Catalytic properties of a highly thermoactive polygalacturonase from the mesophilic fungus Penicillium occitanis and use in juice clarification

Tounsi, Hajer; Sassi, A. Hadj; Romdhane, Zamen Ben; Lajnef, Marwa; Dupuy, Jean-William; Lapaillerie, Delphine; Lomenech, Anne-Marie; Bonneu, Marc; Gargouri, Ali; Hadj-Taieb, Noomen

doi:10.1016/j.molcatb.2016.02.012

Cited by 24 publications

(24 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The PG activity was increased by Mg 2+ . Similar results were reported with the fungus P. occitanis , with increase in enzymatic activity by 130%(Tounsi et al ). Many enzymes require an additional chemical component, known as a cofactor, which may be one or more inorganic ions.…”

Section: Discussionsupporting

confidence: 89%

“…The higher activity at pH 5·0 is in the range of most fungal pectinases described, which have ideal pHs between 3·0 and 6·0, and which is also the optimum pH for the activity of PG from the fungi P. janthinellum sw09 and Penicillium occitanis (Ma et al ; Tounsi et al ). The pH stability shown in the present study is in agreement with Siddiqui et al (), who observed that the maximum stability of the PG is between pH 4·0 and 5·0; above this there is a decrease in the enzymatic activity.…”

Section: Discussionmentioning

confidence: 99%

“…According to Sassi et al (), the inhibition caused by Ca 2+ and Fe 2+ is a result of the interaction of these ions with the enzyme or with the pectic substrate causing gelation or precipitation of the substrate. In the other way, some ions, such as, Cu 2+ , Mn 2+ , Pb 2+ and Hg 2+ , can inhibit the PG activity (Sassi et al ; Tounsi et al ).…”

Section: Discussionmentioning

confidence: 99%

“…Polygalacturonases are classified according to their substrate specificity and the position of the bonds they hydrolyse (Ma et al ). When enzymes of the endo‐polygalacturonase type (endo‐PGs) act on PGA, they liberate oligosaccharides with a low degree of polymerization (tri‐ and tetragalacturonic acids) as the final hydrolysis product, while exo‐polygalacturonase (exo‐PG) releases mainly mono‐ and digalacturonic acid (Tounsi et al ).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

“…Recently, pectinases have gained attention due to their numerous industrial applications in fruits and vegetable processing, wine processing, saccharification of agricultural substrates, extraction of vegetable oil, processing of textile material, tea and coffee processing, processing of animal feed, biobleaching of kraft pulp, and recycling of wastepaper (AlMatar and Makky 2016; Garg et al 2016). Polygalacturonase (PG) is an important subgroup of pectinases, which are responsible for hydrolysis of a-1,4-glycosidic bonds in polygalacturonic acid in a sequential fashion and are classified under depolymerases (Demir and Tari 2016;Tounsi et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Microparticle-enhanced polygalacturonase production by wild type Aspergillus sojae

et al. 2017

View full text Add to dashboard Cite

Polygalacturonases (PGs), an important industrial enzyme group classified under depolymerases, catalyze the hydrolytic cleavage of the polygalacturonic acid chain through the introduction of water across the oxygen bridge. In order to produce and increase the concentration of this enzyme group in fermentation processes, a new approach called microparticle cultivation, a promising and remarkable method, has been used. The aim of this study was to increase the PG activity of using aluminum oxide (AlO) as microparticles in shake flask fermentation medium. Results indicated that the highest PG activity of 34.55 ± 0.5 U/ml was achieved with the addition of 20 g/L of AlO while the lowest activity of 15.20 ± 0.2 U/mL was obtained in the presence of 0.1 g/L of AlO. In fermentation without microparticles as control, the activity was 15.64 ± 3.3 U/mL. Results showed that the maximum PG activity was 2.2-fold higher than control. Additionally, smaller pellets formed with the addition of AlO where the lowest pellet diameter was 955.1 µm when 10 g/L of the microparticle was used. Also, it was noticed that biomass concentration gradually increased with increasing microparticle concentration in the fermentation media. Consequently, the PG activity was significantly increased in microparticle-enhanced shake flask fermentation. In fact, these promising preliminary data can be of significance to improve the enzyme activity in large-scale bioreactors.

show abstract

A key residue for the substrate affinity enhancement of a thermophilic endo-polygalacturonase revealed by computational design

Luo

et al. 2018

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Protein engineering has been a research hotspot to improve the catalytic efficiency of industrially important enzymes. In the present study, a novel computational strategy was developed to in silico screen mutants with enhanced binding interaction between enzyme and substrate as well as catalytic efficiency. Through homology modeling and molecular dynamics (MD) simulation, four key residues related to substrate binding were identified in the endo-polygalacturonase BiPG28A from Bispora sp. MEY-1. Further analyses of the conformation, hydrogen bond interactions, and binding free energy revealed that lysine at position 129 (subsite - 2) has the strongest affinity to substrate. Biochemical and calorimetry experiments confirmed the functional role of Lys129 in substrate binding through non-covalent interactions. The common role of Lys129 was also verified in another GH28 endo-polygalacturonase. Distinguished from other protein engineering strategies involving structure resolution and construction of certain enzymes, this computational strategy represents an insightful and efficient approach to develop a "designed" enzyme with significantly enhanced binding affinity and catalytic efficiency.

show abstract

Catalytic properties of a highly thermoactive polygalacturonase from the mesophilic fungus Penicillium occitanis and use in juice clarification

Cited by 24 publications

References 40 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

Microparticle-enhanced polygalacturonase production by wild type Aspergillus sojae

A key residue for the substrate affinity enhancement of a thermophilic endo-polygalacturonase revealed by computational design

Contact Info

Product

Resources

About