Purification and properties of a xylanase from <i>Streptomyces lividans</i>

Morosoli, Rolf; Bertrand, J L; Mondou, Francine; Shareck, François; Kluepfel, Dieter

doi:10.1042/bj2390587

Cited by 99 publications

(47 citation statements)

References 17 publications

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“…, 1984; Kusakabe et a/., 1977; Morosoli et al, 1986). Finally, genes coding for endoglucanase activity in T. fusca (Collmer & Wilson, 1983;Ghangas & Wilson, 1987) and endoxylanase activity in a Streptomyes sp.…”

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confidence: 99%

Sacchariiication of Straw by Actinomycete Enzymes

Ball

McCarthy

1988

Microbiology

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Over 200 strains of actinomycetes, representing nine distinct genera, were screened directly for the ability to release reducing sugar from ball-milled wheat straw, using a microtitre plate assay system. Xylanase activity was detected in nearly all of the strains examined while activities against purified cellulosic substrates were less widespread and relatively low. Straw saccharification resulted from cooperative enzyme action and sugar yields were not simply correlated with substrate particle size. Straw-saccharifying activity was further characterized in selected strains comprising five representatives of the genera Thermomonospora and Streptomyces, one Micromonospora strain and the type strain of Microbispora bispora. Common features included optimal saccharification of straw in the pH range 64-9.0 and xylose and its oligomers as the principal products, although low concentrations of glucose were also detected. Optimal activity and increased stability at 70 "C was a feature of enzyme preparations from Thermomonospora and thermophilic Streptomyces strains. P-Xylosidase and P-glucosidase activities were largely intracellular, but significant amounts of extracellular P-xylosidase activity were also found in two strains. Other enzymes involved in straw saccharification include acetylesterase and arabinofuranosidase, and these activities were detected in all strains. Acetylesterase and arabinofuranosidase activities were largely extracellular, but in some strains significant amounts of intracellular activity were also detected.

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confidence: 99%

Sacchariiication of Straw by Actinomycete Enzymes

Ball

McCarthy

1988

Microbiology

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“…The enzyme showed optimum activity at 55°C. Xylanase of Streptomyces livindas 1326 was optimally active at 60°C and pH 6 (Morosoli et al 1986). Xylanase that are active at high temperature and pH values are required in the pulp and paper industry (Karlsson et al 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Thus it was a true cellulase free xylanase. Xylanase produced by Aeromonas caviae ME-1 did not hydrolyze starch, cellulose and carboxymethyl cellulose (Kubata et al1995) and xylanase from Streptomyces lividans-1326 showed no activity towards carboxymethylcellulose (Morosoli et al 1986). The cellulase free xylanase will be more applicable and beneficial in pre-bleaching of paper pulp because cellulase may adversely affect the quality of the paper pulp by destroying the structure of cellulose.…”

Section: Discussionmentioning

confidence: 99%

Optimization of alkali-thermostable and cellulase-free eylanase production from Bacillus Sp.

et al. 2012

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Context: To analyze the nutritional and physicochemical parameters for the production of alkali-thermostable and cellulase free xylanase from bacteria. Objectives:The aim of this study was to isolation and identification and of alkali-thermostable and cellulase free xylanase producing bacteria from soil as well as optimization of process parameters for xylanase production. Materials and Methods:The bacterium Bacillus sp. was isolated from soil by serial dilution technique on xylan agar medium and identified by morphological and biochemical studies. The production of xylanase was carried out on xylan broth medium and xylanase activity was assayed by dinitrosalicylic acid (DNS) method. The effect of cultural parameters on the production of xylanase was determined by measuring the activity of xylanase. The effect of temperature and pH on the activity of partially purified xylanase as well as substrate specificity of xylanase were examined. Results:The maximum xylanase production (4000 U/L) by a Bacillus sp. was attained when the medium containing 0.5% wheat bran xylan and peptone at pH 8.0 and 50-55°C within 48-60 h. The partially purified xylanase was optimally active at pH 9.0 and 55°C. The xylanase showed high substrate activity towards wheat bran xylan but no activity towards cellulose, carboxymethyl cellulose and starch. Thus the enzyme was alkali-thermostable and cellulase free xylanase. Conclusion:The results obtained in this study suggest that the Bacillus sp. used is highly potential and useful for the production of cellulase free xylanase.

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“…Most of the secreted proteins are enzymes which are well suited to hydrolyze complex organic material, thus permitting the bacteria to survive in their environment. In the past, we reported the homologous cloning of three xylanase genes (30) and purified the corresponding enzymes XlnA, XlnB, and XlnC from Streptomyces lividans (16,17,19). Xylanases degrade xylan, one of the major components of hemicellulose, which is a ␤-1,4-linked polymer of xylose substituted with uronic acid, hexoses, and side chains of other pentoses.…”

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Increase in Xylanase Production by Streptomyces lividans through Simultaneous Use of the Sec- and Tat-Dependent Protein Export Systems

Gauthier

Morosoli

2005

Appl Environ Microbiol

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Xylanase B1 (XlnB1) from Streptomyces lividans is a protein consisting of two discrete structural and functional units, an N-terminal catalytic domain and a C-terminal substrate binding domain. In the culture medium, two forms of xylanase B are present, namely, XlnB1 and XlnB2, the latter of which corresponds to the catalytic domain of XlnB1 deprived of the substrate binding domain. Both forms of the xylanase have the same activity on xylan. The enzyme is secreted through the Sec-dependent pathway with a better yield of XlnB1 than XlnB2. Interestingly, XlnB2 exhibits 80% identity with XlnC which is secreted exclusively through the Tatdependent pathway. To demonstrate whether XlnB1 and XlnB2 could also be secreted through the Tatdependent pathway, the Tat-targeting xlnC signal sequence was fused to the structural genes of xlnB1 and xlnB2. Both XlnB1 and XlnB2 were secreted through the Tat-dependent pathway, but XlnB2 was better produced than XlnB1. As XlnB1 and XlnB2 could be better secreted through the Sec-and Tat-dependent systems, respectively, a copy of the structural gene of xlnB1 fused to a Sec signal sequence and a copy of the structural gene of xlnB2 fused to a Tat signal sequence were inserted into the same plasmid under the control of the xlnA promoter. The transformant produced xylanase activity which corresponded approximately to the sum of activities of the individual strain producing xylanase by either the Sec-or Tat-dependent secretion system. This indicated that both secretion systems are functional and independent of each other in the recombinant strain. This is the first report on the efficient secretion of a protein using two different secretion systems at the same time. Assuming that the protein to be secreted could be properly folded prior to and after translocation via the Tat-and Sec-dependent pathways, respectively, the simultaneous use of the Sec-and Tat-dependent pathways provides an efficient means to increase the production of a given protein.

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Purification and properties of a xylanase from Streptomyces lividans

Cited by 99 publications

References 17 publications

Sacchariiication of Straw by Actinomycete Enzymes

Sacchariiication of Straw by Actinomycete Enzymes

Optimization of alkali-thermostable and cellulase-free eylanase production from Bacillus Sp.

Increase in Xylanase Production by Streptomyces lividans through Simultaneous Use of the Sec- and Tat-Dependent Protein Export Systems

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