Cloning, sequence analysis, and heterologous expression of a β-mannanase gene from Bacillus subtilis Z-2

Zhang, Q; Yan, Xing‐Gang; Zhang, L; Tang, Wenda

doi:10.1134/s0026893306030034

Cited by 31 publications

(19 citation statements)

References 25 publications

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“…Besides the carbon source, various organic or inorganic nitrogen sources play an important role in mannanase production. Organic nitrogen sources like peptone, yeast autolysate, corn steep liquor (CSL), and beef extract are preferred (Puchart et al 2004 ;Zhang et al . 2006 ;Cui et al .…”

Section: Microbial Production Of Mannanasesmentioning

confidence: 99%

Microbial Mannanases: Properties and Applications

Soni

Kango

2013

Advances in Enzyme Biotechnology

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Mannans are a major constituent of the hemicellulose fraction of lignocelluloses. Mannans perform distinct functions as structural components in cell walls of softwoods and storage functions in seeds. Enzymatic hydrolysis of mannan involves the backbone hydrolyzing endo-β-mannanases and β-mannosidases. Mannans are heteropolymeric and their hydrolysis also requires the action of β-glucosidases and side-chain cleaving α-galactosidases and acetyl mannan esterases. Microorganisms are therefore explored for the production of such repertoire of enzymes so that effective mannan hydrolysis can be achieved. The present chapter discusses the occurrence and structural properties of mannans in plant materials and its hydrolysis using enzymes sourced from various fungi and other microorganisms. The production and properties of mannanolytic enzymes, their cloning and expression in heterologous hosts, and their application have also been discussed .

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Section: Microbial Production Of Mannanasesmentioning

confidence: 99%

Microbial Mannanases: Properties and Applications

Soni

Kango

2013

Advances in Enzyme Biotechnology

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“…More-over, typical mannanase domain sequences of family GH5 were rather distributed throughout the entire gene. Family GH26 typically shows a short conserved region rich in aromatic amino acid, WFWWG 33 , which can be found in the N-terminal region but also in other parts of the protein 34 . The N-terminal sequence of mannanase S1 does not show this conserved region.…”

Section: Discussionmentioning

confidence: 99%

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Chantorn¹,

Pongsapipatana²,

Keawsompong³

et al. 2013

ScienceAsia

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The mannanase S1 from Klebsiella oxytoca KUB-CW2-3 was purified by a single anion exchange chromatography to electrophoretic homogeneity. S1 is a protein with a molecular mass of approximately 165 kDa and a pI value of 3.5. The optimum pH and temperature of mannanase activity were 4.0 and 40°C, respectively. The enzyme exhibited good stability over the broad pH range of 3-6. The mannanase S1 exhibited specific activity for different mannan substrates including galactomannan from locust bean gum (LBG), copra meal, and glucomannan from konjac, while neither xylanase nor cellulase activity were detectable. The Michaelis-Menten constants (Km), maximum velocity (Vmax), and the catalytic constant (kcat) values of S1 against LBG and konjac mannan were 1.038-1.056 mg/ml, 6.149-6.183 µU ml −1 min −1 , and 0.047 s −1 , respectively. In addition, mannanase activity was activated by Co 2+ (129%) but completely inhibited by EDTA and Zn 2+ . The N-terminal amino acid sequence (GRVGEAGPHGPHGPH) of mannanase S1is different from the N-terminal region of other bacterial mannanases belonging to the glycoside hydrolase family GH5. The degradation products of mannanase S1 from LBG hydrolysis were galactose and unknown oligosaccharides with a different molecular structure to mannobiose, triose, and tetraose indicating the cleavages of α-1,6-galactosidic and β-1,4-mannosidic linkages. Its hydrolysis of 100 mM CoCl2-treated copra mannan enhanced the growth of Lactobacillus reuteri KUB-AC5 but inhibited that of Salmonella serovar Enteritidis S003, indicating potential prebiotic properties by the action of mannanase from K. oxytoca.

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“…The highest volumetric and specific enzyme activities of 13,073 nkat/ml (±1,027) and 1,020 nkat/(mg dcw) (±100), respectively, were produced by Y. lipolytica[man1] [13] after 5 days of cultivation. The use of the LIP2 secretion signal resulted in a 26-fold lower b-mannanase activity, compared to activities obtained using b-mannanase's own secretion signal, with the highest volumetric b-mannanase activity of 496.2 nkat/ml (±22.4) obtained with Y. lipolytica[man1-LIP2] [4]. Both homologous and heterologous secretion signals have been used successfully in Y. lipolytica [10], with the most common homologous secretion signals used being the XPR2 prepro region [23], the XPR2 pre-region alone [24], the prepro region of the Y. lipolytica LIP2 gene [25] and a hybrid between XPR2 and LIP2 prepro regions [14].…”

Section: Construction Of Expression Vectors and Recombinant Strainsmentioning

confidence: 98%

“…3.2.1.78) belongs to the glycosyl hydrolase family and has been cloned from bacterial and fungal origins [1][2][3][4]. b-mannanase catalyses the random hydrolysis of b-1,4-mannans, which forms the main chains of mannans and heteromannans, and is useful in several industrial processes such as extraction of vegetable oils from leguminous seeds, the reduction of viscosity of coffee extracts during the manufacture of instant coffee [5] and the biobleaching of softwood Kraft pulps to enhance extractability of lignin [6,7].…”

Section: Introductionmentioning

confidence: 99%

Heterologous Expression and Optimized Production of an Aspergillus aculeatus Endo-1,4-β-mannanase in Yarrowia lipolytica

2009

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The Aspergillus aculeatus MRC11624 man1 gene, encoding an endo-beta-1,4-mannanase, was cloned and expressed in the promising heterologous enzyme producer, the ascomycetous yeast Yarrowia lipolytica. Both single- and multi-copy transformants were constructed, and the secretion of the enzyme was evaluated as an in-frame fusion with the LIP2 secretion signal, as well as with its natural secretion signal. In shake-flask analysis, the highest volumetric enzyme activity (13,073 nkat/ml) and specific enzyme activity (1,020 nkat/(mg dcw)) were obtained with a multi-copy integrant utilizing beta-mannanase's own secretion signal. The best beta-mannanase-producing strain was subsequently evaluated in batch fermentation and resulted in a maximum volumetric enzyme activity of 6,719 nkat/ml. Fed batch fermentations resulted in a 3.9-fold increase in volumetric enzyme activity compared with batch fermentation, and a maximum titre of 26,139 nkat/ml was obtained. The results reported in this study indicate that Y. lipolytica is a promising producer of A. aculeatus beta-mannanase, producing higher beta-mannanase activity than that of recombinant Saccharomyces cerevisiae or Aspergillus niger when cultivated in shake flasks, which is encouraging for the use of the enzyme in industrial processes such as extraction of vegetable oil from leguminous seeds and the reduction in viscosity of coffee extracts.

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Cloning, sequence analysis, and heterologous expression of a β-mannanase gene from Bacillus subtilis Z-2

Cited by 31 publications

References 25 publications

Microbial Mannanases: Properties and Applications

Microbial Mannanases: Properties and Applications

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Heterologous Expression and Optimized Production of an Aspergillus aculeatus Endo-1,4-β-mannanase in Yarrowia lipolytica

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