Production of alkaline xylanase by a newly isolated alkaliphilic Bacillus sp. strain 41M-1

Nakamura, Satoshi; Wakabayashi, Kenji; Nakai, Ryuichiro; Aono, Rikizo; Horikoshi, Koki

doi:10.1007/bf00327842

Cited by 84 publications

(75 citation statements)

References 10 publications

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“…One unit of activity (U) is defined as the amount of enzyme capable of releasing reducing sugars equivalent to one mole of xylose per minute under the conditions described [21]. was also performed.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Xylanases of marine fungi of potential use for biobleaching of paper pulp

Raghukumar

Muraleedharan

Gaud

et al. 2004

J IND MICROBIOL BIOTECHNOL

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Microbial xylanases that are thermostable, active at alkaline pH and cellulasefree are generally preferred for biobleaching of paper pulp.. We screened obligate and facultative marine fungi for xylanase activity with these desirable traits.Several fungal isolates obtained from marine habitat showed alkaline xylanase activity. The crude enzyme from NIOCC isolate # 3 (Aspergillus niger) with high xylanase activity, cellulase-free and unique properties containing 580 U L -1 of xylanase, could bring about bleaching of sugarcane bagasse pulp by a 60 min treatment at 55 o C, resulting in a decrease of 10 kappa numbers and a 30% reduction in consumption of chlorine during bleaching process. The culture filtrate showed peaks of xylanase activity at acidic pH (3.5) and alkaline pH (8.5). When assayed at pH 3.5 optimum activity was detected at 50 o C with a second peak of activity at 90 o C. When assayed at pH 8.5 optimum activity was seen at 80 o C. The crude enzyme was thermostable at 55 o C for at least 4 h and retained about 60% of the activity. Gel filtration of the 50-80% ammonium sulfate precipitatedfraction of the crude culture filtrate separated into two peaks of xylanase having specific activities of 393 and 2457 U mg -1 protein. The two peaks showing xylanase activities had molecular masses of 13 and 18 kDa. Zymogram analysis of xylanase of crude culture filtrate as well as the 50-80% ammonium sulphateprecipitated fraction showed two distinct xylanase activity bands on native PAGE The crude culture filtrate also showed moderate activities of -xylosidase and -L-arabinofuranosidase which could act synergistically with xylanase in attacking xylan. This is the first report showing potential application of crude culture filtrate of a marine fungal isolate possessing thermostable, cellulase-free alkaline xylanase activity in biobleaching of paper pulp.

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Section: Enzyme Assaysmentioning

confidence: 99%

Xylanases of marine fungi of potential use for biobleaching of paper pulp

Raghukumar

Muraleedharan

Gaud

et al. 2004

J IND MICROBIOL BIOTECHNOL

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“…strains from soil produced multiple xylanases extracellularly. 63),64) One of the enzymes, xylanase J, was most active at pH 9.0. The optimum temperature for the activity at pH 9.0 was around 50˚C.…”

Section: )mentioning

confidence: 99%

Alkaliphiles

Horikoshi

2004

Proc. Jpn. Acad., Ser. B

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Abstract:The term alkaliphile is used for microorganisms that grow optimally or very well at pH values above 9, but cannot grow or grow only slowly at the near neutral pH value of 6.5. Alkaliphiles include prokaryotes, eukaryotes, and archaea. Alkaliphiles can be isolated from normal environments such as garden soil, although viable counts of alkaliphiles are higher in samples from alkaline environments. The cell surface plays a key role in keeping the intracellular pH value in the range between 7 and 8.5, allowing alkaliphiles to thrive in alkaline environments. Alkaliphiles have made a great impact in industrial applications. Biological detergents contain alkaline enzymes, such as alkaline cellulases and/or alkaline proteases that have been produced from alkaliphiles. Another important application is the industrial production of cyclodextrin with alkaline cyclomaltodextrin glucanotransferase. This enzyme reduced the production cost and paved the way for cyclodextrin use in large quantities in foodstuffs, chemicals and pharmaceuticals. It has also been reported that alkali-treated wood pulp could be biologically bleached by xylanases produced by alkaliphiles.

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“…On the other hand, an XBD truncated XynJ derivative (∆XBD), and a fusion protein of glutathione S transferase (GST) and the XBD (GST XBD) were prepared. 6,7) GST XBD bound tightly to insoluble xylan and ∆XBD showed far lower hydrolyzing activity toward insoluble xylan than full length XynJ. These results indicated that the XBD would bind to insoluble xylan and enhance hydrolyzing activity of the adjacent CatD.…”

mentioning

confidence: 94%

“…41M 1 from a soil sample. 4) The strain produced a xylanase that had an alkaline pH optimum. 5) The enzyme, named xylanase J (XynJ), consists of two functional domains: a glycoside hydrolase (GH) family 11 catalytic domain (CatD) and a xylan binding domain (XBD) belonging to carbohydrate binding module family 36 (http: www.…”

mentioning

confidence: 99%

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Analysis of Functional Domains and Improvement of Alkaliphily of an Alkaline Xylanase on the Basis of Its Three-dimensional Structure

Umemoto¹,

Yazawa²,

Takakura³

et al. 2010

J. Appl. Glycosci.

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Xylanase J (XynJ) from alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme consisting of a glycoside hydrolase (GH) family 11 catalytic domain and a carbohydrate-binding module family 36 xylan-binding domain (XBD). Structural comparison of the GH family 11 catalytic domains indicated that there were several specific salt bridges in the catalytic cleft of XynJ. Mutant enzymes were prepared by substituting several amino acid residues responsible for the characteristic salt bridges. Elimination of the salt bridges caused an acidophilic shift in optimum pH, suggesting that the characteristic salt bridges contributed to the alkaliphily of XynJ. On the other hand, reinforcing one of the characteristic salt bridges in the catalytic domain shifted the optimum pH of XynJ from 8.5 to 9.0. Furthermore, introducing excess Arg residues on the protein surface was also effective to improve the alkaliphily of XynJ. Xylan-binding properties of various XBD mutants were investigated as fusion proteins with glutathione-S-transferase. Furthermore, the same substitutions were introduced into the XBD region of XynJ and insoluble xylan-hydrolyzing activity was measured. The results indicated that some Asp, Trp and Tyr residues were important for xylan-binding activity of the XBD, and that xylan-hydrolyzing activity of XynJ was closely correlated to xylan-binding activity of the XBD region.

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Production of alkaline xylanase by a newly isolated alkaliphilic Bacillus sp. strain 41M-1

Cited by 84 publications

References 10 publications

Xylanases of marine fungi of potential use for biobleaching of paper pulp

Xylanases of marine fungi of potential use for biobleaching of paper pulp

Alkaliphiles

Analysis of Functional Domains and Improvement of Alkaliphily of an Alkaline Xylanase on the Basis of Its Three-dimensional Structure

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