Purification and characterization of periplasmic alpha-amylase from Xanthomonas campestris K-11151.
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.
Abe
J
J
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Japan.
Onitsuka
N
N
Nakano
T
T
Shibata
Y
Y
Hizukuri
S
S
Entani
E
E
D000687:Amylopectin / Q000378:metabolism; D000688:Amylose / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology*; D003505:Cyclodextrins / Q000378:metabolism; D005936:Glucans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism; D012988:Soil Microbiology; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D016959:Xanthomonas campestris / Q000201:enzymology* / Q000302:isolation & purification; D000516:alpha-Amylases / Q000302:isolation & purification / Q000378:metabolism*
D003505:Cyclodextrins; D005936:Glucans; D009844:Oligosaccharides; C021705:maltooligosaccharides; C009109:pullulan; D000688:Amylose; D000687:Amylopectin; D006026:Glycoside Hydrolases; D000516:alpha-Amylases; C058484:neopullulanase; C048745:cyclomaltodextrinase