Cloning of a Family 11 Xylanase Gene from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang

Baek, Chang Un; Lee, S. G.; Chung, Young Ryun; Cho, I.; Kim, J. H.

doi:10.1007/s12088-012-0260-4

Cited by 12 publications

(11 citation statements)

References 20 publications

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“…Genus Bacillus is known to produce industrially valuable xylanases, a number of which are reported (13,16,19,(27)(28)(29). The catalytic domain of xynBT21 (from B. tequilensis) showed high homology with xylanases belonging to glycosyl hydrolase family 11 according to the hydrophobic cluster analysis (27).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Recombinant Xylanase from Bacillus tequilensis BT21: Biochemical Characterization and Its Application in Production of Xylobiose from Agricultural Residues

Khandeparker

Parab

Amberkar

2017

Food Technol. Biotechnol.

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Section: Discussionmentioning

confidence: 99%

“…There is a widespread occurrence of xylanase family 11 in Bacillus sp. (13,(27)(28)(29). The amino acid sequence of the B. tequilensis BT21 xylanase was compared with other reported xylanases in the NCBI database with the help of BLAST search program (14).…”

Section: Discussionmentioning

confidence: 99%

Recombinant Xylanase from Bacillus tequilensis BT21: Biochemical Characterization and Its Application in Production of Xylobiose from Agricultural Residues

Khandeparker

Parab

Amberkar

2017

Food Technol. Biotechnol.

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“…In order to compare the protein expression difference, sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to separate the protein using the Laemmli's buffers [10]. Protein concentration was initially determined according to the Bradford method [11], with bovine serum albumin (BSA) as the protein standard.…”

Section: Protein Extraction and Sds-page Electrophoresismentioning

confidence: 99%

Isolation and Analysis of Salt Response of Lactobacillus plantarum FS5-5 from Dajiang

Song

Wang

et al. 2016

Indian J Microbiol

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From 15 samples of dajiang collected in northeast of China, three salt resistant lactic acid bacteria were isolated and identified as Lactobacillus plantarum through physiological studies and 16S rDNA sequence alignment. L. plantarum FS5-5 showed better growth in an environment with 12 % (w/v) NaCl than the other two strains. The expression of proteins extracted from L. plantarum FS5-5 cultured in de Man, Rogosa, and Sharp (MRS) containing 0, 3, 6 and 9 % (w/v) NaCl was analyzed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). The results showed that 42 kinds of proteins were identified, which could be divided into three groups: 27 kinds of proteins related to protein synthesis and degradation, six kinds of proteins related to carbohydrate metabolism and energy metabolism, nine proteins related to nucleic acid metabolism. Overexpression of these proteins imply that a series of changes have occurred in the process of protein synthesis and degradation, carbohydrate metabolism, energy metabolism and nucleic acid metabolism after L. plantarum FS5-5 exposed to salt stress. All these proteins may have effects on the salt-tolerant characteristics of the L. plantarum FS5-5.

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“…Now, the discrepancies in the posttranslational modification are not very clear, but the definite mechanism analysis will be taken into account in further study. Compared with xylanases from other microorganisms (Baek et al, 2012;Wang et al, 2012a, b), reXyn43A could be more suitable for application in many of the low or moderate temperature processes, such as in the food industry. Furthermore, considering that most industrial enzymatic operations are carried out at high temperatures, the thermostability of reXyn43A could be enhanced by means of genetic engineering technology, such as N-terminus replacement or directed evolution.…”

Section: Properties Of the Recombinant Xyn43amentioning

confidence: 99%

“…However, enzymes with xylanase activity are also found in GH families 5,7,8,16,43,52 and 62, but not much information is available . Since Bernier et al isolated a xylanase gene from Bacillus subtilis PAP115 for the first time in 1983, many kinds of xylanases have been cloned (Bernier et al, 1983;Baek et al, 2012;Guo et al, 2013;Xie et al, 2012), and expressed in heterologous hosts (Buanafina et al, 2012;Shi et al, 2013;Verma et al, 2013). Many studies have been conducted on exploiting novel xylanases with superior properties.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, sequence analysis and expression of a GHF 43 xylanase from Aspergillus niger in Escherichia coli

Zhou

Wang

Zhu

et al. 2014

J. Gen. Appl. Microbiol.

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A new xylanase gene (xyn43A) from Aspergillus niger XZ-3S was cloned and expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL. The coding region of the gene was separated by only one intron 86 bp in length. It encoded 318 amino acid residues of a protein with a calculated molecular weight (MW) of 33.47 kDa plus a signal peptide of 19 amino acids. The amino acid sequence of the xyn43A gene showed 77.56% amino acid identity to A. nidulans xylanase, and the phylogenetic tree analysis revealed that xyn43A had close relationships with those of family 43 of glycosyl hydrolases reported from other microorganisms. Three-dimensional structure modeling showed that Xyn43A had a typical five-blade β-propeller fold. The mature peptide encoding cDNA was subcloned into pET-28a (+) expression vector. The resultant recombinant plasmid pET-28a-xyn43A was transformed into Escherichia coli BL21-CodonPlus (DE3)-RIL, and xylanase activity was measured. A maximum activity of 61.43 U/mg was obtained from the cellular extract of E. coli BL21-CodonPlus (DE3)-RIL harboring pET-28a-xyn43A. The recombinant xylanase had optimal activity at pH5.0 and 45 C. Fe 3+ , Cu 2+ and EDTA had an obvious active effect on the enzyme.

show abstract

Cloning of a Family 11 Xylanase Gene from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang

Cited by 12 publications

References 20 publications

Recombinant Xylanase from Bacillus tequilensis BT21: Biochemical Characterization and Its Application in Production of Xylobiose from Agricultural Residues

Recombinant Xylanase from Bacillus tequilensis BT21: Biochemical Characterization and Its Application in Production of Xylobiose from Agricultural Residues

Isolation and Analysis of Salt Response of Lactobacillus plantarum FS5-5 from Dajiang

Molecular cloning, sequence analysis and expression of a GHF 43 xylanase from Aspergillus niger in Escherichia coli

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