Some aspects of a 1,4-β-?-xylanase and a β-?-xylosidase secreted by Bacillus coagulans strain 26

Esteban, R

doi:10.1016/0378-1097(83)90249-5

Cited by 7 publications

(8 citation statements)

References 4 publications

(6 reference statements)

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“…These data suggest that both activities may reside within a single bifunctional protein, which would be a rather novel enzyme. Xylosidases have been purified from Clostridium acetobutylicum (11), Bacillus pumilus (16), Bacillus coagulans (6), and Thermomonospora fusca (1), and all are multisubunit enzymes ranging in molecular weight from 130,000 to 224,000. None of these enzymes display arabinosidase activity.…”

Section: Pvuii Kpnl Ecorimentioning

confidence: 99%

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

Whitehead

Hespell

1990

J Bacteriol

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Genes coding for three xylan-degrading activities, xylanase, xylosidase, and arabinosidase, were simultaneously cloned from the colonic anaerobic organism Bacteriodes ovatus. The genes for the three enzymes were located on a 3.8-kilobase EcoRI genomic insert and were cloned by using plasmid pUC18. All three activities were expressed in Escherichia coli JM83, and all were cell associated. Expression of the xylanase gene was independent from expression of the xylosidase and arabinosidase genes, whereas expression of the latter two genes appeared to be coordinated. Restriction endonuclease analysis of the arabinosidase and xylosidase genes and partial purification of these enzyme activities from E. coli suggested that these activities were catalyzed by a bifunctional protein or two proteins of very similar molecular weight. All three enzyme activities were regulated in B. ovatus in response to the carbon source used for growth. This is the first report of the cloning and expression of B. ovatus genes.

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Section: Pvuii Kpnl Ecorimentioning

confidence: 99%

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

Whitehead

Hespell

1990

J Bacteriol

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“…Xylanases with high pIs have been shown in several Bacillus species. Bacillus coagulans produces a xylanase with a molecular mass of 22 kDa and a pI of 10.0 (Esteban et al 1983). Bacillus circulans and Bacillus subtilis have xylanases of 22 kDa with a pI of 9.0 Paice et al 1986).…”

Section: Identification and Characterization Of Xylanases Producedmentioning

confidence: 99%

Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23

Blanco¹,

Pastor²

1993

Can. J. Microbiol.

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BLANCO, A., and PASTOR, F.I.J. 1993. Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23. Can. J. Microbiol. 39: 1162-1166. A Bacillus strain with xylanase activity has been isolated. Maximum xylanase production was obtained when the strain was cultured in media supplemented with birchwood xylan or rice straw; production was repressed by glucose and xylose. The optimal temperature and pH for xylanase activity were 4550°C and 5.5-7.5, respectively. Crude xylanase was highly stable at a wide range of pH values, retaining 100070 of the activity after 24 h of incubation at 37°C in buffer at pH 10.0. Analysis by polyacrylamide gel electrophoresis and zymogram techniques showed four xylanase activity bands with apparent molecular masses of 32, 48, 61, and 66 kDa. The most active of them (molecular mass 32 kDa) apparently corresponded to a xylanase with an isoelectric point (PI) of 9.3 in isoelectrofocusing gels developed as zymograms. Four other bands with xylanase activity were detected at pIs of 7.7, 5.6, 5.0, and 4.5. Analysis for carboxymethylcellulase activity revealed that only the band of 48 kDa and the band with a pI of 7.7 showed hydrolytic activity against the cellulosic substrate.

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“…Some microorganisms excrete large amount of xylanolytic enzymes in culture media while other, although growing on xylan, excrete little or no enzymes into the medium.Thousands of bacterial species are xylanase producing (xylan degrading) that occur in nature [20]. Xylanase producing bacteria are Bacillus agaradhaerens [21], Bacillus circulans [22], Bacillus subtilis [23], Bacillus coagulans [24], Geobacillus stearothermophilus [25], Streptomyces halstedii [26], Streptomyces lividans [27], Cellvibrio japonicus [28] etc. A large number of fungi have been characterized to have xylanase activity.…”

Section: Introductionmentioning

confidence: 99%

Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from <i>Paenibacillus sp.</i>

Siddiqui¹

2016

AJLS

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Abstract:Xylanases are hydrolytic enzymes that cleave the β-1,4-linkage ofwheat bran xylan. For screening of xylanase producing bacteria soil samples were diluted by serial dilution and cultured on selective wheat bran xylan agar media. Two bacterial strains showing clear transparent zone around the colony on xylan agar plate were selected as xylanase producing bacteria. The strain Paenibacillus sp. showed highest xylanolytic activity. The strain was thermophile and produced highly active cellulase free xylanase. The enzyme secretion was enhanced when the medium was supplemented with 0.5% wheat bran xylan, peptone and Ca 2+ salt. The peak in xylanase production was achieved within 48-60 hours at temperature 50°-55°C and at pH 7.0.The cellulase free xylanase was partially purified by ammonium sulfate fractionation and heat treatment at 50°C. The xylanase was optimally active at pH 7.0 and 55°C; and showed high substrate activity to wheat bran xylan but no activity towards carboxymethylcellulose, cellulose and starch.In future we want to know the structure function relationship of the purified enzyme and also want to known the molecular biological study using highly purified xylanase. For this purpose we have to determine the N-terminal & C-terminal amino acid sequence.

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Some aspects of a 1,4-β-?-xylanase and a β-?-xylosidase secreted by Bacillus coagulans strain 26

Cited by 7 publications

References 4 publications

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23

Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from <i>Paenibacillus sp.</i>

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Some aspects of a 1,4-β-?-xylanase and a β-?-xylosidase secreted by Bacillus coagulans strain 26

Cited by 7 publications

References 4 publications

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region

Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23

Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from &lt;i&gt;Paenibacillus sp.&lt;/i&gt;

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Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from <i>Paenibacillus sp.</i>