Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation

Silva, Dênis; Martins, Eduardo Silva; Leite, Rodrigo Simões Ribeiro; Silva, Roberto da; Ferreira, Viviani; Gomes, Eleni

doi:10.1016/j.procbio.2007.05.025

Cited by 37 publications

(31 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…2). This observation was in the range reported for PGs from several fungi, which have molecular masses ranging from 20 to 95 kDa (Gomes et al 2009, Silva et al 2007). In comparison with other Penicillium sp., lower molecular weights (24.1 kDa) were detected for PG from P. viridicatum (Mohamed et al 2003).…”

Section: Characterization Of Exo-pgsupporting

confidence: 78%

Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

Sun

et al. 2016

An. Acad. Bras. Ciênc.

View full text Add to dashboard Cite

A soil isolate, Penicillium janthinellum sw09 has been found to produce significant amounts of an extracellular pectinase subsequently characterized as exo-polygalacturonase (exo-PG). By optimizing growth conditions, P. janthinellum sw09 produced high amount of exo-PG (16.54 units/mL). The crude enzyme was purified by gel filtration chromatography and two exo-PG activity peaks (designated as PGI and PGII) were revealed. On SDS-PAGE analysis, purified PGII using DEAE-Sepharose FF column, was found to be a single band with a molecular mass of 66.2 kDa. The purified PGII exhibited maximal activity at the temperature of 45 o C and pH 5.0. The stability profiles show that PGII is more stable in the pH range of 4.0-8.0 and below 60 o C. The K m and V max for the enzyme was 1.74 mg/mL and 18.08 μmol/ (mL•min), respectively. Due to this enzymatic characterization, this pectinase is an attractive candidate for applications in degradation of pectin.

show abstract

Section: Characterization Of Exo-pgsupporting

confidence: 78%

Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

Sun

et al. 2016

An. Acad. Bras. Ciênc.

View full text Add to dashboard Cite

show abstract

“…Maciel et al (2011) obtained the maximum endo-and exo-PG activities of A. niger URM 4645 at pH 5.0 and 7.0, respectively. The maximum activity of exo-PG from P. viridicatum RFC3 was observed at pH 6.0 (Silva et al, 2007), Moniliella sp. SB9 at pH 4.5, and Penicillium sp.…”

Section: Enzyme Characterizationmentioning

confidence: 97%

“…For PL activity, the initial moisture content and temperature (2 × 3) interacted positively, such that an increase in the values of these variables resulted in an increase in the activity. The cultivation of microbial cells in an excess of water can lead to sticking of particles, limited gas exchange, and higher vulnerability to bacterial contamination, whereas that in low levels of water is correlated with reduced microbial growth, reduced enzyme stability, substrate swelling, and diffusion of nutrients (Silva et al, 2007).…”

Section: Production Of Pectinolytic Enzymesmentioning

confidence: 99%

“…The results are in agreement with those obtained by Silva et al (2002) with PG from P. viridicatum RFC3 that was stable at pH 5.0 to 8.0, retaining 80% of its activity at pH 9.0. Furthermore, Silva et al (2007) reported the stability of exo-PG from P. viridicatum RFC3 at pH 7.0 to 10.0. Maciel et al (2011) observed that endo-PG and exo-PG from A. niger URM 4645 were stable at pH 3.5 to 11.0, and more than 40 and 70% of the endo-and exo-PG activities were maintained, respectively.…”

Section: Enzyme Characterizationmentioning

confidence: 99%

See 1 more Smart Citation

Pectinolytic complex production by Aspergillus niger URM 4645 using yellow passion fruit peels in solid state fermentation

Maciel¹,

Herculano²,

Fernandes³

et al. 2014

Afr. J. Biotechnol.

View full text Add to dashboard Cite

The activities of endo-polygalacturonase (endo-PG), exo-polygalacturonase (exo-PG), pectin lyase (PL), and pectin methylesterase (PE), produced by Aspergillus niger URM 4645, were studied in solid state fermentation (SSF) using yellow passion fruit peels as substrate. The effect of substrate amount, initial moisture content, and temperature on pectinase production was studied using a full factorial design (2³). Maximum endo-PG, exo-PG, PL, and PE activities were 31.35, 7.98, 551,299.39, and 447.93 U g −1 dry substrate, respectively. Optimum activities of the four enzymes were obtained with 5.0 g of the substrate and an initial moisture content of 30% at 34°C with 96 h of fermentation. Optimum endo-PG activity was found at pH 7.5 at an optimum temperature of 40°C; exo-PG and PL at pH 7.0 at an optimum temperature of 80°C; and PE at pH 3.5 at an optimum temperature of 30°C. Endo-PG was stable at pH 7.0 to 8.0 at 40°C, and exo-PG and PL at pH 6.0 to 8.0 and 6.0 to 7.5, respectively at 60 to 70°C. PE was stable at pH 3.5 to 5.0 at 30 to 60°C. The enzyme production optimization clearly demonstrated the impact of process parameters on the yield of pectinolytic enzymes.

show abstract

“…This observation was in the range reported for exo-PGs from several fungi, which have molecular weight ranging from 20 to 95 kDa. 21,23 The molecular mass of the PG from A. niger NRRL3 was 32 kDa as estimated by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 24 In contrast, a heterodimer of 34 and 69 kDa subunit was detected for PG from A. niger MTCC 3323, 9 and two exo-PGs 1 and 2 from another A. niger had the molecular masses of 82 and 56 kDa, respectively.…”

Section: Characterization Of Exo-pgmentioning

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.

View full text Add to dashboard Cite

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.

show abstract

Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation

Cited by 37 publications

References 31 publications

Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

Pectinolytic complex production by Aspergillus niger URM 4645 using yellow passion fruit peels in solid state fermentation

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

Contact Info

Product

Resources

About