +3 . Our findings provide a contribution to the use of natural wastes such as sugarcane bagasse as substrate for growth and production of thermophilic CMCase. Further optimization to increase the production of cellulase enables the use in industrial applications.

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“…The pH stability of the CMCase produced by Bacillus sp. strain C1AC5507 over a broad pH range seems to be a common characteristic of many Bacillus CMCases (Ko et al, 2010).…”

Section: Resultsmentioning

confidence: 99%

PRODUCTION AND CHARACTERIZATION OF THERMOPHILIC CARBOXYMETHYL CELLULASE SYNTHESIZED BY Bacillus sp. GROWING ON SUGARCANE BAGASSE IN SUBMERGED FERMENTATION

Padilha

Carvalho

Dias

et al. 2015

Braz. J. Chem. Eng.

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“…When refining increased freeness decreased by 36%, WRV increased by 7.9%, and tensile index improved by 43.4%. Ko (2010) studied the refining effects on BKP with two cellulases enzymes, one produced by Paenibacillus campinasensis and the other one a commercial product named FiberCare®. FiberCare® is an enzymatic formulation in which endoglucanase (carboxyl methyl cellulose) predominates; the enzyme protein content in the product is 6 mg/mL.…”

Section: Chemical Pulpsmentioning

confidence: 99%

Enzymatic approaches in paper industry for pulp refining and biofilm control

Torres

Negro

Fuente

et al. 2012

Appl Microbiol Biotechnol

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The use of enzymes has a high potential in the pulp and paper industry to improve the economics of the paper production process and to achieve, at the same time, a reduced environmental impact. Specific enzymes contribute to reduce the amount of chemicals and energy required for the modification of fibers and helps to prevent the formation or development of biofilms. This review is aimed at presenting the latest progresses made in the application of enzymes as refining aids and biofilm control agents.

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“…Fermentable sugars are used as a renewable energy source to produce bioethanol. They also improve paper web formation and flexibility in the pulp and paper industry [12].…”

Section: Cel5amentioning

confidence: 99%

“…In particular, they have been used in the degradation of agricultural wastes and can be converted into soluble sugars, alcohol, and other chemicals. Since converting cellulosic wastes to glucose has a global significance, cellulases play an important role for achieving benefits of biomass utilization [12,14,16]. Fermentable sugars are used as a renewable energy source to produce bioethanol.…”

Section: Cel5amentioning

confidence: 99%

Gene Cloning of Endoglucanase Cel5A from Cellulose-Degrading Paenibacillus xylanilyticus KJ-03 and Purification and Characterization of the Recombinant Enzyme

et al. 2012

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The bacterial strain Paenibacillus xylanilyticus KJ-03 was isolated from a sample of soil used for cultivating Amorphophallus konjac. The cellulase gene, cel5A was cloned using fosmid library and expressed in Escherichia coli BL21 (trxB). The cel5A gene consists of a 1,743 bp open reading frame and encodes 581 amino acids of a protein. Cel5A contains N-terminal signal peptide, a catalytic domain of glycosyl hydrolase family 5, and DUF291 domain with unknown function. The recombinant cellulase was purified by Ni-affinity chromatography. The cellulase activity of Cel5A was detected in clear band with a molecular weight of 64 kDa by zymogram active staining. The maximum activity of the purified enzyme was displayed at a temperature of 40 °C and pH 6.0 when carboxymethyl cellulose was used as a substrate. It has 44% of its maximum activity at 70 °C and retained 66% of its original activity at 45 °C for 1 h. The purified cellulase hydrolyzed avicel, CMC, filter paper, xylan, and 4-methylumbelliferyl β-D-cellobiose, but no activity was detected against p-nitrophenyl β-D-glucoside. The end products of the hydrolysis of cellotetraose and cellopentaose by Cel5A were detected by thin layer chromatography, while enzyme did not hydrolyze cellobiose and cellotriose.

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Characterization and pulp refining activity of a Paenibacillus campinasensis cellulase expressed in Escherichia coli

Cited by 36 publications

References 32 publications

PRODUCTION AND CHARACTERIZATION OF THERMOPHILIC CARBOXYMETHYL CELLULASE SYNTHESIZED BY Bacillus sp. GROWING ON SUGARCANE BAGASSE IN SUBMERGED FERMENTATION

PRODUCTION AND CHARACTERIZATION OF THERMOPHILIC CARBOXYMETHYL CELLULASE SYNTHESIZED BY Bacillus sp. GROWING ON SUGARCANE BAGASSE IN SUBMERGED FERMENTATION

Enzymatic approaches in paper industry for pulp refining and biofilm control

Gene Cloning of Endoglucanase Cel5A from Cellulose-Degrading Paenibacillus xylanilyticus KJ-03 and Purification and Characterization of the Recombinant Enzyme

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