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Purification and characterization of an extracellular amylase from a thermophilic streptomycete
Author(s) -
Goldberg J.D.,
Edwards C.
Publication year - 1990
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1990.tb01568.x
Subject(s) - thermostability , thermophile , maltose , divalent , amylase , enzyme , starch , biochemistry , alpha amylase , extracellular , chemistry , streptomyces , enzyme assay , biology , bacteria , organic chemistry , genetics
G oldberg , J.D. & E dwards , C. 1990. Purification and characterization of an extracellular amylase from a thermophilic streptomycete. Journal of Applied Bacteriology 69 , 712–717. A single extracellular alpha‐amylase (1,4‐α‐D‐glucan glucanohydrolase, EC 3.2.1.1) from Streptomyces thermoviolaceus subsp. apingens was purified to homogeneity by a starch adsorption method. SDS‐PAGE indicated that the enzyme had an apparent M, of 57 kDa and activity was optimal at a pH of 7–2 and a temperature of 55d̀C. It employed an endo‐active mechanism to liberate predominantly maltose, as well as smaller amounts of higher oligosaccharides when incubated with starch. EDTA inhibited enzyme activity, suggesting an involvement of a divalent cation in activity. The enzyme was also stabilized by divalent cations when heated and the results suggested a major role for Ca 2+ ions for both activity and thermostability. The alpha‐amylase from S. thermoviolaceus displayed some similarities with commercially‐used streptomycete alpha‐amylases.