Purification and properties of a low-molecular-weight α-mannosidase from Cellulomonas sp.

Kaoru Takegawa, Satoshi Miki, Takayuki Jikibara, Shojiro Iwahara

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Cellulomonas sp. isolated from soil produces a high level of α-mannosidase (α-mannanase) inductively in culture fluid. The enzyme had two different molecular weight forms, and the properties of the high-molecular-weight form were reported previously (Takegawa, K. et al.: Biochim. Biophys. Acta, 991, 431-437, 1989). The low-molecular-weight α-mannosidase was purified to homogeneity by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was over 150,000 by gel filtration. Unlike the high-molecular-weight form, the low-molecular-weight enzyme readily hydrolyzed α-1,2- and α-1,3-linked mannose chains.

Original languageEnglish
Pages (from-to)129-131
Number of pages3
JournalJournal of Fermentation and Bioengineering
Issue number2
Publication statusPublished - 1990
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Applied Microbiology and Biotechnology
  • Biotechnology


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