Purification and characterization of a beta-Glucanase produced by Trichoderma harzianum showing biocontrol potential

Marco, Janice Lisboa De; Félix, Carlos Roberto

doi:10.1590/s1516-89132007000100003

Cited by 43 publications

(24 citation statements)

References 24 publications

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“…Similar values have been reported, but the optimum temperature of M. perniciosa was lower when compared to most others (Nagata et al 1990, Fontaine et al 1997, Bara et al 2003, Marco and Felix 2007, and higher in relation to T. harzianum (Théodore and Panda 1995). Murray et al (2001) have also pointed out that the thermal stability of the T. emersonii enzyme is noteworthy because the estimated t 1/2 values at 70 • C and 80 • C were 136 min and 25 min, respectively, while 15% of the original activity remained after 15 min at 100 • C in the absence of substrate.…”

Section: Discussionsupporting

confidence: 83%

“…Notario et al (1976) found that the β-1,3-glucanases are acidic proteins, and our results agree with theirs. Similar values of pH have been reported for β-1,3-glucanases from other fungi, including Trichoderma harzianum (Marco and Felix 2007) and Trichoderma asperellum (Bara et al 2003).…”

Section: Discussionsupporting

confidence: 77%

“…The β-1,3-glucanase of Agaricus brasiliensis was stable up to 50 • C and showed a half-life of 30 min when incubated at 55 • C (SHU et al 2006). Low thermal stability was found at 45, 50 and 60 • C in Trichoderma harzianum (Marco and Felix 2007), and half-life values of 55, 21.5 and 5 minutes were found for the same enzyme in Chaetomium thermophilum, when incubated at 65, 70 and 80 • C. This demonstrates the superiority of β-1,3-glucanase from M. perniciosa in comparison with the thermal stability of other fungi studied by other authors. Thus, β-1,3-glucanase could be effective at the standard temperatures typically used for industrial processes.…”

Section: Discussionsupporting

confidence: 48%

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Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Sena

Valasques

Góes-Neto

et al. 2011

An. Acad. Bras. Ciênc.

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The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology -RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L −1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33, 1.86 and 3.03, respectively. The partially purified enzymatic extract showed an optimum pH of 5.0 and an optimum temperature of 40 • C. The enzymatic activity increased in the presence of KCl at all concentrations studied. The glucanase activity was highest in the presence of 0.2 M NaCl. The enzyme showed high thermal stability, losing only 10.20% of its specific activity after 40 minutes of incubation at 90 • C. A purified enzyme with relatively good thermostability that is stable at low pH might be used in future industrial applications.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionsupporting

confidence: 77%

Section: Discussionsupporting

confidence: 48%

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Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Sena

Valasques

Góes-Neto

et al. 2011

An. Acad. Bras. Ciênc.

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“…Chitinase [E. C. 3.2.1.14] and b-1,3-glucanase [E. C. 3.2.1.39] production were estimated quantitatively using the method described by De Marco and others (2000) and De Marco and Felix (2007), respectively. The cultures were grown in Trichoderma liquid medium for obtaining the supernatant.…”

Section: Physiological and Biochemical Characterization Of Selected Amentioning

confidence: 99%

Elevation of Defense Network in Chilli Against Colletotrichum capsici by Phyllospheric Trichoderma Strain

Saxena

Raghuwanshi

Singh

2015

J Plant Growth Regul

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Biocontrol strategies have been mainly focused on proposing the use of biocontrol agents (BCAs) isolated from the rhizospheric region of the plant for protection against phytopathogens. The present study evaluates the effectiveness of phyllospheric Trichoderma isolates in elevating the defense responses in chilli against Colletotrichum capsici infection and comparing its efficiency to the conventionally recommended rhizospheric Trichoderma strains. The elicitation of the defense network in the plants was analyzed using biochemical assays for important enzymes, that is, PAL, PO, PPO, TPC, SOD along with the total protein level in challenged plants over untreated and unchallenged control plants. The results recorded 2.1, 5.18, 3, 0.67, and 0.5-fold increases in TPC, PAL, PO, PPO, and total protein content in BHUF4 (phyllopsheric Trichoderma isolate)-treated plants when compared to control plants under C. capsici challenge. This was at par with the increment recorded in T16A (rhizospheric Trichoderma isolate)-treated chilli plants. The increment in growth parameters was also recorded after treatment with the isolated Trichoderma strains. Interestingly, the phyllospheric isolate (BHUF4) treatment recorded comparable growth promotion in chilli plants recording 36, 62, and 60 % increases in one of the major parameters of plant growth, that is, root length, no. of leaves, and dry weight, respectively. This study proposes the use of combined application of both rhizospheric as well as phyllospheric Trichoderma isolates for better and all around protection of plants against foliar as well as soil phytopathogens. This would be a novel approach in biological control strategy for better management of anthracnose disease of chilli.

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“…In this work, the molecular weight (MW) of related esterases was estimated applying the principles described above. Such procedure has the advantage of allowing a preliminary MW determination without any previous protein purification method, such as Bio-Gel (Sierecka, 1998), Phenyl Sepharose (Marco and Felix, 2007) or Chitosan gel column (Tang and Qian, 2007). Two esterases, EST-4 and EST-5, found in the sibling species pair Drosophila mojavensis and D. arizonae, well characterized by Zouros and Johnson (1976), were selected.…”

Section: Introductionmentioning

confidence: 99%

Molecular weight estimation of esterase isoenzymes in closely related Drosophila Species (Diptera: Drosophilidae) in non-denaturing polyacrylamide gel electrophoresis

Mateus

Cabral

Bonilla-Rodriguez

et al. 2009

Braz. arch. biol. technol.

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Purification and characterization of a beta-Glucanase produced by Trichoderma harzianum showing biocontrol potential

Abstract: ABSTRACT

Cited by 43 publications

References 24 publications

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Elevation of Defense Network in Chilli Against Colletotrichum capsici by Phyllospheric Trichoderma Strain

Molecular weight estimation of esterase isoenzymes in closely related Drosophila Species (Diptera: Drosophilidae) in non-denaturing polyacrylamide gel electrophoresis

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