Separation and limited characterization of three polygalacturonases of Aspergillus niger

Behere, A.; Satyanarayan, Vaduvatha; Padwal-Desai, S. R.

doi:10.1016/0141-0229(93)90042-z

Cited by 21 publications

(9 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The same pH optimum was reported for PGs from Asergillus niger (Behere et al 1993), T. harzianum (Mohamed et al 2006). The effect of pH on the stability of P. janthinellum PGII was at different pH's for 4 h. The results showed that the enzyme was the most stable in pH of 6.0, with 90-100% of the full activity in a broader pH range of 4.0-8.0 (Fig.…”

Section: Characterization Of Exo-pgsupporting

confidence: 59%

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: 59%

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

“…The optimum pH and temperature determined for both enzymes did not differ greatly from those reported for other fungal exopolygalacturonases (2,9). P. frequentans secretes 7 polygalacturonases, of which one endo-PG and one exo-PG have been characterized (Chellegatti et al, personal communication).…”

Section: Resultsmentioning

confidence: 82%

Partial purification and characterization of exopolygalacturonase II and III of Penicillium frequentans

Barense¹,

Chellegatti²,

Fonseca³

et al. 2001

Braz. J. Microbiol.

View full text Add to dashboard Cite

Previous studies from our laboratory have demonstrated that the fungus Penicillium frequentans produces high levels of polygalacturonase and pectinesterase. Endopolygalacturonase I (Endo-PG I) and Exopolygalacturonase I (Exo-PG I) were previously purified and characterized. In the present study two extracellular polygalacturonases were separated, partially purified and biochemically characterized. Both were characterized as exopolygalacturonases so they were named exopolygalacturonase II (Exo-PG II) and exopolygalacturonase III (Exo-PG III) which had a molecular mass of 63 kDa (Exo-PG II) and 79 kDa (Exo-PG III). The Km values were 1.6 and 0.059 g/L and the Vmax values were 2571 and 185 U/mg, respectively. The optimum temperature was 50ºC for both enzymes, while the optimum pH was 5.0 for Exo-PG II and 5.8 for Exo-PG III.

show abstract

“…It is well documented, that several organisms are able to produce pectin degrading enzymes including plants, filamentous fungi, bacteria and yeast [9][10][11][12]. For industrial purposes moulds such as Aspergillus niger, Coniotryrium diplodiela, Penicillum and Rhizopus species are preferred, because as much as 90% of the enzyme can be excreted into the culture medium [9,[13][14][15].…”

Section: Introductionmentioning

confidence: 99%

“…In this study, Aspergillus sojae ATCC 20235 (from here on A. sojae only), which has been mostly used in the production of a well-known Japanese food (koji), by means of solid-state fermentation [12] is considered in the production of polygalacturonase enzyme (PG), which attracts the most attention among the family of pectionolytic enzymes due to its wide use. To best of our knowledge there is no literature report on the pectinase production by this organism in submerged or solid state fermentation.…”

Section: Introductionmentioning

confidence: 99%

Optimization of biomass, pellet size and polygalacturonase production by Aspergillus sojae ATCC 20235 using response surface methodology

Tarı

Gogus

Tokatlı

2007

Enzyme and Microbial Technology

View full text Add to dashboard Cite

A two-step optimization procedure using central composite design with four factors (concentrations of maltrin and corn steep liquor (CSL), agitation speed and inoculation ratio) was used in order to investigate the effect of these parameters on the polygalacturonase (PG) enzyme activity, mycelia growth (biomass) and morphology (pellet size) of Aspergillus sojae ATCC 20235. According to the results of response surface methodology (RSM), initial concentrations of maltrin and CSL and agitation speed were significant (p < 0.05) on both PG enzyme production and biomass formation. As a result of this optimization, maximum PG activity (13.5 U/ml) was achievable at high maltrin (120 g/l), at low CSL (0 g/l), high agitation speed (350 rpm) and high inoculation ratio (2 × 10 7 total spore). Similarly, maximum biomass (26 g/l) could be obtained under the same conditions with only the difference for higher level of CSL requirement. The diameter of pellets in all optimization experiments ranged between 0.05 and 0.76 cm. The second optimization step improved the PG activity by 74% and the biomass by 40%.

show abstract

Separation and limited characterization of three polygalacturonases of Aspergillus niger

Cited by 21 publications

References 19 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

Partial purification and characterization of exopolygalacturonase II and III of Penicillium frequentans

Optimization of biomass, pellet size and polygalacturonase production by Aspergillus sojae ATCC 20235 using response surface methodology

Contact Info

Product

Resources

About