Contribution to Phenotypic and Genotypic Characterization of Bacillus licheniformis and Description of new Genomovars

Manachini, P. L.; Fortina, María Grazia; Levati, Laura; Parini, Carlo

doi:10.1016/s0723-2020(98)80064-7

Cited by 20 publications

(17 citation statements)

References 31 publications

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“…According to the physiological and microscopic tests, both F5 and F11 are suggested to be representatives of the B. licheniformis species. These findings agree with the fact that no extrachromosomal elements (approximately 1 to 20 kb in size) could be detected within cells of F5 and F11 (data not shown) since small plasmids are rarely found in B. licheniformis strains (6 to 25%) (17,34). However, definite evidence for the affiliation of the isolates with the species B. licheniformis was obtained from sequencing the 16S rRNA gene, including the hypervariable regions V1 to V3; 100% identity to B. licheniformis DSM13/ATCC 14580, which was totally sequenced only recently, was found (Fig.…”

Section: Resultssupporting

confidence: 88%

“…B. licheniformis is a ubiquitously occurring bacterium that can routinely be isolated from a number of different sources, such as soil (17) and wasted organic material (the present study). Physiological tests (API) (14) and 16S rRNA gene comparison (9), as well as microscopic and macroscopic investigations, revealed only faint differences between the bacterial isolates F5 and F11.…”

Section: Discussionmentioning

confidence: 99%

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Isolation and Molecular Characterization of Chitinase-Deficient Bacillus licheniformis Strains Capable of Deproteinization of Shrimp Shell Waste To Obtain Highly Viscous Chitin

Waldeck

Daum

Bisping

et al. 2006

Appl Environ Microbiol

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Proteolytic but chitinase-deficient microbial cultures were isolated from shrimp shell waste and characterized. The most efficient isolate was found to be a mixed culture consisting of two Bacillus licheniformis strains, which were first determined microscopically and physiologically. Molecular characterization was carried out by sequencing the 16S rRNA gene of both strains. According to the residual protein and ash content, the chitin obtained by fermentation of such a mixed culture was found to be comparable to a commercially available, chemically processed product. However, the strikingly high viscosity (80 versus 10 mPa of the commercially available sample) indicates its superior quality. The two strains differed in colony morphology and in their secretion capabilities for degradative extracellular enzymes. Sequencing of the loci encoding amylase, cellulase, chitinases, and proteases, as well as the degS/degU operon, which is instrumental in the regulation of degradative enzymes, and the pga operon, which is responsible for polyglutamic acid production, revealed no differences. However, a frameshift mutation in chiA, encoding a chitinase, was validated for both strains, providing an explanation for the ascertained absence of chitinolytic activities and the concomitant possibility of producing highly viscous chitin in a fermentational deproteinization process.Chitin (a polysaccharide consisting of ␤-1,4-linked N-acetyl-D-glucosamine moieties) is the second most abundant biopolymer on earth; thus, it represents a nearly constant source of renewable raw material. Along with its deacetylated derivative chitosan, chitin recently has gained biotechnological significance, not only because of favorable pharmaceutical features, such as antimicrobial, anticholesterol, and antitumor activities, but also because of its potential for wastewater treatment, drug delivery, and wound healing and as a dietary fiber (26).Approximately 50 to 60% of the total weight of shellfish, such as shrimp, crab, and krill, consists of nonedible material, i.e., "heads" and exoskeletons rich in chitin but also protein, which form, on the one hand, major environmental pollutants as a result of uncontrolled dumping (12). On the other hand, however, due to their chemical composition (20 to 30% chitin, 20 to 40% protein, 30 to 60% minerals, and 0 to 14% lipids) and their actual availability from seafood industries, shrimp waste also constitutes the major source for chitin and chitosan production (21). Currently applied methods to purify and modify chitin from such material and to transform it to useful carbohydrate products involve harsh chemical treatments accompanied by uncontrollable hydrolysis and chemical modifications that eventually result in the formation of undesired by-products such as irregularly deacetylated polymers (33).Exploitation limits are mainly set by the purification costs, which mainly arise from removal of proteins and calcium carbonate by alternating acid and alkali treatment, ultimately resulting in large amounts of aque...

