Change in maltose- and soluble starch-hydrolyzing activities of chimeric α-glucosidases of Mucor javanicus and Aspergillus oryzae

Manabu Sugimoto, Takeshi Ohta, Fusako Kawai

    Research output: Contribution to journalArticlepeer-review

    9 Citations (Scopus)

    Abstract

    The chimeric α-glucosidases of Mucor javanicus and Aspergillus oryzae, which has high activity toward not only maltooligosaccharides but also soluble starch and has high activity toward maltooligosaccharides but faint activity toward soluble starch, respectively, were constructed by shuffling the C-terminal regions where low homology is observed between the two enzymes. The chimera genes were expressed in Pichia pastoris to produce and secrete the enzymes that have predicted molecular masses in the culture medium. The two chimeric M. javanicus α-glucosidases, of which the N- and C-terminal regions are substituted for those of A. oryzae, respectively, decreased in soluble starch-hydrolyzing activity, however, increased in maltose-hydrolyzing activity by 2.1 and 4.9 times higher than that of the native form of M. javanicus α-glucosidase, respectively. The chimeric enzymes changed on the Vmax values for maltose significantly, whereas the Km values were similar to that of the native enzyme.

    Original languageEnglish
    Pages (from-to)1-5
    Number of pages5
    JournalBiochimica et Biophysica Acta - Proteins and Proteomics
    Volume1645
    Issue number1
    DOIs
    Publication statusPublished - Jan 31 2003

    Keywords

    • Aspergillus oryzae
    • Chimeric enzyme
    • Glycoside hydrolase family 31
    • Mucor javanicus
    • Subsite
    • α-Glucosidase

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Biophysics
    • Biochemistry
    • Molecular Biology

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