Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria

Laribi-Habchi, Hassiba; Bouanane‐Darenfed, Amel; Drouiche, Nadjib; Pauss, André; Mameri, N.

doi:10.1016/j.ijbiomac.2014.10.035

Cited by 72 publications

(42 citation statements)

References 34 publications

(37 reference statements)

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“…So far, many microbial chitinases have been identified and characterized [1,12,13], whereas there is still few information on the chitinases from marine bacteria [10,11,14,15]. Two chitinases from marine bacterium Paenibacillus barengoltzii have been reported in our recent studies: PbChi70 is an endo type chitinase with a molecular mass of 70.6 kDa.…”

Section: Discussionmentioning

confidence: 99%

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Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Yan

Wang

et al. 2016

International Journal of Biological Macromolecules

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Section: Discussionmentioning

confidence: 99%

“…[10], Massili timonae [3], Alcaligene faecalis [11], Paenibacillus sp. [7], Bacillus cereus [9], Bacillus licheniformis [12], Chitinibacter sp. [13] and Pseudoaltermonas tunicata [14].…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Yan

Wang

et al. 2016

International Journal of Biological Macromolecules

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“…Their outstanding properties explain the craze for these natural macromolecules extracted from crustacean shells, considered so far as waste. Chitin is a linear polymer which has a similar structure to cellulose, but it is an amino polysaccharide with acetamide groups, C-2 instead of the hydroxyl Laribi-Habchi et al 2015). Its chemical structure is a sequence of monomeric units linked by a glycosidicbond (1-4) N-acetyl-(beta)-D-glucosamine.…”

Section: Introductionmentioning

confidence: 99%

Effects of chitin and its derivatives on human cancer cells lines

Bouhenna

Salah

Bakour

et al. 2015

Environ Sci Pollut Res

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The present study is focused on the effect of chitin derivatives against human cancer cell lines RD and Hep2. As an outcome from this research, chitin was cytotoxic at IC50 = 400 μg/ml and 200 μg/ml against Hep2 cells and RD cells lines, respectively. Irradiated chitin had an IC50 value of 450 μg/ml for Hep2 and an IC50 of 200 μg/ml for RD. The lowest IC50 is attributed to chitosan, 300 μg/ml in Hep2 and 190 μg/ml in RD.

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“…Chitinase activity at temperature 20°C was only found on S. marcescens KAHN 15.12 although, it was lower than the optimum temperature. The same result also reported that chitinase had optimum activity between 35-75°C (Wang et al, 2002;Dai et al, 2011;Tu et al, 2010;Zarei et al, 2011;Asril et al, 2014;Laribi-Habchi et al, 2015).…”

Section: Discussionmentioning

confidence: 59%

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

Azizah¹,

Mubarik²,

Sudirman³

2015

Research J. of Microbiology

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The objective of this research was to screen and identify of chitinolytic bacteria which have an ability to inhibit the growth of G. boninense and also to characterize its chitinase activity on degrading the chitin of G. boninense. Screening of chitinolytic bacteria against G. boninense by using dual culture method on Potato Dextrose Agar (PDA) showed that bacterial isolates SAHA 12.07 and KAHN 15.12 had the highest percentage inhibition of 68,19 and 40, 29%, respectively. Based on 16S rRNA identifications, SAHA 12.07 and KAHN 15.12 were identified as Bacillus amyloliquefaciens and Serratia marcescens, respectively. Isolate SAHA 12.07 produced optimum chitinase at 48 h and KAHN 15.12 at 54 h of incubation in chitin medium. Crude chitinase of SAHA 12.07 and KAHN 15.12 have precipitated by acetone at 60 and 20%, respectively. Chitinase activity had active at pH 4-10 and temperature about 20-80°C. In vitro lysis of G. boninense bioassay showed that the chitinase of SAHA 12.07 and KAHN 15.12 were capable to inhibit the growth of mycelium G. boninense and could release of N-acetylglucosamine by incubation of G. boninense with partially purified enzyme.

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Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria

Cited by 72 publications

References 34 publications

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Effects of chitin and its derivatives on human cancer cells lines

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

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