Abstract
An Antarctic bacterial isolate was found to show extracellular a-amylolytic activity. Based on 16S rRNA sequence analysis, the strain was named Flavobacterium sp. PCK1. The optimal activity of the amylase occurred at 30°C and pH 6.0. The enzyme was highly specific for soluble starch with no activity on other polysaccharides tested, and it exhibited endoamylolytic activity on chromogenic substrates such as amylose-azure, amylopectin-azure and non-reducing end blocked p-nitrophenyl maltoheptaoside (BPNPG7). The enzyme activity was significantly stimulated by Ca2+ and strongly inhibited by Ni2+, Zn2+, Cu2+ or ethylenediaminetetraacetic acid (EDTA). The enzyme may offer potential for use as a cold-adaptive biocatalyst in biotechnological applications. Key words: Antarctic, Flavobacterium sp., amylase, endoamylolytic, biocatalyst.
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