Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001

Hwang, In Taek; Lim, Hee Nam; Song, Ha Young; Cho, Soo-Jin; Chang, Jong‐San; Park, No‐Joong

doi:10.1016/j.biotechadv.2010.05.007

Cited by 33 publications

(17 citation statements)

References 45 publications

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“…Cloned xylanase KRICT PX1 from Paenibacillus sp. HPL-001 has shown maximum activity at pH 5Á5 and 9Á5 at 50 and 45°C, respectively (Hwang et al 2010).…”

Section: Effect Of Ph and Temperature On Xylanase Activitymentioning

confidence: 99%

Xylanases of Bacillus spp. isolated from ruminant dung as potential accessory enzymes for agro-waste saccharification

Thite

Nerurkar

2015

Lett Appl Microbiol

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The uncontrolled use of fossil fuels and concerns about its future availability, have invoked interest over unconventional alternative energy sources like solar, hydropower, geothermal, nuclear and biomass. Plants, being largest renewable biomass on earth, have received consideration as a source of biofuels. Ruminant dung isolates M35, R31 and J208 belonging to Bacillus sp. produces majorly endo-xylanase when induced with wheat bran. Such plant cell wall degrading endo-xylanases with broad pH optima and mesophilic nature can act as accessory enzymes with cellulases to enhance the saccharification of plant biomass in biofuel industries.

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“…Cloned xylanase KRICT PX1 from Paenibacillus sp. HPL-001 has shown maximum activity at pH 5Á5 and 9Á5 at 50 and 45°C, respectively (Hwang et al 2010).…”

Section: Effect Of Ph and Temperature On Xylanase Activitymentioning

confidence: 99%

Xylanases of Bacillus spp. isolated from ruminant dung as potential accessory enzymes for agro-waste saccharification

Thite

Nerurkar

2015

Lett Appl Microbiol

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“…Fungi such as Trichoderma reesei and Aspergillus niger are common sources of plant-hydrolyzing enzymes (6,23,32); however, these enzymes require acidic pH (30) and have a short half-life at high temperatures (12) and a low specific activity (10), which are bottlenecks to using fungal enzymes. Bacterial plant-hydrolyzing enzymes have been reported to work at a wide range of pHs and temperatures (10,21) and, therefore, are potential catalysts for biomass hydrolysis (3,14,15,16,18). Bacteria living in the guts of organisms are of special interest owing to their ability to degrade complex substrates, such as lignocellulosic biomass, at rapid rates (8,35).…”

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confidence: 99%

Synthesis and Characterization of Chimeric Proteins Based on Cellulase and Xylanase from an Insect Gut Bacterium

Adlakha

Rajagopal

Kumar

et al. 2011

Appl Environ Microbiol

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Insects living on wood and plants harbor a large variety of bacterial flora in their guts for degrading biomass. We isolated a Paenibacillus strain, designated ICGEB2008, from the gut of a cotton bollworm on the basis of its ability to secrete a variety of plant-hydrolyzing enzymes. In this study, we cloned, expressed, and characterized two enzymes, ␤-1,4-endoglucanase (Endo5A) and ␤-1,4-endoxylanase (Xyl11D), from the ICGEB2008 strain and synthesized recombinant bifunctional enzymes based on Endo5A and Xyl11D. The gene encoding Endo5A was obtained from the genome of the ICGEB2008 strain by shotgun cloning. The gene encoding Xyl11D was obtained using primers for conserved xylanase sequences, which were identified by aligning xylanase sequences in other species of Paenibacillus. Endo5A and Xyl11D were overexpressed in Escherichia coli, and their optimal activities were characterized. Both Endo5A and Xyl11D exhibited maximum specific activity at 50°C and pH 6 to 7. To take advantage of this feature, we constructed four bifunctional chimeric models of Endo5A and Xyl11D by fusing the encoding genes either end to end or through a glycine-serine (GS) linker. We predicted three-dimensional structures of the four models using the I-TASSER server and analyzed their secondary structures using circular dichroism (CD) spectroscopy. The chimeric model Endo5A-GS-Xyl11D, in which a linker separated the two enzymes, yielded the highest C-score on the I-TASSER server, exhibited secondary structure properties closest to the native enzymes, and demonstrated 1.6-fold and 2.3-fold higher enzyme activity than Endo5A and Xyl11D, respectively. This bifunctional enzyme could be effective for hydrolyzing plant biomass owing to its broad substrate range.Cellulose and hemicellulose constitute ϳ70 to 80% of wood and agricultural biomass and can serve as an abundant and inexpensive source of fermentable sugar for producing various chemicals and biofuels (34,35). Three enzymes hydrolyze the ␤-1,4 glycosidic linkages that are present in cellulose. ␤-1,4-Endoglucanases cleave within the chain, cellobiohydrolases cleave at either end of the chain, and ␤-glucosidases break oligomers into monomers (22). Another class of enzymes, which includes xylanase and xylosidase, hydrolyzes ␤-1,4-xylan into xylose and is involved in the breakdown of hemicellulose (2).Although a process to convert lignocellulosic biomass into ethanol has been developed by various research groups, costeffective production of lignocellulosic ethanol is still a major issue, largely because of the high cost associated with the enzymes (20,22,34). Fungi such as Trichoderma reesei and Aspergillus niger are common sources of plant-hydrolyzing enzymes (6, 23, 32); however, these enzymes require acidic pH (30) and have a short half-life at high temperatures (12) and a low specific activity (10), which are bottlenecks to using fungal enzymes. Bacterial plant-hydrolyzing enzymes have been reported to work at a wide range of pHs and temperatures (10, 21) and, therefore, are potential cata...

