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.
| Original language | English |
|---|---|
| Pages (from-to) | 129-131 |
| Number of pages | 3 |
| Journal | Journal of Fermentation and Bioengineering |
| Volume | 69 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1990 |
| Externally published | Yes |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biotechnology
- Applied Microbiology and Biotechnology
- Bioengineering
Cite this
Purification and properties of a low-molecular-weight α-mannosidase from Cellulomonas sp. / Takegawa, Kaoru; Miki, Satoshi; Jikibara, Takayuki; Iwahara, Shojiro.
In: Journal of Fermentation and Bioengineering, Vol. 69, No. 2, 1990, p. 129-131.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and properties of a low-molecular-weight α-mannosidase from Cellulomonas sp.
AU - Takegawa, Kaoru
AU - Miki, Satoshi
AU - Jikibara, Takayuki
AU - Iwahara, Shojiro
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0025118166&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025118166&partnerID=8YFLogxK
U2 - 10.1016/0922-338X(90)90201-7
DO - 10.1016/0922-338X(90)90201-7
M3 - Article
AN - SCOPUS:0025118166
VL - 69
SP - 129
EP - 131
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 2
ER -