Summary
A purification procedure for an extracellular α-amylase from Streptomyces rimosus, oxytetracycline-producing strain, is described. The enzyme obtained was shown to be an acidic (pI 4.75) monomer with a relative molecular mass (Mr) of 43 000, containing three cysteines involved in the catalytic activity of the enzyme. Its amino-terminal part has 57–67% homology with amylases from other Streptomyces species. S. rimosus α-amylase is sensitive to higher temperatures, and partially stabilized by Ca2+ ions. It hydrolyses starch (optimum at pH 5.0–6.0) in an endohydrolase manner giving rise to maltotriose, maltotetraose and higher oligosaccharides. Starch granules, except those from rice, were not significantly affected by the isolated α-amylase.
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References
Babitskaya VG (1970) Amylase from Actinomyces aureofaciens and its properties. In: Samsevich SA (ed) Fiziologya i biokhimya mikroorganizmov. Nauka i tehnika, Minsk, USSR, pp 91–95
Choi SH, Kim CJ, Oh MJ, Lee JS (1989) Characteristics of raw starch-digesting enzyme from Streptomyces sp. 4M-2. CA 111 (1989) 92662d
El-Sayed MA, El-Raheem A, El-Shaushoury R, El-Hawar MA, Aly MF (1987) Biosynthesis of amylase by Streptomyces lipmanii. Delta J Sci 11:1153–1167
Fairbairn DA, Priest FG, Stark JR (1986) Extracellular amylase synthesis by Streptomyces limosus. Enzyme Microb Technol 8:89–92
Goldberg JD, Edwards C (1990) Purification and characterization of an extracellular amylase from a thermophilic streptomycete. J Appl Bacteriol 69:712–717
Henschen A (1986) Analysis of cyst(e)ine residues, disulfide bridges, and sulfhydryl groups in proteins. In: Wittmann-Liebold et al. (eds) Advanced Methods in Protein Microsequence Analysis. Springer, Berlin Heidelberg New York, pp 244–255
Hidaka H, Koaze Y, Yoshida K, Niwa T, Shomura T, Niida T (1974) Isolation and some properties of amylase from Streptomyces hygroscopicus SF-1084. Starch 26:413–416
Hoshiko S, Makabe O, Nojiri C, Katsumata K, Satoh E, Nagaoka K (1987) Molecular cloning and characterization of the Streptomyces hygroscopicus α-amylase gene. J Bacteriol 169:1029–1036
Hostinová E, Zelinka J (1978) Alpha-amylase from Streptomyces aureofaciens — purification and properties. Starch 30:338–341
Hunkapiller MW, Hood LE (1983) Analysis of phenylthiohydantoins by ultrasensitive gradient high-performance liquid chromatography. Methods Enzymol 91:486–493
Hyvarinen A, Nikkila BA (1962) Specific determination of blood glucose with o-toluidine. Clin Chim Acta 7:140–143
Kindle KL (1983) Characteristics and production of thermostable α-amylase. Appl Biochem Biotechnol 8:153–170
Levitzki A, Steer ML (1974) The allosteric activation of mammalian α-amylase by chloride. Eur J Biochem 41:171–180
Long CM, Virolle M-J, Chang S-Y, Chang S, Bibb MJ (1987) α-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate α-amylases. J Bacteriol 169:5745–5754
Moseley MH, Keay L (1970) Purification and characterization of the amylase of B. subtilis NRRL B3411. Biotechnol Bioeng 12:251–271
Pasero L, Mazzei-Pierron Y, Abadie B, Chicheportiche Y, Marchis-Mouren G (1986) Complete amino acid sequence and location of the five disulfide bridges in porcine pancreas α-amylase. Biochim Biophys Acta 869:147–157
Pokorny M, Vitale Lj, Turk V, Renko M, Žuvanić J (1979) Streptomyces rimosus extracellular proteases. 1. Characterization and evaluation of various crude preparations. Eur J Appl Microbiol Biotechnol 8:81–90
Rick W, Stegbauer HP (1974) α-Amylase. Messungen der reduzierenden Gruppen. In: Bergmeyer HU (ed) Methoden enzymatischen Analyse, vol 3. Verlag Chemie, Weinheim, pp 918–923
Simpson RJ, Neuberger MR, Liu TY (1976) Complete amino acid analysis of proteins from a single hydrolyzate. J Biol Chem 251:1936–1940
Suganuma T, Mizukami T, Moori K, Ohnishi M, Hiromi K (1980) Studies of the action pattern of an α-amylase from Streptomyces praecox NA-273. J Biochem 88:131–138
Takagi T, Toda H, Isemura T (1971) Bacterial and mold amylases. Enzymes 5:235–271
Takaya T, Sugimoto Y, Wako K, Fuwa H (1979) Degradation of starch granules by alpha-amylase of Streptomyces praecox NA-273. Starch 31:205–208
Vigal T, Gil JA, Daza A, Garcia-Gonzales MD, Martin JF (1991) Cloning, characterization and expression of an α-amylase gene from Streptomyces griseus IMRU3570. Mol Gen Genet 225:278–288
Virolle M-J, Long CM, Chang S, Bibb MJ (1988) Cloning, characterization and regulation of an α-amylase gene from Streptomyces venezuelae. Gene 74:321–334
Vitale Lj, Turk V, Pokorny M, Vukelić B, Renko M (1980) Hydrolytic enzymes complex from Streptomyces rimosus. Period biol 82:485–490
Weill EE, Hanke P (1962) Thin-layer chromatography of maltooligosaccharides. Anal Chem 34:1736–1737
Williams ST, Goodfellow M, Alderson G, Wellington EMH, Sneath PHA, Sackin MJ (1983) Numerical classification of Streptomyces and related genera. J Gen Microbiol 129:1743–1813
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Vukelić, B., Ritonja, A., Renko, M. et al. Extracellular α-amylase from Streptomyces rimosus . Appl Microbiol Biotechnol 37, 202–204 (1992). https://doi.org/10.1007/BF00178171
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DOI: https://doi.org/10.1007/BF00178171