Purification and characterization of an exo-polygalacturonase from Pycnoporus sanguineus

Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Molina, César; Sampietro, Diego Alejandro; Soberón, José Rodolfo; Vattuone, Marta Amelia

doi:10.1016/j.mycres.2009.09.007

Cited by 12 publications

(5 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several reports in the literature corroborate this result and show enzymes with similar reaction mode. Sakamoto et al (2002) describe two A. niger exo-PGs and Quiroga et al (2009) describe one Pycnoporus sanguineus exo-PG.…”

Section: Discussionmentioning

confidence: 99%

“…Pectinases have several applications in industry, especially in the extraction and clarification of wine and fruit juice, vegetable fibre degumming, vegetable oil extraction, coffee fermentation, degumming and waste water treatment and in the animal feed industry (Quiroga et al ; Dey and Banerjee ; Garg et al ; Trindade et al ). Of commercial pectinases, most enzymes are produced from fungal sources such as Aspergillus sp.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

et al. 2019

View full text Add to dashboard Cite

Aims The aim of this work was to characterize and apply a polygalacturonase of Penicillium janthinellum new strain VI2R3M. Methods and Results The polygalacturonase obtained from P. janthinellum VI2R3M was incubated in cultures of passion fruit peel and was partially purified by ion‐exchange chromatography and gel filtration. The enzyme showed a relative molecular mass of 102·0 kDa, maximum activity at pH 5·0, temperature of 50°C, 100% stablity at 50°C and 80% stablity at pH 3·0–5·0. The apparent Km, Vmax and Kcat values for hydrolyzing polygalacturonic acid were 2·56 mg ml−1, 163·1 U mg−1 and 277 s−1 respectively. The polygalacturonase presented exo activity and was activated by Mg2+. The juices treated with polygalacturonase presented increases in transmittance with reduction in colour. Conclusions The results suggest that the new lineage P. janthinellum VI2R3M presents a high yield of an exo‐polygalacturonase induced by agro‐industrial residues, with excellent activity and stability in acidic pH and at 50°C. Significance and Impact of the Study The use of agro‐industrial residue to obtain the polygalacturonase can contribute to a decrease enzyme production cost. The results of the activity, stability to acidic pH and excellent performance in the clarification of juices show that the enzyme is promising for industrial application.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Pectin, an acidic polysaccharide whose basic structural repeats are α-1,4-linked-D-galacturonic acid, is widely found in the middle lamella and primary cell wall of plants [22]. As an important renewable resource, pectin has great potential applications in the biomedical, food, agricultural, and other industries [18]. The degradation of pectin is mainly based on pectinase, including pectin methyl esterases (PME, E.C.…”

Section: Introductionmentioning

confidence: 99%

Secretory Expression and Characterization of an Acidic Endo-Polygalacturonase from Aspergillus niger SC323 in Saccharomyces cerevisiae

Zhou¹,

Li²,

Guo³

et al. 2015

Journal of Microbiology and Biotechnology

View full text Add to dashboard Cite

The endo-polygalacturonase gene (endo-pgaA) was cloned from DNA of Aspergillus niger SC323 using the cDNA synthesized by overlapping PCR, and successfully expressed in Saccharomyces cerevisiae EBY100 through fusing the α-factor signal peptide of yeast. The full-length cDNA consists of 1,113 bp and encodes a protein of 370 amino acids with a calculated molecular mass of 38.8 kDa. After induction by galactose for 48 h, the activity of recombinant endo-PgaA in the culture supernatant can reach up to 1,448.48 U/mg. The recombinant protein was purified to homogeneity by ammonium sulfate precipitation and gel filtration column chromatography and subsequently characterized. The optimal pH and temperature of the purified recombinant enzyme were 5.0 and 50°C, respectively. The Michaelis-Menten constant (Km) and maximal velocity (Vmax) of the enzyme for pectin were 88.54 μmol/ml and 175.44 μmol/mg/min, respectively. The enzyme activity was enhanced by Ca(2+), Cu(2+), and Na(+), and strongly inhibited by Pb(2+) and Mn(2+). The pectin hydrolysates were mainly galacturonic acid and other oligo-galacturonates. Therefore, these characteristics suggest that the recombinant endo-PgaA may be of potential use in the food and feed industries.

show abstract

“…Determinations of optimal temperature for pectinases from different sources are closely related, for instance 60˚C for Acrophialophora nainiana [14] or 65˚C for Paenibacillus sp [38] and Paecilomyces variotii [39]. Optimal temperature of polygalacturonases from Rhizomucor pusillus [18], Penicillium viridicatum [15], Thermoascus aurantiacus [20], Pycnoporus sanguineus [40] and A. giganteus [35] ranged from 55˚C to 65˚C. Other optimal temperatures are registered as 45˚C for Neurospora crassa [23], 40˚C for T. harzianum [32] and E. carotovora [24].…”

Section: Physicochemical Characterizationmentioning

confidence: 99%

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

Adalberto¹,

Golfeto²,

Moreira³

et al. 2016

AER

View full text Add to dashboard Cite

The present study aimed to purify and characterize one polygalacturonase from L. gongylophorus (PGaseLg), the symbiotic fungus of Atta sexdens. The enzyme was isolated by salting out of crude extract followed by two chromatographic steps. PGaseLG was identified with MS analysis and molecular exclusion chromatography revealed the monomeric nature of a protein with an estimated molecular weight of about 39 kDa. PGaseLg has an optimum temperature of 60˚C and optimum pH activity at 5.0. Using polygalacturonate as a substrate, the calculations of KM, Vmax and kcat were 0.65 mg•mL −1 , 1800 μmol•min −1 •mg −1 and 35.97 s −1 , respectively. The enzyme was stable for more than 3 h at 50˚C at pH 5.0; otherwise, at lower or higher pH values, the PGaseLg was less stable. The influence of several metals, EDTA and β-mercaptoethanol on enzyme activity was also determined. Thin layer chromatography (TLC) analyses indicated that PGaseLg is an exopolygalacturonase.

show abstract

Purification and characterization of an exo-polygalacturonase from Pycnoporus sanguineus

Cited by 12 publications

References 19 publications

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

Secretory Expression and Characterization of an Acidic Endo-Polygalacturonase from Aspergillus niger SC323 in Saccharomyces cerevisiae

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

Contact Info

Product

Resources

About

Purification and characterization of an exo-polygalacturonase from Pycnoporus sanguineus

Cited by 12 publications

References 19 publications

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

Secretory Expression and Characterization of an Acidic Endo-Polygalacturonase from Aspergillus niger SC323 in Saccharomyces cerevisiae

Characterization of an Exopolygalacturonase from &lt;i&gt;Leucoagaricus gongylophorus&lt;/i&gt;, the Symbiotic Fungus of &lt;i&gt;Atta sexdens&lt;/i&gt;

Contact Info

Product

Resources

About

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>