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

Authors :
Takayuki Jikibara
Kaoru Takegawa
Satoshi Miki
Shojiro Iwahara
Source :
Journal of Fermentation and Bioengineering. 69:129-131
Publication Year :
1990
Publisher :
Elsevier BV, 1990.

Abstract

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.

Details

ISSN :
0922338X
Volume :
69
Database :
OpenAIRE
Journal :
Journal of Fermentation and Bioengineering
Accession number :
edsair.doi...........ce73c5dd2e3ab6551bb183aa5287748c