Purification and Characterization of a Polyextremophilic <i>α</i>-Amylase from an Obligate Halophilic <i>Aspergillus penicillioides</i> Isolate and Its Potential for Souse with Detergents

<div>SDS-PAGE analysis of the enriched <i>α</i>-amylase from<i> A. penicillioides</i> TISTR 3639. Lane 1: molecular mass ladder; lane 2 the enriched <i>α</i>-amylase, showing a single band at approximately 42 kDa.</div>

BioMed Research International

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Figure 1

Figure 1: Purification and Characterization of a Polyextremophilic <i>α</i>-Amylase from an Obligate Halophilic <i>Aspergillus penicillioides</i> Isolate and Its Potential for Souse with Detergents 

Figure 1 | Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents 