First Insights into the Completely Annotated Genome Sequence of Bacillus licheniformis Strain 9945A

Rachinger, Michael; Volland, Sonja; Meinhardt, Friedhelm; Daniel, Rolf; Liesegang, Heiko

doi:10.1128/genomea.00525-13

Cited by 22 publications

(28 citation statements)

References 14 publications

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“…licheniformis strains are widely used in biotechnology for enzyme and antibiotics production [13]. This strain is known for thermostable amylase and for production of gamma-poly(glutamic acid) [14][15][16].…”

Section: Production and Purification Of Recombinant Laccasementioning

confidence: 99%

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Lončar

Božić

Vujčić

2016

Journal of Molecular Catalysis B: Enzymatic

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Please cite this article as: Nikola Lončar, Nataša Božić, Zoran Vujčić, Expression and characterization of a thermostable organic solevent-tolerant laccase from Bacillus licheniformis ATCC 9945a, Journal of Molecular Catalysis B: Enzymatic http://dx.Abstract Highlights  Bacillus licheniformis 9945a laccase is overexpressed in E. coli with yield 50 mg/L.  Temperature optimum of laccase is 90⁰C and pH optimum is 7.0. Enzyme is thermostable with a melting temperature of 79⁰C at pH 7.0. Presence of organic solvents reduces melting temperature but activity remains impaired. Lignin model compounds are dimerized after one electron oxidation of phenolic group. AbstractBacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90⁰C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79⁰C at pH 7.0 and above 70⁰C in range of pH 5.0-8.0, while having half-life of 50 min at 70⁰C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52ᴼC but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained 3 ~40% of initial activity. EDTA and 300 mM sodium-chloride have positive effect on activity.Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2-naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications.

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Section: Production and Purification Of Recombinant Laccasementioning

confidence: 99%

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Lončar

Božić

Vujčić

2016

Journal of Molecular Catalysis B: Enzymatic

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“…The high extracellular protease activity, the wrinkled colony phenotype and the adjustment of the transduction data to the presently available B. licheniformis genome sequence (Rachinger et al, 2013a;Rey et al, 2004;Veith et al, 2004) suggested that the general transition state regulator AbrB was possibly hit. Subsequent PCR analysis (included in Fig.…”

Section: M18 Has a Deletion In The Abrb-locusmentioning

confidence: 99%

Unravelling the genetic basis for competence development of auxotrophic Bacillus licheniformis 9945A strains

et al. 2014

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Bacterial natural genetic competence -well studied in Bacillus subtilis -enables cells to take up and integrate extracellularly supplied DNA into their own genome. However, little is known about competence development and its regulation in other members of the genus, although DNA uptake machineries are routinely encoded. Auxotrophic Bacillus licheniformis 9945A derivatives, obtained from repeated rounds of random mutagenesis, were long known to develop natural competence. Inspection of the colony morphology and extracellular enzyme secretion of two of these derivatives, M28 and M18, suggested that regulator genes are collaterally hit. M28 emerged as a 14 bp deletion mutant concomitantly displaying a shift in the reading frame of degS that encodes the sensor histidine kinase, which is part of the molecular switch that directs cells to genetic competence, the synthesis of extracellular enzymes or biofilm formation, while for M18, sequencing of the suspected gene revealed a 375 bp deletion in abrB, encoding the major transition state regulator. With respect to colony morphology, enzyme secretion and competence development, both of the mutations, when newly generated on the wild-type B. licheniformis 9945A genetic background, resulted in phenotypes resembling M28 and M18, respectively. All of the known naturally competent B. licheniformis representatives, hitherto thoroughly investigated in this regard, carry mutations in regulator genes, and hence genetic competence observed in domesticated strains supposedly results from deregulation.

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“…Our protein C1 from B. licheniformis HS10 was identified as carboxylase, a-amylase, catalasesorphage-like protein instead of chitinase by using MALDI-TOF/TOF-MS and blasting in NCBI. Among them, the highest coverage of putative carboxy peptidase (Protein ID:gi| 510141549), was dissociated 39 peptides [30]. This protein function is likely predicted from the genome of B. licheniformis.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of an antifungal protein from Bacillus licheniformis HS10

Wang

Zheng

et al. 2014

Biochemical and Biophysical Research Communications

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First Insights into the Completely Annotated Genome Sequence of Bacillus licheniformis Strain 9945A

Cited by 22 publications

References 14 publications

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Unravelling the genetic basis for competence development of auxotrophic Bacillus licheniformis 9945A strains

Isolation and characterization of an antifungal protein from Bacillus licheniformis HS10

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