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The molecular weights of most of the ?-amylases produced by fungi were between
45-65 kDa Han et al. reported the molecular weight of monomeric McAmyA that was
found to be 60.3 and 57.5 kDa by SDS-PAGE and gel filtration, respectively, which
contradicts the present findings. To describe the properties of a complex
protein of the macromolecule type, it is essential to elucidate the structural
levels of organization of the protein according to the complexity of its
molecule. Very often, the unfolded straight polypeptide chain reaches a helical
configuration to create the secondary structure. In addition, the percentage of
occurrence of ?
helix, parallel ?
sheets, ?
turns and random spirals determines the stability and properties of the protein.
Circular dichroism spectroscopy is an important method to evaluate the general
secondary structure and observe protein folding. The characteristics of the CD
spectra indicate that the purified ?-amylase possesses high ? sheet and ? back contents and the purification steps
produced a native secondary structure of ?-amylase. The composition of the secondary
structure of glucoamylase was also studied from Aspergillus niveus by da Silva
et al. that was on par with the crystal structures of the glucoamylases of
other Aspergillus species.

The maximum yield of the product, the
productivity of the process and the rate of utilization of the substrate end
the economy of the fermentation. In view of this, the fermentation kinetics
plays a significant role in the identification of key cost breakpoints.
Therefore, in this study, the parameters of the basic fermentation kinetics
were evaluated to develop a triumphant process that will be reasonably viable.
In comparison with the present study, Iftikhar et al. They reported a similar
type of observation. for the production of lipase from Rhizopus oligosporus
var. microsporus.

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Conclu ..

This study reports the efficient exploitation
of agroindustrial waste for the production of ?-amylase by both static liquid surface and solid
state fermentations that are generated in abundance in developing countries
such as India. These economic substrates such as pearl millet (PM) can serve as
a source of carbon, nitrogen and other metabolites essential for the growth and
maintenance of fungi and, finally, can produce biotechnologically relevant
enzymes. In this study, different process parameters for the production of ?-amylase were optimized using PM as
substrate. The amylase production was improved up to 60 times at 30 ° C for 96
h with the supplementation of vitamin E (30 mg / 100 ml) to the PM fermentation
medium. In addition, the spectroscopic analysis of circular dichroism confirmed
the secondary structure of amylase. The secondary structure of amylase is rich
in random coils (36.8%) that contribute to the stability of secondary
structures of amylase. Therefore, such a singularity in stability would be one
of the most preferred characteristics of this amylase for suitable industrial
operations. However, such optimization of the fermentation parameters would not
only develop an ecological protocol to rationalize the total cost of
production, but would also help in the effective management of agroindustrial
waste. Therefore, this study represents a cost-effective maneuver, with simpler
techniques for modifying cultural parameters for better production and recovery
of ?-amylase.

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