Partition of glucose oxidase from Aspergillus niger in aqueous two-phase systems based on salt and polyethylene glycol

Abstract

The aim of this work was to study the isolation of glucose oxidase (GOx)

Evaluation of Antimicrobial Activity of Glucose Oxidase from Aspergillus niger EBL-A and Penicillium notatum

“…Glucose oxidase by A. niger and P. notatum showed specific activity of 29.09 and 25.72 U mg -1 , respectively. Singh and Verma (2010) reported the production of glucose oxidase by A. niger and obtained 3.3 U mg -1 specific activity of the enzyme after PEG based two-phase isolation system. After gel filtration chromatography, specific activity of enzyme was 62.0 and 59.37 U mg -1 by A. niger and P. notatum, respectively (Fig.…”

Isolation, purification, and investigation of some properties of glucose oxidase of the wood-degrading fungus Lentinus (Panus) tigrinus strain VKM F-3616D

“…2, and the purification results are shown in Table 1. Compared with previous reports, the yield of the enzyme was small, but the degree of purification was quite high (Kelley and Reddy 1986;Abbas and Mahmood 2007;Zia et al 2007;Bhatti and Saleem 2009;Singh and Verma 2010;Hwang et al 2011;Singh and Verma 2013).…”

“…There was a clear band corresponding to a molecular mass of approximately 80 kDa. Based on published data (Kelley and Reddy 1986;Abbas and Mahmood 2007;Zia et al 2007;Bhatti and Saleem 2009;Singh and Verma 2010;Hwang et al 2011;Singh and Verma 2013), the enzyme probably consists of two subunits that differ insignificantly in molecular masses.…”

“…The GOx of fungi have a molecular weight in the range of 140 kDa to 186 kDa and typically consist of two identical subunits of the polypeptide chain covalently bound by disulfide bonds (Kelley and Reddy 1986;Abbas andMahmood 2007 Zia et al 2007;Bhatti and Saleem 2009;Singh and Verma 2010;Hwang et al 2011;Singh and Verma 2013). The molecular weight of GOx from L. tigrinus was calculated using electrophoresis, in non-denaturing conditions with 4% (stacking gel) and 12% (separating gel) of PAGE, and was determined to be 160 ± 10 kDa, as shown in Fig.…”