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. 1994 Jun;176(12):3584–3588. doi: 10.1128/jb.176.12.3584-3588.1994

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

J Abe 1, N Onitsuka 1, T Nakano 1, Y Shibata 1, S Hizukuri 1, E Entani 1
PMCID: PMC205547  PMID: 8206836

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.

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Selected References

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