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Bleach enhancement of mixed wood pulp by mixture of thermo-alkali-stable xylanase and mannanase derived through co-culturing of Alkalophilic Bacillus sp. NG-27 and Bacillus nealsonii PN-11.

ABSTRACT: The Application of a combination of enzymes is the best alternative to reduce the use of chemicals in the paper industry. Bacillus sp. NG-27 and Bacillus nealsonii PN-11 are known to produce thermoalkali stable xylanse (X) and mannanase (M) respectively having potential for pulp biobleaching. The Present study, reports the production of a mixture of X + M by co-culturing of strains in SSF and standardizing its application for pulp biobleaching. Production of enzymes by co-cultivation in SSF was optimized by statistical methods. Substantial increase in the yield of enzymes; 3.61 fold of xylanase and 37.71 fold of mannanase was achieved. Application of enzyme cocktail for pulp biobleaching resulted in a 45.64% reduction of kappa number with 55 IU g^-1odp of enzyme dose (xylanase:mannanase; 3:1) at pH 8.0 in 1h at 65 °C along with significant increase in brightness (11%) and whiteness (75%). The Same quality of paper as made up from chemical treated pulp can be made from enzyme-treated pulp with 30% less use of chlorine. Structural analysis of enzyme-treated pulp showed dissolution of hemicellulose as indicated by pores, cracks and increased roughness all over the surface. Cocktail of X + M produced economically in a single fermentation having all the requisite characteristics for pulp biobleaching is a highly suitable candidate for application in the pulp and paper industry.

SUBMITTER: Angural S

PROVIDER: S-EPMC7855340 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BACKGROUND:?-Mannanase catalyzes the cleavage of ?-1,4-linked internal linkages of mannan backbone randomly to produce new chain ends. Alkaline and thermostable ?-mannanases provide obvious advantages for many applications in biobleaching of pulp and paper, detergent industry, oil grilling operation and enzymatic production of mannooligosaccharides. However, only a few of them are commercially exploited as wild or recombinant enzymes, and none heterologous and secretory expression of alkaline ?-mannanase in Bacillus subtilis expression system was reported. Alkaliphilic Bacillus clausii S10 showed high ?-mannanase activity at alkaline condition. In this study, this ?-mannanase was cloned, purified and characterized. The high-level secretory expression in B. subtilis was also studied. RESULTS:A thermo-alkaline ?-mannanase (BcManA) gene encoding a 317-amino acid protein from alkaliphilic Bacillus clausii strain was cloned and expressed in Escherichia coli. The purified mature BcManA exhibited maximum activity at pH 9.5 and 75 °C with good stability at pH 7.0-11.5 and below 80 °C. BcManA demonstrated high cleavage capability on polysaccharides containing ?-1,4-mannosidic linkages, such as konjac glucomannan, locust bean gum, guar gum and sesbania gum. The highest specific activity of 2366.2 U mg-1 was observed on konjac glucomannan with the Km and kcat value of 0.62 g l-1 and 1238.9 s-1, respectively. The hydrolysis products were mainly oligosaccharides with a higher degree of polymerization than biose. BcManA also cleaved manno-oligosaccharides with polymerization degree more than 3 without transglycosylation. Furthermore, six signal peptides and two strong promoters were used for efficiently secreted expression optimization in B. subtilis WB600 and the highest extracellular activity of 2374 U ml-1 with secretory rate of 98.5% was obtained using SPlipA and P43 after 72 h cultivation in 2?×?SR medium. By medium optimization using cheap nitrogen and carbon source of peanut meal and glucose, the extracellular activity reached 6041 U ml-1 after 72 h cultivation with 6% inoculum size by shake flask fermentation. CONCLUSIONS:The thermo-alkaline ?-mannanase BcManA showed good thermal and pH stability and high catalytic efficiency towards konjac glucomannan and locust bean gum, which distinguished from other reported ?-mannanases and was a promising thermo-alkaline ?-mannanase for potential industrial application. The extracellular BcManA yield of 6041 U ml-1, which was to date the highest reported yield by flask shake, was obtained in B. subtilis with constitutive expression vector. This is the first report for secretory expression of alkaline ?-mannanase in B. subtilis protein expression system, which would significantly cut down the production cost of this enzyme. Also this research would be helpful for secretory expression of other ?-mannanases in B. subtilis.

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Bleach enhancement of mixed wood pulp by mixture of thermo-alkali-stable xylanase and mannanase derived through co-culturing of Alkalophilic Bacillus sp. NG-27 and Bacillus nealsonii PN-11.

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