Isolation, Identification, and Characterization of a Cellulolytic<i>Bacillus amyloliquefaciens</i>Strain SS35 from Rhinoceros Dung

Singh, Shuchi; Moholkar, Vijayanand S.; Goyal, Arun

doi:10.1155/2013/728134

Cited by 74 publications

(48 citation statements)

References 37 publications

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“…: JX674030) and gyrase A (GenBank accession no. : KF019284) gene . The medium composition and pH for CMCase production (as per optimization results of our previous study ) was: CMC–Na (19.0 g/L), yeast extract (8 g/L), peptone (2 g/L), K 2 HPO 4 (1 g/L), MgSO 4 ·7H 2 O (0.2 g/L), NaCl (1 g/L), pH = 5.6.…”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of acidic cellulase from Bacillus amyloliquefaciens SS35 for hydrolyzing Parthenium hysterophorus biomass

Singh

Dikshit

Moholkar

2014

Env Prog and Sustain Energy

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This study reports purification and characterization of an acidic endoglucanase (carboxymethylcellulase, CMCase) produced by Bacillus amyloliquefaciens SS35. Purification of enzyme was done using ion exchange chromatography (Yield = 2.1%, Purification fold = 18.5). The molecular weight of the CMCase was determined as ∼37 kDa. The purified CMCase was able to hydrolyze carboxymethylcellulose (CMC), barley–β–d–Glucan, lichenan, hydroxyethylcellulose, starch, and xylan, which indicated endoglucanase activity. However, the enzyme could not hydrolyze avicel and p–nitrophenyl–β–d–glucopyranoside (pNPG). These results were indications of absence of exoglucanase and β–glucosidase activity in the enzyme. Optimum temperature and pH for CMCase activity were determined as 55°C and 5.0, respectively. The enzyme also displayed high stability in temperature range of 20–40°C and pH range of 5.0–9.0 for more than 20 h with significant residual CMCase activity of 80%. Five metal ions, viz. Co2+, Ca2+, K+, Na+, Mn2+ were found to be cofactors of the enzyme that enhanced its activity, while other metal ions such as Fe3+, Zn2+, Hg2+ rendered inhibition effect on the enzyme. Using Lineweaver–Burk plot, the kinetic parameters Km and Vmax for CMCase were determined as 0.33 mg/mL and 4.19 μmol/mg/min, respectively. The asset of the enzyme was evaluated with hydrolysis of pretreated Parthenium hysterophorus. The total reducing sugar yield of 271 mg/g biomass was obtained. © 2014 American Institute of Chemical Engineers Environ Prog, 34: 810–818, 2015

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Section: Methodsmentioning

confidence: 99%

Purification and characterization of acidic cellulase from Bacillus amyloliquefaciens SS35 for hydrolyzing Parthenium hysterophorus biomass

Singh

Dikshit

Moholkar

2014

Env Prog and Sustain Energy

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“…Carboxymethyl cellulose yeast extract agar (CYA) medium containing in L −1 ; yeast extract, 1 g; K 2 HPO 4 ·3H 2 O, 0.25 g; (NH 4 ) 2 SO 4 , 2.5 g; MgSO 4 · 7H 2 O, 0.125 g; NaCl, 0.1 g; FeSO 4 · 7H 2 O, 0.0025 g; MnSO 4 · 4H 2 O, 0.025 g and CMC, 10 g was used for assay of cellulase enzyme [39,40]. The media were constructed in 1 L of distilled water, the components were mixed well, and pH was adjusted to 7.2 as mentioned above.…”

Section: Enzymes Production By the Fungi Inactivated By Sc-comentioning

confidence: 99%

Inactivation of Aspergillus Spores in Clinical Wastes by Supercritical Carbon Dioxide

Efaq

Rahman²,

Nagao³

et al. 2016

Arab J Sci Eng

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The present work investigated the inactivation of Aspergillus spp. spores by supercritical carbon dioxide (SC-CO 2 ) based on the destruction of enzyme activity and the alteration of spore morphology as documented using a scanning electron microscope (SEM). Six Aspergillus spp. included A. niger, Aspergillus sp. in section Nigri, A. fumigatus, A. tubingensis, A. hortai and Aspergillus sp. strain no 145 were isolated from clinical waste samples and inactivated by using SC-CO 2 at optimal conditions (35 MPa, 75 • C and 90 min). The inactivation of spores was determined by the culturing method. Aspergillus sp. strain no 145 and Aspergillus hortai were further analysed to quantify enzyme activity, and the morphology of spores was determined by SEM to demonstrate the inactivation mechanism. The results revealed that growth and enzyme activity of the SC-CO 2 treated fungal spores were not detected. The SEM observation demonstrated complete destruction of spore morphology and exsorption of protoplasmic contents. The findings proved the high efficiency of SC-CO 2 for the destruction of fungal contaminants in clinical wastes. B A. N. Efaq

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“…Culturable cellulolytic bacteria have been isolated from a wide array of environments ranging from soil, lakes [9], decomposing material [10], animal dung [11,12], rumen of ruminants and termite gut [13 -15], goldmines [16] and hot springs [17]. This clearly shows that bacteria have a wide range of natural habitats and this endows them with the capability of producing stable enzymes.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of a Thermostable Cellulase from Bacillus licheniformis Strain Vic Isolated from Geothermal Wells in the Kenyan Rift Valley

Kiio¹,

Jackim²,

Munyali³

et al. 2016

TOBIOTJ

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Cellulolytic microorganisms such as fungi and bacteria are responsible for much of the cellulose degradation in soils. Despite the vast number of cellulase producers, there is a deficiency of microorganisms that can produce significant amount of the three components of a cellulase system. i.e. CMCases, exoglucanases and β-glucosidases to efficiently degrade cellulose to fermentable products.Soil samples were collected from two sites of the Kenyan Rift valley; Hell's gate National Park and a geothermal well in Eburru hill at depths of 155 m, 156 m and 157 m. Isolation of cellulolytic bacteria was carried out using minimal media supplemented with 1% CMC. Isolates obtained were characterized using both morphological and molecular methods. A quantitative cellulolytic test was carried out to select the isolate with the highest specific activity. Additionally the cell-free supernatant was used for functional studies to determine the isolate's cellulase system components, optimum temperature, pH and time stability.Phylogenetic analyses indicated that all isolates associated mainly with members of the Bacillus licheniformis. All isolates were capable of utilizing CMC, avicel and Cellobiose as their sole carbon sources. Isolate 3 from a depth of 156 m in the well was identified as Bacillus licheniformis strain vic and selected for further functional studies. This isolate was found to bear the three enzyme components of a cellulase system. A cell free extract was noted to hydrolysecellobiose, Avicel and CMC with enzyme specific activities of 0.46878 U/mg, 0.18784 U/mg and 0.13571 U/mg respectively. Optimum temperature for activity measured over 60 minutes was found to be 60 o C with relatively high activity at both 70 o C and 80 o C. The optimum pH at the predetermined optimum temperature was found to be pH 5. The crude enzyme extract was stable for eight hours of incubation at 60 o C and pH 5 retaining 92.2% of its activity. This makes B.licheniformis strain vic a quite attractive isolate for potential application in industries.

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Isolation, Identification, and Characterization of a CellulolyticBacillus amyloliquefaciensStrain SS35 from Rhinoceros Dung

Cited by 74 publications

References 37 publications

Purification and characterization of acidic cellulase from Bacillus amyloliquefaciens SS35 for hydrolyzing Parthenium hysterophorus biomass

Purification and characterization of acidic cellulase from Bacillus amyloliquefaciens SS35 for hydrolyzing Parthenium hysterophorus biomass

Inactivation of Aspergillus Spores in Clinical Wastes by Supercritical Carbon Dioxide

Isolation and Characterization of a Thermostable Cellulase from Bacillus licheniformis Strain Vic Isolated from Geothermal Wells in the Kenyan Rift Valley

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