Enantioselective Resolution of γ-Lactam by a Novel Thermostable Type II (+)-γ-Lactamase from the Hyperthermophilic Archaeon Aeropyrum pernix.A thermostable formamidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix was revealed a novel type II (+)-γ-lactamase.  This type II (+)-γ-lactamase is only composed of 377 amino acid residues, in contrast to another thermostable (+)-γ-lactamase from Sulfolobus solfataricus with 504 amino acid residues (type I).  The gene of this thermostable (+)-γ-lactamase was cloned, functionally expressed in Escherichia coli BL21, and purified by a simple yet effective heat treatment method.  It showed incredible thermostability, retaining 100% of its activity after 12 h at 100 °C.  This thermo- and alkaline-tolerant (+)-γ-lactamase presents promising properties for the industrial application. 
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