Multiple Regulatory Mechanisms Control the Expression of the Geobacillus stearothermophilus Gene for Extracellular Xylanase

Microbial xylanase and pectinase are two extremely valuable enzymes, which have captivated much attention. This can be seen from the increased demand for these enzymes by many industrial sectors. This study investigates the isolation and screening of extracellular xylanopectinolytic enzymes-producing bacteria in a submerged fermentation (SmF). Samples are collected from the compost of empty fruit bunch (EFB) at Biocompost Pilot Plant, located at Biorefinery Plant, Universiti Putra Malaysia. From the experiment, out of 20 isolates, 11 isolates show xylanase or/and pectinase activity, and only one isolate (EFB-11) shows the concurrent activities of xylanase and pectinase. These activities are selected for enzyme production under submerged fermentation (quantitative screening). At the 72nd hour of incubation, xylanase and pectinase show the highest production, which ranges about 42.33 U/mL and 62.17 U/mL (with low amount of cellulase present), supplemented with 2% (w/v) of rice bran as carbon source at incubation temperature level, which is 30°C. Meanwhile, the pH of media is shifted to 8.42, which indicates that EFB-11 isolate is alkalotolerant bacteria and identified as Bacillus subtilis ADI1. This strain proves to have potential in agroindustrial bioconversion and has a promising ability to scale up to an industrial scale.

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“…There are several reports regarding the catabolite repression of xylanase [32–35] and pectinase [36–39] in bacteria and fungi.…”

Section: Resultsmentioning

confidence: 99%

Extracellular Xylanopectinolytic Enzymes byBacillus subtilisADI1 from EFB’s Compost

Nawawi

Mohamad

Tahir

et al. 2017

International Scholarly Research Notices

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“…The short unsubstituted XOSs are then transported into the cells, which are the substrates for the intracellular ␤-xylosidase to produce xylose (41). The reason for the intracellular xylanase activity is probably for the hydrolysis of short XOSs that enter the cell to xylobiose (42). In addition to PcAxy43A, other intracellular endo-xylanases are found in the genus Paenibacillus, such as Xyn10B from strain B-6 (25) and XynA2 from strain JDR-2 (43).…”

Section: Resultsmentioning

confidence: 99%

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Teeravivattanakit

Baramee

Phitsuwan

et al. 2016

Appl Environ Microbiol

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The axy43A gene encoding the intracellular trifunctional xylanolytic enzyme from Paenibacillus curdlanolyticus B-6 was cloned and expressed in Escherichia coli. Recombinant PcAxy43A consisting of a glycoside hydrolase family 43 and a family 6 carbohydrate-binding module exhibited endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase activities. PcAxy43A hydrolyzed xylohexaose and birch wood xylan to release a series of xylooligosaccharides, indicating that PcAxy43A contained endo-xylanase activity. PcAxy43A exhibited ␤-xylosidase activity toward a chromogenic substrate, p-nitrophenyl-␤-D-xylopyranoside, and xylobiose, while it preferred to hydrolyze long-chain xylooligosaccharides rather than xylobiose. In addition, surprisingly, PcAxy43A showed arabinoxylan arabinofuranohydrolase activity; that is, it released arabinose from both singly and doubly arabinosylated xylose,Moreover, the combination of PcAxy43A and P. curdlanolyticus B-6 endo-xylanase Xyn10C greatly improved the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan, suggesting that these two enzymes function synergistically to depolymerize arabinoxylan. Therefore, PcAxy43A has the potential for the saccharification of arabinoxylan into simple sugars for many applications. IMPORTANCEIn this study, the glycoside hydrolase 43 (GH43) intracellular multifunctional endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase (AXH) from P. curdlanolyticus B-6 were characterized. Interestingly, PcAxy43A AXH showed a new property that acted on both the C(O)-2 and C(O)-3 positions of xylose residues doubly substituted with arabinosyl, which usually obstruct the action of xylanolytic enzymes. Furthermore, the studies here show interesting properties for the processing of xylans from cereal grains, particularly rye arabinoxylan, and show a novel relationship between PcAxy43A and endo-xylanase Xyn10C from strain B-6, providing novel metabolic potential for processing arabinoxylans into xylose and arabinose.

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“…Different Geobacillus strains produce some glycoside hydrolases (Shulami et al, 2014). However, the insertion of additional genes encoding these enzymes could increase their polysaccharide-degrading activity.…”

Section: Applications Of Genetically Engineered Geobacillus Strainsmentioning

confidence: 99%

Genetic engineering of Geobacillus spp.

Kananavičiūtė

Čitavičius

2015

Journal of Microbiological Methods

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Multiple Regulatory Mechanisms Control the Expression of the Geobacillus stearothermophilus Gene for Extracellular Xylanase

Cited by 34 publications

References 91 publications

Extracellular Xylanopectinolytic Enzymes byBacillus subtilisADI1 from EFB’s Compost

Extracellular Xylanopectinolytic Enzymes byBacillus subtilisADI1 from EFB’s Compost

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Genetic engineering of Geobacillus spp.

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