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J Bacteriol. 1994 June; 176(12): 3584-3588

research-article

Purification and characterization of periplasmic alpha-amylase from Xanthomonas campestris K-11151.

Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Japan.

ABSTRACT

Xanthomonas campestris K-11151, isolated from soil, produced a periplasmic alpha-amylase of a new type. The enzyme was purified to homogeneity, as shown by several criteria. The purified enzyme showed almost the same activities on alpha-, beta-, and gamma-cyclodextrins, soluble starch, and amylose. Moreover, it was active on branched cyclodextrins, pullulan, and maltose but not on glycogen. Kinetic analysis showed that alpha-cyclodextrin was the best substrate among the cyclodextrins. The substrate specificity suggested that this enzyme had the combined activities of alpha-amylase, cyclodextrinase, and neopullulanase.