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

Sena, Amanda Reges de; Valasques, Gildomar Lima; Góes-Neto, Aristóteles; Taranto, Alex Gutterres; Pirovani, Carlos Priminho; Cascardo, Júlio Cézar M.; Zingali, Russolina B.; Bezerra, Marcos Almeida; Assis, Sandra Aparecida de

doi:10.1590/s0001-37652011005000007

Cited by 20 publications

(15 citation statements)

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“…Similar results were reported for the laminarinase produced by P. oxalicum (pH 4.0) (Copa-Patiño et al 1989), whereas the laminarinase from P. italicum had an optimum pH of 6.0 (Sánchez et al 1982). Laminarinases with an optimum of pH 5.0 are produced by a wide variety of organisms (Bara et al 2003;Chipoulet and Chararas 1984;Kulminskaya et al 2001;Sena et al 2011). Fig.…”

Section: Resultssupporting

confidence: 83%

Purification and Characterization of a Thermostable Laminarinase from Penicillium rolfsii c3-2(1) IBRL

Lee¹,

Arai²,

Demirtaş³

et al. 2014

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A laminarinase (endo-β-1,3-glucanase) was purified to homogeneity from Penicillium rolfsii c3-2(1) IBRL, which was originally produced in liquid culture containing 1% xylan from birchwood, via anion-exchange chromatography, gel filtration on Sephacryl S-100, and hydrophobic interaction chromatography. A single protein band with a molecular weight of 75 kDa was detected by sodium dodecyl sulfatepolyacrylamide gel electrophoresis, which had an optimum catalytic activity at pH 4.0 to 5.0 and 70 °C. This purified enzyme was most stable in the pH range 4 to 7, while it was thermostable up to 55 °C and retained up to 90% of its activity after 4 h pre-incubation. A substrate laminarin kinetic study yielded estimated K m and V max values of 0.0817 mg/mL and 372.2 µmol/min/mg, respectively. Laminari-oligosaccharide degradation, which was analyzed by thin layer chromatography, yielded the major hydrolysis products laminaribiose and glucose.

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Section: Resultssupporting

confidence: 83%

Purification and Characterization of a Thermostable Laminarinase from Penicillium rolfsii c3-2(1) IBRL

Lee¹,

Arai²,

Demirtaş³

et al. 2014

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“…Purification of glucanase and chitinase from M. perniciosa was performed according to previous studies by the authors (SENA et al, 2011, GALANTE et al, 2012. On the other hand, in this study, an experimental design was used to evaluate the influence of independent variables on lysis of Pseudozyma sp.…”

Section: Resultsmentioning

confidence: 99%

“…Incubation was carried out at 28 °C for 14 days, as described in Sena et al (2011). The liquid culture medium, on which M. perniciosa was grown, was filtered and centrifuged (Centrifuge 5804R -Eppendorf, São Paulo, Brazil) at 8.000 g for 15 minutes at 4 °C, and the supernatant containing the secretes proteins from M. perniciosa was used as a crude enzymatic extract (HUA et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Application of Doehlert experimental design in the optimization of experimental variables for the Pseudozyma sp. (CCMB 306) and Pseudozyma sp. (CCMB 300) cell lysis

