Xylanase from Alkalophilic<i>Bacillus</i>sp. YC-335

Yum, Do Young; Bai, Dong Hoon; Yu, Ji Hea

doi:10.1271/bbb.56.1355

Cited by 10 publications

(5 citation statements)

References 2 publications

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“…The inactivation of xylanase by p-chloromercury benzoate indicates involvement of cysteine residues in the activity. Similar results are also reported by other workers (Park et al, 1992;Tsujibo et al, 1990). Max.…”

Section: Discussionsupporting

confidence: 93%

Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn.

Sapre

Jha

Patil

2005

J. Gen. Appl. Microbiol.

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Syncephalastrum racemosum Cohn. produces an extracellular xylanase that was shown to potentially bleach pulp at pH 10 and 50°C. The enzyme was found to be a dimer with an apparent molecular weight of 29 kDa as determined by SDS-PAGE. The optimum activity was found at two pH values 8.5 and 10.5; however the activity sharply decreased below pH 6 and above pH 10.5. The enzyme was stable for 72 h at pH 10.5 and at 50°C. Kinetic experiments at 50°C gave V max and K m of 1,400 U/ml min ؊1 mg ؊1 protein and 0.05 mg/ml respectively. The enzyme had no apparent requirement for cofactors, and its activity was strongly inhibited by group II b metal ions like Zn 2؉, Hg 2؉, etc. Xylan completely protected the enzyme from being inactivated by N-bromosuccinimide.

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Section: Discussionsupporting

confidence: 93%

Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn.

Sapre

Jha

Patil

2005

J. Gen. Appl. Microbiol.

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“…3). All the xylanases from alkaliphiles described earlier had pH optima in the near neutral range (9,12,13,20,21,25,31), although some of them showed ::…”

Section: Resultsmentioning

confidence: 94%

“…Microbial xylanases usually exhibit acidic or neutral pH optima. Several xylanases from alkaliphilic (9,12,13,20,21,25,31) and alkalitolerant bacteria (27) have been studied to date, but the pH optima of these enzymes lie in the near neutral region.…”

mentioning

confidence: 99%

Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1

Nakamura

Wakabayashi

Nakai

et al. 1993

Appl Environ Microbiol

176

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An alkaliphilic BaciUlus sp. strain, 41M-1, isolated from soil produced multiple xylanases extracellularly. One of these xylanases was purified to homogeneity by ammonium sulfate fractionation and anion-exchange chromatography. The molecular mass of this enzyme (xylanase J) was 36 kDa, and the isoelectric point was pH 5.3. Xylanase J was most active at pH 9.0. The optimum temperature for the activity at pH 9.0 was around 50°C. The enzyme was stable up to 55°C at pH 9.0 for 30 min. Xylanase J was completely inhibited by the Hg2+ ion and N-bromosuccinimide. The predominant products of xylan hydrolysate were xylobiose, xylotriose, and higher oligosaccharides, indicating that the enzyme was an endoxylanase. The apparent Km and Vmax values on xylan were 3.3 mg/ml and 1,100 ,umol min-' mg-', respectively. Xylanase J showed high sequence homology with the xylanases from Bacillus pumilus and Clostridium acetobutylicum in the N-terminal region. Xylanase J acted on neither crystalline cellulose nor carboxymethyl cellulose, indicating a possible application of the enzyme in biobleaching processes.

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“…From the application point of view, xylanases active and stable in the alkaline pH range and at elevated temperature are very important. Most alkaliphilic and alkalitolerant microorganisms produce xyla-nases optimally active around neutrality (1,6,(10)(11)(12). Although some strains are known to produce xylanases having good activity at pHs greater than 8, the optimum temperature for activity and stability is at or below 50 to 55°C (4,9,15).…”

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confidence: 99%

Purification and Properties of Two Thermostable Alkaline Xylanases from an Alkaliphilic Bacillus sp

Gessesse

1998

Appl Environ Microbiol

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Two xylanases, designated XylA and XylB, were purified from the culture supernatant of the alkaliphilic Bacillus sp. strain AR-009. The molecular masses of the two enzymes were estimated to be 23 kDa (XylA) and 48 kDa (XylB) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pHs for activity were 9 for XylA and 9 to 10 for XylB. The temperature optima for the activity of XylA were 60°C at pH 9 and 70°C at pH 8. XylB was optimally active at 75°C at pH 9 and 70°C at pH 8. Both enzymes were stable in a broad pH range and showed good stability when incubated at 60 and 65°C in pH 8 and 9 buffers.

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Xylanase from AlkalophilicBacillussp. YC-335

Cited by 10 publications

References 2 publications

Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn.

Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn.

Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1

Purification and Properties of Two Thermostable Alkaline Xylanases from an Alkaliphilic Bacillus sp

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