Characterization and mode of action of exo-1,3-β-d-glucanase from Aspergillus saitoi

Shin Kasahara, Tasuku Nakajima, Chikara Miyamoto, Kenji Wada, Yasuhiro Furuichi, Eiji Ichishima

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)


    An acid exo-β-1,3-d-glucanase was isolated from the commercial digestive enzyme Molsin prepared from Aspergillus saitoi. The enzyme had a molecular weight of 57,000, isoelectric point of pH 4.1, optimum pH of 3.8 and an optimum temperature of 50°C. Major amino acid components of the enzyme were Asx, Ser, Thr and Gly which comprised more than 60% of the molecule, while 11% was carbohydrates. The N-terminal amino acid was determined to be Gly. The enzyme acted on the β-1,3-d-glucan (Pachyman) or laminaritetraose in an exo-type manner and the hydrolysis product was α-d-glucose.

    Original languageEnglish
    Pages (from-to)238-240
    Number of pages3
    JournalJournal of Fermentation and Bioengineering
    Issue number4
    Publication statusPublished - 1992

    ASJC Scopus subject areas

    • Biotechnology
    • Applied Microbiology and Biotechnology


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