- 1) Manners, D.J., Observation on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci., 44, 83-85 (1997).
- 2) Kennedy, J.F., Cabalda, V.M., and White, C.A., Enzymic starch utilization and genetic engineering. Trends Biotechnol., 6, 184-189 (1988).
- 3) Plant, A.R., Morgan, H.W., and Daniel, R.M., A highly stable pullulanase from Thermus aquaticus YT-1. Enzyme Microb. Technol., 8, 668-672 (1986).
- 4) Kim, C.-H., Nashiru, O., and Ko, J.H., Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24. FEMS Microbiol. Lett., 138, 147-152 (1996).
- 5) Sashihara, N., Nakamura, N., Nagayama, H., and Horikoshi, K., Cloning and expression of the thermostable pullulanase gene from Thermus sp. strain AMD-33 in Escherichia coli. FEMS Microbiol. Lett., 49, 385-388 (1988).
- 6) Albertson, G.D., McHale, R.H., Gibbs, M.D., and Bergquist, P.L., Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus. Biochim. Biophys. Acta, 1354, 35-39 (1997).
- 7) Katsuragi, N., Takizawa, N., and Murooka, Y., Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J. Bacteriol., 169, 2301-2306 (1987).
- 8) Yoshizaki, F., Ohshima, T, and Imahori, K., Studies on Phosphoglucomutase from an Extreme Thermophile, Flavobacterium thermophilum HB8. J. Biochem., 69, 1083-1089 (1971).
- 9) Ibuka, A., Tonozuka, T., Matuzawa, H., and Sakai, H., Conversion of neopullulanase-α-amylase from Thermoactionomyces vulgaris R-47 into an amylopullulanase-type enzyme. J. Biochem., 123, 275-282 (1998).
- 10) Somogyi, M., Notes on sugar determination. J. Biol. Chem., 195, 19-23 (1952).
- 11) Ochman, H., Medhora, M.M., Garza, D., and Hartl, D.L., Amplification of franking sequences by inverse PCR, in “PCR Protocols: A guide to methods and application”, Eds. Innis, M.A., Gelfand, D.H., Sninsky, J.J., and White, T.J., Academic press, Inc. San Diego, pp. 219-227 (1990).
- 12) Nakamura, N., and Sashihara, N., Pullulanase of Thermus sp. AMD-33, in “Superbugs: Microorganisms in extreme environment”, Horikoshi, K. and Grant, W.D. eds., Springer-Verlag, Berlin and New York, pp 99-110 (1991).
- 13) Kuriki, T., Park, J.-H., and Imanaka, T., Characteristics of thermostable pullulanase from Bacillus stearothermophilus and the nucleotide sequence of the gene. J. Ferment. Bioeng., 69, 204-210 (1990).
- 14) Liong, E.C., and Ferenci, T., Molecular cloning of a maltose transport gene from Bacillus stearothermophilus and its expression in Escherichia coli K-12. Mol. Gen. Genet. 243, 343-352 (1994).
- 15) Kunst, F. et al, The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature, 390, 249-256 (1997).
- 16) Decker, K., Peist, R., Reidl, J., Kossmann, M., Brand, B., and Boos, W., Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system. J. Bacteriol., 175, 5655-5665 (1993)
- 17) Russell, R.R.B., Aduse-Opoku, J., Suteliffe, I.C., Tao, L., and Ferretti, J.J., A binding protein dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism. J. Biol. Chem., 267, 4631-4637 (1992).
- 18) Fiedler, G., Pajatsch, M., and Bök, Genetics of novel starch utilization pathway present in Klebsiella oxytoca. J. Mol. Biol., 256, 279-291 (1996).
- 19) Kunkel, T.A., Roberts, J.D., and Zakour, R.A., Rapid and efficient site-specific mutagenesis without phenotypic selection, Methods Enzymol., 154, 367-382 (1987).
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Cloning and Nucleotide Sequence of the Pullulanase Gene of Thermus thermophilus HB8 and Production of the Enzyme in Escherichia coli
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