×
Loading...

Characterization of alpha-Amylase Produced by the Endophytic Strain of Penicillium digitatum in Solid State Fermentation (SSF) and Submerged Fermentation (SmF) by John Doe

Book Information

TitleCharacterization of alpha-Amylase Produced by the Endophytic Strain of Penicillium digitatum in Solid State Fermentation (SSF) and Submerged Fermentation (SmF)
PPI300
LanguageEnglish
Mediatypetexts
SubjectPenicillium digitatum, α-amylase, starch, enzymes, endophytics.
Collectionijaers, folkscanomy_academic, folkscanomy, additional_collections
Uploadereditor.ijaers
Identifier28CharacterizationOfAlphaAmylaseProducedByThe
Telegram icon Share on Telegram
Download Now

Description

α-Amylases are enzymes responsible for breaking the α-1.4 bond in polysaccharides with three or more glucose units, occupying the second place in the most widely employed enzymes in industry in the world. The objective of this study was to compare the yields of α-amylase produced by the endophytic fungus, Penicillium digitatum, strain D1-FB, isolated from Baccharis dracunculifolia D.C. (Asteraceae), through the solid state fermentation (SSM) and submerged fermentation (SmF) processes, in addition to characterizing the produced enzyme. The two fermentations were conducted for 120 hours, taking samples every 24 hours to obtain the peaks of production. The enzymes were characterized according to their optimal pH and temperature for performance and stability regarding the incubation in the presence of ions, variations in pH and temperature. The maximum yield of the enzyme was observed with SSF, using rice bran as substrate after 72 hours of fermentation, with 1,625 U/mL. The α-amylase had an optimal pH at 6.5 and optimal temperature at 45°C. All the ions resulted in a decrease in the activity of α-amylase in the concentration of 5mM. The enzyme proved to be quite stable in a pH range of 6.0 to 7.5 and up to the temperature of 37°C, but it presented great drops in activity with temperatures above 45°C and in the presence of ions at the concentration of 5 mM.