Stimulation of polygalacturonase production in an immobilized system by Aspergillus sp.: effect of pectin and glucose

Polygalacturonases (PG) are pectinolytic enzymes that have technological, functional and biological applications in food processing, fruit ripening and plant-fungus interactions, respectively. In the present, a microtitre plate methodology was used for rapid screening of 61 isolates of fungi from Aspergillus section Nigri to assess production of endo- and exo-PG. Studies of scale-up were carried out in a fixed bed reactor operated under different parameters using the best producer strain immobilised in orange peels. Four experiments were conducted under the following conditions: the immobilised cells without aeration; immobilised cells with aeration; immobilised cells with aeration and added pectin; and free cells with aeration. The fermentation was performed for 168 h with removal of sample every 24 h. Aspergillus niger strain URM 5162 showed the highest PG production. The results obtained indicated that the maximum endo- and exo-PG activities (1.18 U·mL−1 and 4.11 U·mL−1, respectively) were obtained when the reactor was operating without aeration. The microtitre plate method is a simple way to screen fungal isolates for PG activity detection. The fixed bed reactor with orange peel support and using A. niger URM 5162 is a promising process for PG production at the industrial level.

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“…Gattás et al . [24] reported the PG production using an Aspergillus sp. immobilised in 3% Ca-alginate.…”

Section: Resultsmentioning

confidence: 99%

Production of Polygalacturonases by Aspergillus section Nigri Strains in a Fixed Bed Reactor

et al. 2013

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“…Commercial pectinase preparation immobilized in 1% alginate by Sardar et al [29] exhibited pH stability in the pH range of 4.5 to 5.5. Polygalacturonase of Mucor sp-7 showed a wide range of pH stability between 4.0 and 8.0 [33]. The thermostability profile of immobilized polygalacturonase of M. circinelloides is shown in Fig.…”

Section: Figmentioning

confidence: 97%

“…• C [33]. The immobilized enzyme produced maximum activity (5.03 U/mg) after 15 Min of incubation; further incubation led to a decrease in activity, which might be due to product inhibition.…”

Section: Immobilization Of Polygalacturonase On Silicamentioning

confidence: 98%

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Effect of immobilized polygalacturonase from Mucor circinelloidesITCC‐6025 on wine fermentation

Sharma

Hiteshi

Gupta

2013

Biotech and App Biochem

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Pectinases are among the most widely distributed enzymes in bacteria, fungi, and plants. Almost all the commercial preparations of pectinases are produced from fungal sources. Mucor circinelloides ITCC-6025 produced polygalacturonase when grown in Riviere's medium containing pectin (methyl ester) as the sole source of carbon. Immobilization of purified polygalacturonase was done on silica gel with 86% efficiency. The enzyme took 60 Min to bind maximally on the support. The immobilized enzyme showed maximum activity at a temperature of 45°C (4.57 U/mg) and pH 5.4. The immobilized enzyme was reused for four cycles as it retained almost 55% of its activity. The immobilized enzyme treatment increased the formation of higher alcohols and phenolics during the course of wine formation from apple and plum juices, whereas there was a decrease in the amount of carbohydrates. The enzyme treatment also resulted in clarification of wine; there was an increase in transmittance at 650 nm (201.78% in the case of apple wine and 223.4% in the case of plum wine) as compared to the control (untreated wine).

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“…This implied that the selected conditions were really the most suitable. Gattás et al 22 found that the optimal pectin level was 2.0% (m/v) for exo-PG production by Aspergillus sp. CC1 in submerged culture, which suggests that the level of substance requirement for exo-PG production depends on the nature of the specific strain, though they belong to the same species (i.e., Aspergillus).…”

Section: Production Of Exo-pg In Flask Culturementioning

confidence: 99%

Production, Purification and Physicochemical Properties of an Exo‑Polygalacturonase from Aspergillus niger SW06

Ma¹,

He²,

Chen³

et al. 2016

J. Braz. Chem. Soc.

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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 activity in the presence of 1% citrus pectin at the temperature of 55 °C and pH of 5.0. The enzyme was stable within the pH range of 3.0-5.0 and below 60 °C. The Michaelis constant (K m ) and maximum velocity (V max ) of the enzyme was found to be 0.58 mg mL -1 and 20.66 μmol (mL min), respectively. The thermostable and acidic nature for the activity of this exo-PG make it possible to have wide range of industrial applications.

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Stimulation of polygalacturonase production in an immobilized system by Aspergillus sp.: effect of pectin and glucose

Cited by 5 publications

References 17 publications

Production of Polygalacturonases by Aspergillus section Nigri Strains in a Fixed Bed Reactor

Production of Polygalacturonases by Aspergillus section Nigri Strains in a Fixed Bed Reactor

Effect of immobilized polygalacturonase from Mucor circinelloidesITCC‐6025 on wine fermentation

Production, Purification and Physicochemical Properties of an Exo‑Polygalacturonase from Aspergillus niger SW06

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