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 journalArticle

33 Citations (Scopus)

Abstract

The fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N. et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993), 60, 293-300 (1996), and 63, 2031-2033 (1999)] 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 - Aug 2000

Fingerprint

Oligochaeta
Serine Proteases
Peptide Hydrolases
Enzymes
Elastin
Soy Foods
Peptones
3-Hydroxybutyric Acid
Hemoglobin
Toluene
Antioxidants
Hexane
Fibrin
Microorganisms
Organic solvents
Hydrolysis
Esters
Hemoglobins
Proteins
Degradation

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

Stable earthworm serine proteases : Application of the protease function and usefulness of the earthworm autolysate. / Nakajima, Nobuyoshi; Sugimoto, Manabu; Ishihara, Kohji.

In: Journal of Bioscience and Bioengineering, Vol. 90, No. 2, 08.2000, p. 174-179.

Research output: Contribution to journalArticle

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