et al. 2012

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Application of Doehlert experimental design in the optimization of experimental variables for the Pseudozyma sp. (CCMB 306) and Pseudozyma sp. (CCMB 300) cell lysis Aplicação do modelo Doehlert na otimização das variáveis experimentais para a lise de Pseudozyma sp. (CCMB 306) e Pseudozyma sp. (CCMB 300)Amanda Reges de SENA 1,3 , Gildomar Lima VALASQUES JÚNIOR 1,2 , Ingara Keisle São Paulo BARRETTO 1 , Sandra Aparecida ASSIS 1 * IntroductionThe cell wall of yeast is basically made of glucan and mannan-protein. Lytic enzymes such as chitinases, proteases and β-1,3-glucanases are usually necessary. There are numerous applications for biotechnologies: preparation of protoplasts, extraction of pigments, mass treatment of residual yeast cell fermentation industries for preparation of animal feed, in studies of the mechanism of cell wall synthesis for control of pathogenic yeast, etc. (HUNTER;ASENJO, 1988;SATO, 2005;SALAZAR; ASENJO, 2007).These enzymes are capable of lysing the cell wall of Saccharomyces cereviseae, Candida sp. and other genera of yeasts, which extends their use allowing the selective manufacture of products, regardless of scale, and can be performed under temperature and pH conditions that do not involve the denaturation of cellular products of interest (FLEURI; SATO, 2005). Mathematical models have been increasingly used to help explain responses of biochemical reactions. This technique is often used for optimization and/or verification of the influence of medium components and cultivation parameters for enzyme production (FLEURI; SATO, 2008).The production and optimization of the parameters that affect the enzymatic synthesis should always be investigated because the optimal conditions vary among different organisms and different enzymes (BRAVO et al., 2000). In many cases, the interaction of parameters that influence fermentation processes can be evaluated with a reduced number of tests using an experimental design (THÉODORE; PANDA, 1995). Several experimental design models could be used to reduce the number of experiments under different conditions. Among them are the Plackett-Burman, Doehlert, Central Composite, and Box-Behnken (LI et al., 2007).The choice of Doehlert design is justified by a number of advantages such as (1) its spherical experimental domain with an uniformity in space filling, (2) its ability to explore the whole of the domain, and (3) its potential for sequentially where the experiments can be reused when the boundaries have not been well chosen at first (BENSALAH et al., 2010). Doehlert designs are easily applied to optimized variables and offer advantages over the Central Composite (CCD) and Box-Behnken designs, used in response surface analysis. They need fewer experiments, ResumoO presente trabalho visou verificar a influência do pH e temperatura na lise de leveduras utilizando planejamento experimental. No estudo, foi utilizado o extrato enzimático, contendo β-1,3-glucanase e quitinase líticas, obtidas do micro-organismo Moniliophthora perniciosa. O delineamento experiment...

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“…The high price of chitinases and β‐1,3 glucanase is associated with low production, even when using recombinant microorganisms 13 . The several purification steps also contribute in increasing the sell price of such enzymes 14 …”

Section: Introductionmentioning

confidence: 99%

Ultrasound‐assisted fermentation for production of β‐1,3‐glucanase and chitinase by Beauveria bassiana

Schmaltz

Aita

Alves

et al. 2020

J of Chemical Tech & Biotech

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BACKGROUND: Ultrasound (US) treatment was applied to increase the production of ⊎-1,3-glucanase and chitinase by Beauveria bassiana (IBCB 66) cultivated in submerged fermentation. Application of US at different growth stages, US power outputs, time of ultrasonication, and duty cycles were the parameters evaluated. RESULTS: The best strategy comprised ultrasonication during 5 min at 24 h of fermentation with a power output of 195 W (fixed frequency of 24 kHz) and a duty cycle of 0.5 s.s −1 (0.5 s ON, 0.5 s OFF). The US treatment resulted in a production increase of 46% for ⊎-1,3-glucanase and 42% for chitinase compared to the non-sonicated control. Fragmentations of the mycelia in the sonicated samples were observed in Scanning Electron Microscopy (SEM) micrographs after the US application, supporting the idea of a better release of enzymes to outside the cell. CONCLUSION: Ultrasound-assisted fermentation was a promising tool to increase the production of ⊎-1,3-glucanase and chitinase by Beauveria bassiana (IBCB 66). The combination of US parameters showed to be decisive in obtaining higher enzyme production when compared to the control non-sonicated experiment. Therefore, this work brings a significant contribution to the field of stimulation of bioprocesses with ultrasound since it shows a strategy to obtain higher enzyme production when compared to traditional fermentation.

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

Cited by 20 publications

References 27 publications

Purification and Characterization of a Thermostable Laminarinase from Penicillium rolfsii c3-2(1) IBRL

Purification and Characterization of a Thermostable Laminarinase from Penicillium rolfsii c3-2(1) IBRL

Application of Doehlert experimental design in the optimization of experimental variables for the Pseudozyma sp. (CCMB 306) and Pseudozyma sp. (CCMB 300) cell lysis

Ultrasound‐assisted fermentation for production of β‐1,3‐glucanase and chitinase by Beauveria bassiana

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