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Evaluation of Antimicrobial Activity of Glucose Oxidase from Aspergillus niger EBL-A and Penicillium notatum BABT
Zia,Muhammad Anjum; Riaz,Ayesha; Rasul,Samreen; Abbas,Rao Zahid.
This work aimed to study the production and purification of glucose oxidase by Aspergillus niger and Penicillium notatum using corn steep liquor as the substrate and evaluate its antimicrobial activity for use in pharmaceutical and food industries. The enzyme was purified by ammonium sulfate precipitation (60-85%), DEAE-cellulose ion exchange and Sephadex G-200 size exclusion chromatography. The crude enzyme extracts of A. niger and P. notatum showed 2.32 and 5.53 U mg-1 specific activities, respectively, which after desalting was 15.52 and 12.05 U mg-1, and after ion exchange and gel filtration chromatography was 29.09 - 62 and 25.72 - 59.37 U mg-1 for A. niger and P. notatum, respectively. The antimicrobial activity was determined by disc diffusion...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucose oxidase; Antimicrobial; Aspergillus niger; Penicillium notatum.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132013000600010
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Study on Thermodynamics and Adsorption kinetics of Purified endoglucanase (CMCase) from Penicillium notatum NCIM NO-923 produced under mixed solid-state fermentation of waste cabbage and Bagasse BJM
Das,Arpan; Ghosh,Uma; Mohapatra,Pradeep Kumar Das; Pati,Bikas Ranjan; Mondal,Keshab Chandra.
In the current study, one thermostable endoglucanase was purified from Penicillium notatum NCIM NO-923 through mixed solid state fermentation of waste cabbage and bagasse. The molecular weight of the purified enzyme was 55kDa as determined by SDS polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme had low activation energy (Ea) of 36.39KJ mol-1 for carboxymethyl cellulose hydrolysis and the enthalpy and entropy for irreversible inactivation was 87 kJ mol −1 and 59.3 J mol −1 K−1 respectively. The enzyme was quite thermostable with a Tm value of 62.2˚C. The pKa1 and pKa2 of ionizable groups of the active sites were 2.5 and 5.3 respectively. Apparent Km, Vmax and Kcat of the enzyme were found to be 5.2 mg mL-1, 80 U/gds and 322.4 sec-1 respectively....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Endoglucanase; Langmuir adsorption isotherm; Penicillium notatum; Solid state fermentation.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000300037
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