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Production and Characterization of Lipases by Two New Isolates of Aspergillus through Solid-State and Submerged Fermentation.

Colla LM, Ficanha AM, Rizzardi J, Bertolin TE, Reinehr CO, Costa JA - Biomed Res Int (2015)

Bottom Line: Lipases obtained through submerged fermentation presented optimal activities at 37 °C and pH 7.2 and those obtained through solid-state fermentation at 35 °C and pH 6.0.The enzymes produced by submerged fermentation were more temperature-stable than those obtained by solid-state fermentation, presenting 72% of residual activity after one hour of exposition at 90 °C.Lipases obtained through submerged fermentation had 80% of stability in acidic pH and those obtained through solid-state fermentation had stability greater than 60% in alkaline pH.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Fermentations, Food Engineering Course, University of Passo Fundo, Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, RS, Brazil.

ABSTRACT
Due to the numerous applications of lipases in industry, there is a need to study their characteristics, because lipases obtained from different sources may present different properties. The aim of this work was to accomplish the partial characterization of lipases obtained through submerged fermentation and solid-state fermentation by two species of Aspergillus. Fungal strains were isolated from a diesel-contaminated soil and selected as good lipases producers. Lipases obtained through submerged fermentation presented optimal activities at 37 °C and pH 7.2 and those obtained through solid-state fermentation at 35 °C and pH 6.0. The enzymes produced by submerged fermentation were more temperature-stable than those obtained by solid-state fermentation, presenting 72% of residual activity after one hour of exposition at 90 °C. Lipases obtained through submerged fermentation had 80% of stability in acidic pH and those obtained through solid-state fermentation had stability greater than 60% in alkaline pH.

No MeSH data available.


Related in: MedlinePlus

Kinetics of thermal destruction of the enzymatic extracts produced by Aspergillus niger in solid-state fermentation: (a) at temperatures of 35°C to 90°C. AR: enzyme residual activity, (b) linear regression of the thermal deactivation constants obtained at 35°C to 90°C (ln of data) as function of inverse of absolute temperature for calculating the energy of thermal deactivation of the enzyme.
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fig3: Kinetics of thermal destruction of the enzymatic extracts produced by Aspergillus niger in solid-state fermentation: (a) at temperatures of 35°C to 90°C. AR: enzyme residual activity, (b) linear regression of the thermal deactivation constants obtained at 35°C to 90°C (ln of data) as function of inverse of absolute temperature for calculating the energy of thermal deactivation of the enzyme.

Mentions: Figure 3(a) shows the thermal destruction kinetics of the enzyme produced through solid-state fermentation between 35°C and 90°C, which follows the pattern of first-order thermal destruction predicted by the Arrhenius model. Table 3 shows the thermal deactivation constants between 35°C and 90°C, obtained from angular coefficients of the curves shown in Figure 3, as well as the determination coefficients of regression and the half-life of enzymes at each temperature. The enzyme had higher thermal stability at 35°C and 40°C, which can be observed from the high half-lives (t1/2), around 6 and 4.3 h, respectively. Above 50°C, the half-life considerably decreased to 29 min between 60°C and 70°C. Figure 3(b) shows the graph of ln (kd) as a function of absolute temperature (K), used to calculate the energy of thermal deactivation, which was 60.33 kJ/mol for the studied enzyme.


Production and Characterization of Lipases by Two New Isolates of Aspergillus through Solid-State and Submerged Fermentation.

Colla LM, Ficanha AM, Rizzardi J, Bertolin TE, Reinehr CO, Costa JA - Biomed Res Int (2015)

Kinetics of thermal destruction of the enzymatic extracts produced by Aspergillus niger in solid-state fermentation: (a) at temperatures of 35°C to 90°C. AR: enzyme residual activity, (b) linear regression of the thermal deactivation constants obtained at 35°C to 90°C (ln of data) as function of inverse of absolute temperature for calculating the energy of thermal deactivation of the enzyme.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4477096&req=5

fig3: Kinetics of thermal destruction of the enzymatic extracts produced by Aspergillus niger in solid-state fermentation: (a) at temperatures of 35°C to 90°C. AR: enzyme residual activity, (b) linear regression of the thermal deactivation constants obtained at 35°C to 90°C (ln of data) as function of inverse of absolute temperature for calculating the energy of thermal deactivation of the enzyme.
Mentions: Figure 3(a) shows the thermal destruction kinetics of the enzyme produced through solid-state fermentation between 35°C and 90°C, which follows the pattern of first-order thermal destruction predicted by the Arrhenius model. Table 3 shows the thermal deactivation constants between 35°C and 90°C, obtained from angular coefficients of the curves shown in Figure 3, as well as the determination coefficients of regression and the half-life of enzymes at each temperature. The enzyme had higher thermal stability at 35°C and 40°C, which can be observed from the high half-lives (t1/2), around 6 and 4.3 h, respectively. Above 50°C, the half-life considerably decreased to 29 min between 60°C and 70°C. Figure 3(b) shows the graph of ln (kd) as a function of absolute temperature (K), used to calculate the energy of thermal deactivation, which was 60.33 kJ/mol for the studied enzyme.

Bottom Line: Lipases obtained through submerged fermentation presented optimal activities at 37 °C and pH 7.2 and those obtained through solid-state fermentation at 35 °C and pH 6.0.The enzymes produced by submerged fermentation were more temperature-stable than those obtained by solid-state fermentation, presenting 72% of residual activity after one hour of exposition at 90 °C.Lipases obtained through submerged fermentation had 80% of stability in acidic pH and those obtained through solid-state fermentation had stability greater than 60% in alkaline pH.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Fermentations, Food Engineering Course, University of Passo Fundo, Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, RS, Brazil.

ABSTRACT
Due to the numerous applications of lipases in industry, there is a need to study their characteristics, because lipases obtained from different sources may present different properties. The aim of this work was to accomplish the partial characterization of lipases obtained through submerged fermentation and solid-state fermentation by two species of Aspergillus. Fungal strains were isolated from a diesel-contaminated soil and selected as good lipases producers. Lipases obtained through submerged fermentation presented optimal activities at 37 °C and pH 7.2 and those obtained through solid-state fermentation at 35 °C and pH 6.0. The enzymes produced by submerged fermentation were more temperature-stable than those obtained by solid-state fermentation, presenting 72% of residual activity after one hour of exposition at 90 °C. Lipases obtained through submerged fermentation had 80% of stability in acidic pH and those obtained through solid-state fermentation had stability greater than 60% in alkaline pH.

No MeSH data available.


Related in: MedlinePlus