Abstract
Amylases are among the most important enzymes with potential applications in the present-day industry. Thus, isolating pure culture from cassava as the cheap source has manifold importance for food industries. In the present study, eleven amylase producing fungal strains were isolated from cassava flour and growth pattern, as well as optimum growth condition, was determined. All isolates showed amylases activity but isolate BR005, BR001 and GR003 recorded maximum clear zone diameters of 54.75 ± 0.957 mm, 53.25 ±0.645 mm 51.5 ± 1.414 mm, respectively. The submerged fermentation method was employed for crude amylase and biomass production. There were significant differences (p˂0.05) in starch concentrations and growth rates between the three isolates. GR003 and BR005 attained their optimal amylase activities of 4.23±0.25 U/mL and 3.75±3.16 U/mL at 50 °C, respectively, whiles BR001 attained its optimum amylase activity of 3.43±0.77 at 60 °C. Whereas, BR005, BR001 and GR003 attained their optimal amylase activity of 5.14±1.99 U/mL, 4.53±0.01 U/mL and 1.25±1.11 U/mL at a pH range of 6 to 7, making them neutrophilic fungi. Moreover, isolates BR005, BR001 and GR003 recorded the highest amylase activities of 4.31±0.14U/mL, 4.67±1.16±U/mL and 3.16±0.12U/mL at the starch concentrations of 3%, 2%, and 2.5% and fermentation period of 48 h, 66 h and 42 h, respectively. Lastly, BR005, BR001 and GR003 achieved their optimal amylase activities of 5.41±0.11U/mL, 6.24±0.14 U/mL and 6.22±0.12 U/mL at 48 h, 66 h and 42 h of incubation, accordingly. Indicating that cassava flour is a good source of amylolytic fungi with a potential application under wide conditions.
Highlights
MATERIALS AND METHODSAmylases are a family of enzymes that degrade starch into simple sugars and lower molecular weight polysaccharides
Amylases are classified into three types namely α-amylase, ß-amylase, and γ.amylase based on their catalytic mechanisms (Akpan et al, 1999). α -Amylase (EC 3.2.1.1), catalysis the hydrolysis of internal α -1,4-glycosidic linkages in starch into low molecular weight products, such as glucose, maltose units. ßamylase (EC 3.2.1.2,) catalysis the hydrolysis of α -1,4-glycosidic linkage of starch and ß-anomeric maltose from the non-reducing ends (David et al, 2000). γ -Amylase (EC 3.2.1.3), hydrolysis α -1,6 glycosidic linkages, in addition to t he last α -1,4 glycosidic linkages at the non-reducing end of amylose and amylopectin, yielding glucose
Amylases from microbes are much preferred because microbes are much easier to manipulate to facilitate enzyme production with desire characteristics (Souza 2010; Sundarram and Murphy, 2014)
Summary
MATERIALS AND METHODSAmylases are a family of enzymes that degrade starch into simple sugars and lower molecular weight polysaccharides. Isolates BR005, BR001 and GR003 recorded the highest amylase activities of 4.31±0.14U/mL, 4.67±1.16±U/mL and 3.16±0.12U/mL at the starch concentrations of 3%, 2%, and 2.5% and fermentation period of 48 h, 66 h and 42 h, respectively. This study reports the isolation and optimization of novel amylase producing fungi from cassava flour.
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