Structure of the Raw-starch-affinity Site on the Aspergillus awamori var. kawachi Glucoamylase I Molecule

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概要

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• The raw-starch-affinity site of Aspergillus awamori var. kawachi glucoamylase I (GAI), that was proved to be essential for its adsorbability and digestibility on raw starch granules, was found to be located separately from the active site in the region corresponding to glycopeptide I (Gp-I) liberated from the glucoamylase I through the action of subtilisin. Gp-I consists of 45 amino acid residues, hydroxy amino acids being characteristically abundant, and 56 mannose residues. The sequence was determined with an automatic amino acid sequencer to be ATGGTTTTATTTGSGGVTST SKTTTTASKTSTTTSSTSCTTPTAV. A structure of parallelly arranged short mannoside chains linked o-glycosidically to the successive sequence of hydroxy amino acid residues on Gp-I was revealed. On comparison of the amino acid sequence of Gp-I with those of three glucoamylases, from Aspergillus awamori, Aspergillus niger and Rhizopus oryzae, significantly homologous regions (91%, 91% and 77% homology, respectively) were detected as the affinity site that could be functionally constrained and essential for raw-starch-digesting glucoamylase.

• 社団法人 日本農芸化学会の論文

著者

• Miyata T

  Hiroshima Univ. Hiroshima Jpn

• Hayashida Shinsaku

  Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Kyushu University

• NAKAHARA Koichi

  Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Kyushu University

• KURODA Kazutaka

  Laboratory of Applied Microbiology, Department of Agricultural Chemistry

• MIYATA Toshiyuki

  Laboratory of Protein Chemistry, Department of Biology, Kyushu University

• IWANAGA Sadaaki

  Laboratory of Protein Chemistry, Department of Biology, Kyushu University

• NAKAHARA Koichi

  Laboratory of Applied Microbiology, Department of Agricultural Chemistry

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