Constitutive exo-pectinase produced byAspergillus sp. CH-Y-1043 on different carbon source

Aguilar, Gonzalo Galicia; Huitrón, Carlos

doi:10.1007/bf01088189

Cited by 88 publications

(40 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A group of enzymes popularly known as pectinases are associated with degradation of pectin and includes exo-and endo-polygalacturonases (PGs, E.C 3.2.115), pectin methyl esterases (PME.E.C 3.2.1.11), pectate lyases (PL,E.C 4.2.2.9) and pectin lyases (PNL 4.2.2.10). These enzymes are widely distributed in higher plants and microorganisms (Whitaker 1990) and are of prime importance for plants as they help in cell wall extension and softening of some plant tissues during maturation and storage (Aguilar and Huirton 1990;Sakai 1992). They also aid in maintaining ecological balance by causing decomposition and recycling of waste plant materials.…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

et al. 2017

View full text Add to dashboard Cite

Using solid-state fermentation, production of an industrially important pectin lyase from a fungal strain Fusarium oxysporum MTCC 1755 was attempted, which was further subjected to purification and characterization. The enzyme was purified by three steps, namely ammonium sulfate fractionation, cation-exchange chromatography on CM cellulose followed by gel filtration chromatography using Sephadex G-100 column. A 16-fold purification with 31.2% yield and 3.2 U/mg specific activity was achieved. The optimum pH of the purified enzyme was 9.0 and stability ranged from pH 5.0-7.0 for 24 h. Optimum temperature of purified enzyme was found to be 40°C while temperature stability ranged from 10 to 50°C for 30 min. The K m and k cat of the enzyme was 1.75 mg/ml and 83.3 s -1 , respectively. The purified enzyme was found to be highly stimulated by Ca 2? ions while sugars like mannitol and sorbitol, and salts like NaCl and CaCl 2 enhanced the thermostability. The purified pectin lyase was found suitable for retting of Crotolaria juncea fiber.

show abstract

Section: Introductionmentioning

confidence: 99%

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

et al. 2017

View full text Add to dashboard Cite

show abstract

“…These partially degrade pectic substances, releasing low-molecular-mass'products which induce the pectinase synthesis (Leone & Van den Heuvel, 1987). Aspergillus constitutively produces exo-pectinase when grown on glucose, sucrose, fructose, glycerol or galacturonic acid (Aguilar & Huitron, 1990).…”

Section: Introductionmentioning

confidence: 99%

Extracellular polygalacturonases from Penicillium frequentans: Separation and regulatory aspects

Siessere

Vieira

Said

1992

Journal of General Microbiology

View full text Add to dashboard Cite

)~~~ Extracellular polygalacturonase activities of Penicilfium frequentans were induced by pectin and repressed, but not inactivated, by glucose. The absence of a carbohydrate source derepressed 50% of viscosity-diminishing activity and 36% of reducing-groups-releasing activity compared to production in the presence of pectin. High concentrations (30 mM and 50 mM) of D-galacturonic acid reduced only the viscosity-diminishing activity, and under these conditions the fungus grew poorly. Neither effect was observed if the mycelium had been previously induced by pectin. Polygalacturonase activities produced in the presence of pectin were separated by ion exchange chromatography. These enzymes eluted in six peaks, characterized as exopolygalacturonases I, I1 and 111 and endopolygalacturonases, I, I1 and 111.

show abstract

“…The number of reducing groups is expressed as the number of lmol galacturonic acid, glucose and xylose liberated after 30 min (pectinases and cellulases) and 10 min (xylanase) at 50°C, with respectively, 2% w/v citrus pectin in 0.05 M citrate buffer pH 4.8 (Aguilar and Huitron 1990), 1% CMC in 0.05 M citrate buffer pH 4.8 (Amouri and Gargouri 2006), or with 1% xylane in 0.05 M phosphate buffer pH 7. After incubation, 3 ml DNS reagent was added and the solution was boiled for 10 min.…”

Section: Pectinolytic Cellulasic and Xylolytic Activities Assaysmentioning

confidence: 99%

Constitutive over-expression of pectinases in Penicillium occitanis CT1 mutant is transcriptionally regulated

et al. 2011

View full text Add to dashboard Cite

The CT1 mutant of Penicillium occitanis hyperproduces extracellular pectinases constitutively since it secretes pectinases even on glucose-containing medium. We show here that all other hydrolytic enzymes remain at low activities in CT1, confirming the specificity of the regulatory mutation towards pectinases. We isolated, by RT-PCR and through the construction of a cDNA library, three fragments coding for: a pectin lyase (pnl1), a polygalacturonase (pga1) and a pectate lyase (pal1). These fragments were used as probes in Northern blots analysis of the wild type strain CL100 and the CT1 mutant of P. occitanis grown in three culture conditions. The CT1 mutant showed a very high amount of pnl1, pga1 and pal1 mRNA either in pectin, glucose or glycerol grown cells while in the wild type CL100 strain, all transcripts were undetectable even on pectin. These results suggest that the CT1 mutation affects a trans-regulatory transcriptional factor regulating pectinase expression.

show abstract

Constitutive exo-pectinase produced byAspergillus sp. CH-Y-1043 on different carbon source

Cited by 88 publications

References 13 publications

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

Extracellular polygalacturonases from Penicillium frequentans: Separation and regulatory aspects

Constitutive over-expression of pectinases in Penicillium occitanis CT1 mutant is transcriptionally regulated

Contact Info

Product

Resources

About