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“…12-11, showed significant xylanase activity. Many Paenibacillus strains have been exploited for the production of xylanolytic enzymes, including two xylanase genes of family 10 and 11 [16], a family 10 xylanase with high activity towards aryl-xylosides [7], and several xylanases with different physical and kinetic properties [12]. All of these strains were from neutral or acidic environments.…”

Section: Discussionmentioning

confidence: 99%

“…E2 [37], Streptomyces megasporus DSM 41476 [29], Paenibacillus sp. HPL-001 [12], and P. curdlanolyticus [34] that had pH optima at pH 5.5 to 9.5 and exhibited good pH stability, XYN7C has some similar alkaline properties, such as a pH optimum at pH 8.0, and good pH adaptability (retaining above 90% of its maximum activity at pH 6.5 to 8.5) and stability (retaining more than 60% of the maximum activity at pH 5.0-12.0). Xylanases from S. megasporus DSM 41476 and C. laeviribosi HY-21 are stable over a broad pH range as XYN7C is, but their specific activities towards oat spelt xylan are only 242.1 and 88.6 U/mg, respectively, far lower than that of XYN7C (1,340 U/mg) [13,29].…”

Section: Discussionmentioning

confidence: 99%

Cloning, Expression, and Characterization of a New Xylanase from Alkalophilic Paenibacillus sp. 12-11

Zhao

Meng²,

Luo³

et al. 2011

J. Microbiol. Biotechnol.

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A xylanase gene, xyn7c, was cloned from Paenibacillus sp. 12-11, an alkalophilic strain isolated from the alkaline wastewater sludge of a paper mill, and expressed in Escherichia coli. The full-length gene consists of 1,296 bp and encodes a mature protein of 400 residues (excluding the putative signal peptide) that belongs to the glycoside hydrolase family 10. The optimal pH of the purified recombinant XYN7C was found to be 8.0, and the enzyme had good pH adaptability at 6.5-8.5 and stability over a broad pH range of 5.0-11.0. XYN7C exhibited maximum activity at 55 o C and was thermostable at 50 o C and below. Using wheat arabinoxylan as the substrate, XYN7C had a high specific activity of 1,886 U/mg, and the apparent K m and V max values were 1.18 mg/ml and 1,961 µmol/mg/min, respectively. XYN7C also had substrate specificity towards various xylans, and was highly resistant to neutral proteases. The main hydrolysis products of xylans were xylose and xylobiose. These properties make XYN7C a promising candidate to be used in biobleaching, baking, and cotton scouring processes.

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Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001

Cited by 33 publications

References 45 publications

Xylanases of Bacillus spp. isolated from ruminant dung as potential accessory enzymes for agro-waste saccharification

Xylanases of Bacillus spp. isolated from ruminant dung as potential accessory enzymes for agro-waste saccharification

Synthesis and Characterization of Chimeric Proteins Based on Cellulase and Xylanase from an Insect Gut Bacterium

Cloning, Expression, and Characterization of a New Xylanase from Alkalophilic Paenibacillus sp. 12-11

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