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Section: Resultssupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Isolation and Molecular Characterization of Chitinase-Deficient Bacillus licheniformis Strains Capable of Deproteinization of Shrimp Shell Waste To Obtain Highly Viscous Chitin

Waldeck

Daum

Bisping

et al. 2006

Appl Environ Microbiol

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“…Manachini et al [21] studied 182 isolates attributed to B. licheniformis on the basis of phenotypic tests. Despite the high phenotypic similarities, DNA^DNA reassociation studies showed three very distinct groups that were therefore regarded by Manachini et al [21] as genomovars of B. licheniformis. Ishihara et al [22] found two clusters within 22 laboratory stock B. licheniformis strains, based on the distribution and variation of bacitracin synthetase gene sequences and erythromycin resistance.…”

Section: B Licheniformis Contaminates Industrial Processes [5^7]mentioning

confidence: 99%

Genotypic diversity amongBacillus licheniformisstrains from various sources

Clerck

Vos

2004

FEMS Microbiology Letters

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Bacillus licheniformis is exploited industrially for the production of enzymes and has been shown to exhibit pathogenic properties. Because of these divergent characteristics, questions arise concerning intraspecies diversity. A comparative study by means of combined repetitive polymerase chain reaction, rpoB and gyrA sequencing, 16S rDNA targeted probe analysis, DNA^DNA hybridizations, gelatinase tests and antibiotic susceptibility tests was performed on a set of strains from diverse sources, including strains with pathogenic potential. B. licheniformis was found to consist of two lineages that are distinguished genotypically.

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“…While, there are a lot of work related with the proteases from alkaliphiles and thermophiles (Mabrouk et al, 1999;Joo and Chang, 2005;Kazan et al, 2005), proteases from halophiles and moderate halophiles have not been investigated extensively. A few proteases from halophilic bacteria have been studied (Manachini et al, 1998;Ventosa et al, 1998;Gimènez et al, 2000;Joo and Chang, 2005;Amoozegar et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…According to carbon utilisation, there were some differences between isolate BA17 and 98 different B. licheniformis strains studied by Manachini et al (1998). Bacillus licheniformis BA17 was able to utilise 25 carbohydrates out of 58 carbon sources examined.…”

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confidence: 96%

Isolation and identification of alkaline protease producer halotolerantBacillus licheniformis strain BA17

et al. 2007

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An alkaline protease producer Bacillus licheniformis strain was isolated from Van Lake in Turkey. The strain is Gram positive, aerobic, motile, sporulating rod-shaped bacterium. Spores were ellipsoidal and positioned central in nonswollen sporangium. The cells were able to grow well at a pH range of 5.7-10. The optimal growth temperature was found to be 37 °C. Growth at a wide range of NaCl concentration (from 0 to 20%) showed that BA17 is halotolerant. Main fatty acid composition of BA17 was anteiso-C15:0 and iso-C15:0. The strain was presumptively identified as B. licheniformis according to 16S rDNA gene sequence analysis. The most appropriate medium for the growth and protease production is composed of 0.5% yeast extract, 0.5% NaNO 3 , 0.02% MgSO 4 ·7H 2 O, 0.1% K 2 HPO 4 and 0.5% maltose. The optimum temperature and pH of the alkaline protease of strain BA17 were found to be 60 o C and pH 11, respectively. The activity was completely lost in the presence of PMSF, suggesting that the preparation contains serine-alkaline protease(s).

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Contribution to Phenotypic and Genotypic Characterization of Bacillus licheniformis and Description of new Genomovars

Cited by 20 publications

References 31 publications

Isolation and Molecular Characterization of Chitinase-Deficient Bacillus licheniformis Strains Capable of Deproteinization of Shrimp Shell Waste To Obtain Highly Viscous Chitin

Isolation and Molecular Characterization of Chitinase-Deficient Bacillus licheniformis Strains Capable of Deproteinization of Shrimp Shell Waste To Obtain Highly Viscous Chitin

Genotypic diversity amongBacillus licheniformisstrains from various sources

Isolation and identification of alkaline protease producer halotolerantBacillus licheniformis strain BA17

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