Abstract
An extracellular α-amylase produced by a cassava-fermenting strain ofMicrococcus luteus was purified 26-fold by gel filtration and ion-exchange chromatography. The molar mass was estimated to be approximately 56 kDa. The optimum temperature of the enzyme was 30°C, optimum pH 6.0 and optimum substrate concentration was 0.6% (W/V). Treatment of the enzyme at 70°C for 10 min resulted in 70% loss of activity. The activation energy was determined to be 34.8 kJ/mol. The activity of the enzyme was enhanced by Mg2+, Ca2+, K+, Na+ and inhibited by EDTA, KCN and citric acid. The enzyme may find some application in local food processing.
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References
Adeleye A.I.: Production and control of extracellular α-amylase inMicrococcus varians.J. Basic Microbiol. 30, 723–727 (1990a).
Adeleye A.I.: Purification and properties of α-amylase fromMicrococcus varians.J. Basic Microbiol. 30, 717–722 (1990b).
Ali S., Hossain Z.: Characteristics of glucoamylase fromAspergillus terreus.J. Appl. Bacteriol. 71, 144–146 (1991).
Amund O.O., Ogunsina O.A.: Extracellular amylase production by cassava fermenting bacteria.J. Industr. Microbiol. 2, 123–127 (1987).
Andrews P.: Estimation of the molecular weights of proteins by Sephadex gel filtration.Biochem. J. 91, 222–233 (1964).
Buchanan R.E., Gibbons N.E.:Bergey's Manual of Determinative Bacteriology. Williams & Wilkins, Baltimore 1974.
Champ M., Szylit P., Raibaud P., Ait-Abdelkader N.: Amylase production by threeLactobacillus strains isolated from chicken crop.J. Appl. Bacteriol. 55, 487–493 (1983).
Chandra A.K., Medda S., Bhadra A.I.C.: Production of extracellular thermostable α-amylase byBacillus licheniformis.J. Ferment. Technol. 58, 1–10 (1980).
Collins C.H., Lyne P.M.:Microbiological Methods. Butterworth and Co., New York 1976.
Fisher E.H., Summerwell N.W., Junge J.M., Stein E.A.:Bacillus subtilis α-amylase properties.Proc. Internat. Congr. Biochem. 8, 124 (1960).
Ghosh H., Chatterjee B., Das A.: Purification and characterization of glucoamylase ofAspergillus terreus NA-170 mutant.J. Appl. Bacteriol. 71, 162–169 (1991).
Harborne J.B.:Phytochemical methods. Chapman and Hall Publ., London 1984.
Hasegawa A., Miwa A., Oshina T., Imahori K.: Studies on α-amylase from a thermophilic bacteria. I. Purification and characterization.J. biochem. 79, 469–477 (1976).
Hopkins R.H.: Action of the amylases.Adv. Enzymol. 6, 389–414 (1946).
Ingle M.B., Erickson R.J.: Bacterial α-amylase.Adv. Appl. Microbiol. 24, 257–278 (1978).
Morris J.G.:A Biologist's Physical Chemistry. Edward Arnold, London 1971.
Okafor N.: Microorganisms associated with cassava fermentation for gari production.J. Appl. Bacteriol. 42, 279–284 (1977).
Pfueller S.L., Elliot W.H.: Extracellular α-amylase activity in avocado fruit pulp.J. Amer. Soc. Hortic. Sci. 103, 673–675 (1969).
Sen S., Chakrabarty S.L.: Amylases fromLactobacillus cellobiosus isolated from vegetable wastes.J. Ferment. Technol. 62, 407–413 (1984).
Tsvetkov V.T., Emanuilova E.I.: Purification and properties of heat stable α-amylase fromBacillus brevis.Appl. Microbiol. Biotech. 31, 246–248 (1989).
Welker N.E., Campbell L.L.: Effect of carbon sources on formation of α-amylase byBacillus stearothermophilus.J. Bacteriol. 86, 681–686 (1978).
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Ilori, M.O., Amund, O.O. & Omidiji, O. Purification and properties of an α-amylase produced by a cassava-fermenting strain ofMicrococcus luteus . Folia Microbiol 42, 445–449 (1997). https://doi.org/10.1007/BF02826551
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DOI: https://doi.org/10.1007/BF02826551