3 research outputs found
Production of thermostable β-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region
Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and β-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions.
Results: The effectiveness of LMI01 was similar to that of QM9414 in volumetric enzyme activity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of β-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the β-glucosidase activity was optimal at pH 6.0. Both CMCase and β-glucosidase had an optimum temperature at 60°C and were thermostable between 50 and 60°C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and β-glucosidases with molecular masses between 70 and 100 kDa.
Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations
Production of thermostable \u3b2-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region
Background: Cellulolytic enzymes of microbial origin have great
industrial importance because of their wide application in various
industrial sectors. Fungi are considered the most efficient producers
of these enzymes. Bioprospecting survey to identify fungal sources of
biomass-hydrolyzing enzymes from a high-diversity environment is an
important approach to discover interesting strains for bioprocess uses.
In this study, we evaluated the production of endoglucanase (CMCase)
and \u3b2-glucosidase, enzymes from the lignocellulolytic complex,
produced by a native fungus. Penicillium sp. LMI01 was isolated from
decaying plant material in the Amazon region, and its performance was
compared with that of the standard isolate Trichoderma reesei QM9414
under submerged fermentation conditions. Results: The effectiveness of
LMI01was similar to that of QM9414 in volumetric enzymeactivity (U/mL);
however, the specific enzyme activity (U/mg) of the former was higher,
corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of
\u3b2-glucosidase. The enzymes produced by LMI01 had the following
physicochemical properties: CMCase activity was optimal at pH 4.2 and
the \u3b2-glucosidase activity was optimal at pH 6.0. Both CMCase and
\u3b2-glucosidase had an optimum temperature at 60\ub0C and were
thermostable between 50 and 60\ub0C. The electrophoretic profile of
the proteins secreted by LMI01 indicated that this isolate produced at
least two enzymes with CMCase activity, with approximate molecular
masses of 50 and 35 kDa, and \u3b2-glucosidases with molecular masses
between 70 and 100 kDa. Conclusions: The effectiveness and
characteristics of these enzymes indicate that LMI01 can be an
alternative for the hydrolysis of lignocellulosic materials and should
be tested in commercial formulations
Production of thermostable β-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region
Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and β-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions.
Results: The effectiveness of LMI01 was similar to that of QM9414 in volumetric enzyme activity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of β-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the β-glucosidase activity was optimal at pH 6.0. Both CMCase and β-glucosidase had an optimum temperature at 60°C and were thermostable between 50 and 60°C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and β-glucosidases with molecular masses between 70 and 100 kDa.
Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations