Stable earthworm serine proteases: Application of the protease function and usefulness of the earthworm autolysate

Nobuyoshi Nakajima, Manabu Sugimoto, Kohji Ishihara

    Research output: Contribution to journalArticlepeer-review

    33 Citations (Scopus)

    Abstract

    The fibrinolytic enzymes from Lumbricus rubellus were further characterized to exploit their catalytic functions. These enzymes are stable in solution for long periods at room temperature and strongly resistant to organic solvents, even toluene and n-hexane. The serine proteases can act on various protein substrates such as elastin and hemoglobin as well as fibrin, and also catalyzed the hydrolysis of esters such as ethyl acetate and a bioplastic, poly[(R)-3-hydroxybutyrate] film. The enzymes, in the absence of microbial degradation, contributed to the production of the earthworm autolysate possessing antioxidant ability and protease activity, whose components were similar to those of soy sauce. The extract of the earthworm autolysate could be used as a peptone substitute in media for the cultivation of microorganisms.

    Original languageEnglish
    Pages (from-to)174-179
    Number of pages6
    JournalJournal of Bioscience and Bioengineering
    Volume90
    Issue number2
    DOIs
    Publication statusPublished - 2000

    Keywords

    • Autolysate
    • Autolysis
    • Degradation
    • Earthworm
    • Fibrinolytic enzyme
    • Serine protease
    • Stability

    ASJC Scopus subject areas

    • Biotechnology
    • Bioengineering
    • Applied Microbiology and Biotechnology

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