2016
DOI: 10.21577/0103-5053.20160210
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Production, Purification and Physicochemical Properties of an Exo‑Polygalacturonase from Aspergillus niger SW06

Abstract: In this study, exo-polygalacturonase (exo-PG) production from Aspergillus niger SW06 was optimized by central composition design and high amount of 21.51 units mL -1 could be achieved in optimizing growth conditions. Both gel filtration and ion exchange chromatography revealed a single exo-PG activity peak, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified protein showed a single band with a molecular mass of 66.2 kDa. The purified enzyme exhibited maximal activi… Show more

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Cited by 2 publications
(3 citation statements)
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“…The effect of enzyme extract concentration on enzyme stability may come from different facts: if the enzyme is multimeric and the first step of the inactivation is enzyme dissociation (but in this case the enzymes are described to be monomeric), if there are some enzyme–enzyme interactions with effect on enzyme stability (e.g., favoring inactivation by aggregation, or stabilizing the enzymes by forming some enzyme complexes), or if some component of the extract may have some effect on enzyme stability (some stabilizing reagent). To evaluate the effect of enzyme concentration on inactivation, two solutions with 1% (0.05 mg mL −1 of protein) and 10% (0.5 mg mL −1 of protein) of enzyme preparation were incubated at pH 10 at 4°C for PE, PG, and PL, at 25°C for PME and 50°C for CE.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The effect of enzyme extract concentration on enzyme stability may come from different facts: if the enzyme is multimeric and the first step of the inactivation is enzyme dissociation (but in this case the enzymes are described to be monomeric), if there are some enzyme–enzyme interactions with effect on enzyme stability (e.g., favoring inactivation by aggregation, or stabilizing the enzymes by forming some enzyme complexes), or if some component of the extract may have some effect on enzyme stability (some stabilizing reagent). To evaluate the effect of enzyme concentration on inactivation, two solutions with 1% (0.05 mg mL −1 of protein) and 10% (0.5 mg mL −1 of protein) of enzyme preparation were incubated at pH 10 at 4°C for PE, PG, and PL, at 25°C for PME and 50°C for CE.…”
Section: Resultsmentioning
confidence: 99%
“…The effect of enzyme extract concentration on enzyme stability may come from different facts: if the enzyme is multimeric and the first step of the inactivation is enzyme dissociation (but in this case the enzymes are described to be monomeric), [83][84][85][86][87] if there are some enzyme-enzyme interactions with effect on enzyme stability third sample for each enzyme was prepared with 1% enzyme preparation plus 9% inactivated enzyme solution after boiling. We cannot find any significant difference on the inactivation courses of all these preparations ( Figure 5).…”
Section: Influence Of the Enzyme Concentration On The Stability Of mentioning
confidence: 99%
“…In addition, the pore size of Fe 2 O 3 -PVA catalyst is much larger than that of the Fe 2 O 3 catalyst (inset of Figure 1 and Table 1). According to the data in Table 1 21,22 but they possess larger pore size, which helps the diffusion of products.…”
Section: Catalytic Activitymentioning
confidence: 99%