Abstract
β-Amylase is an exo-type enzyme that hydro-lyzes starch by removing stepwise maltose of the β-anomeric configuration from the nonre-ducing end of the starch molecule. Although α-amylases, endo-type enzymes that hydro-lyze α-1,4 linkages of starch at random, are distributed in various kinds of organisms, β-amylases are known to be produced only by plants and certain bacteria. Extensive studies on α-amylases have revealed that α-amylases of diverse origins from mammalian to bacterial contain common well-conserved regions including active centers (Toda et al., 1982; Nakajima et al., 1986). Three-dimensional structures of α-amylases from Aspergillus oryzae and porcine have been determined at 3 and 2.9 Å resolution, respectively (Matsuura et al., 1984; Buisson et al., 1987).
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Yamagata, H., Udaka, S. (1993). Nucleotide Sequence of the Gene and Primary Structure of the Thermophilic β-Amylase from Clostridium thermosulfurogenes . In: Sebald, M. (eds) Genetics and Molecular Biology of Anaerobic Bacteria. Brock/Springer Series in Contemporary Bioscience. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-7087-5_31
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DOI: https://doi.org/10.1007/978-1-4615-7087-5_31
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