In this study, the strain named A. oryzae CH93 was isolated
from soil samples. SEM scanning revealed some morphological features
of this fungal strain. A. oryzae is a filamentous fungi [42].
According to the data presenting herein, we concluded that best
conditions for the production fungal protease from A. oryzae CH93
were addition 1% w/v of glucose as carbon source and 1% w/v
of yeast extract as nitrogen source and incubation of the strain
at 28 ◦C and pH 6 for a period of 96 h. The key properties of
the A. oryzae CH93 protease were having a molecular weight of
47.5 kDa, the optimum pH and temperature of 8 and 50 ◦C, respectively.
Because of this protease was not sensitive to be inhibited by
PMSF, therefore the enzyme couldn’t belong to serine proteases.
Meanwhile, 2-mercaptoethanol (2-ME) and EDTA led to decrease
protease activity, whilst, the enzyme activity increase in the presence
of acetone and isoamyl alcohol and decreased in the presence
2-propanol, isopropanol, and DMSO. Hexane (both concentrations15% and 30%), chloroform (at 15% concentration) and toluene (at
30% concentration) have not significantly affect on protease activity.
The half-life of the protease at optimum temperature was
100 min. The best substrate was casein with the maximum velocity
(Vmax) of 0.1411 ± 0.004 g/min and Km of 2.432 ± 259 g/ml.
In conclusion, the protease isolated from A. oryzae CH93 showed
some new biochemical characteristics that have not been reported
until now from Aspergillus genus.
In this study, the strain named A. oryzae CH93 was isolatedfrom soil samples. SEM scanning revealed some morphological featuresof this fungal strain. A. oryzae is a filamentous fungi [42].According to the data presenting herein, we concluded that bestconditions for the production fungal protease from A. oryzae CH93were addition 1% w/v of glucose as carbon source and 1% w/vof yeast extract as nitrogen source and incubation of the strainat 28 ◦C and pH 6 for a period of 96 h. The key properties ofthe A. oryzae CH93 protease were having a molecular weight of47.5 kDa, the optimum pH and temperature of 8 and 50 ◦C, respectively.Because of this protease was not sensitive to be inhibited byPMSF, therefore the enzyme couldn’t belong to serine proteases.Meanwhile, 2-mercaptoethanol (2-ME) and EDTA led to decreaseprotease activity, whilst, the enzyme activity increase in the presenceof acetone and isoamyl alcohol and decreased in the presence2-propanol, isopropanol, and DMSO. Hexane (both concentrations15% and 30%), chloroform (at 15% concentration) and toluene (at30% concentration) have not significantly affect on protease activity.The half-life of the protease at optimum temperature was100 min. The best substrate was casein with the maximum velocity(Vmax) of 0.1411 ± 0.004 g/min and Km of 2.432 ± 259 g/ml.In conclusion, the protease isolated from A. oryzae CH93 showedsome new biochemical characteristics that have not been reporteduntil now from Aspergillus genus.
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