Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent

<div>Expression of amy175 in E. coli BL21 (DE3). (a) Native-PAGE and SDS-PAGE analysis of the purified Amy175. Lane 1, native-PAGE of purified enzyme; Lane 2, noninduced protein extracts of E. coli; Lane 3, purified recombinant protein of Amy175; Lane 4, protein molecular mass marker; Lane 5, E. coli extracts with Amy175 expression induced. (b) MALDI-TOF-MS analysis of the purified recombinant Amy175.</div>

BioMed Research International

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Figure 4

Figure 4: Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent

Figure 4 | Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent 