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Purification And Characterization Of Endoxylanase Xln-2 From Aspergillus Niger B03, Georgi Dobrev, Boriana Zhekova
Purification And Characterization Of Endoxylanase Xln-2 From Aspergillus Niger B03, Georgi Dobrev, Boriana Zhekova
Turkish Journal of Biology
An extracellular multiple form of endoxylanase was isolated from the xylanolytic complex of Aspergillus niger B03. The enzyme was purified to a homogenous form using ultrafiltration, anion exchange chromatography, and gel filtration. It was a nonglycosylated protein with a molecular weight of 20,000 Da as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and 21,000 Da as determined by gel filtration. The optimal pH for the enzyme action was 5.0 and the optimal temperature was 55 °C. Endoxylanase stability was significantly improved in the presence of glycerol and sorbitol. The enzyme activity was activated by Mn^{2+} and Co^{2+}, and it was …
An Anti-Shigella Dysenteriae Bacteriocin From Pediococcus Pentosaceus Mtcc 5151 Cheese Isolate, Renu Agrawal, Shylaja Dharmesh
An Anti-Shigella Dysenteriae Bacteriocin From Pediococcus Pentosaceus Mtcc 5151 Cheese Isolate, Renu Agrawal, Shylaja Dharmesh
Turkish Journal of Biology
A cheese isolate Pediococcus pentosaceus lactic acid bacterium, which has been deposited at the Microbial Type Culture Collection Centre Chandigarh with the accession number MTCC 5151, was tested for anti-Shigella dysenteriae activity and the bacteriocin was characterized. The protein band was observed with tricine sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) as a single band with a molecular mass of 23 kDa. This is a new and novel bacteriocin that inhibits S. dysenteriae and has not yet been reported from P. pentosaceus. It was purified on a Sephacryl column and the active fraction specific for anti-Shigella dysenteriae with 23 kDa …
Purification And Properties Of An Endoglucanase From Aspergillus Niger Vtcc-F021, Thi Hoa Pham, Dinh Thi Quyen, Ngoc Minh Nghiem
Purification And Properties Of An Endoglucanase From Aspergillus Niger Vtcc-F021, Thi Hoa Pham, Dinh Thi Quyen, Ngoc Minh Nghiem
Turkish Journal of Biology
An extracellular endoglucanase (EG) from Aspergillus niger VTCC-F021 was purified 2.09-fold to homogeneity with a yield of 18.4%. The enzyme had a molecular mass of 31 kDa and a specific activity of 14.122 U/mg protein. Optimum temperature was observed at 55 °C and optimum pH at 5. The enzyme was stable up to 50 °C and from pH 5 to 6 with residual activity >80% and 60%, respectively. The kinetic constants K_m and V_{max} determined for EG, with carboxyl methyl cellulose as a substrate, were 8.5815 mg CMC/mL and 20.121 U/mg protein, respectively. EDTA increased EG activity by 35% at …