A /3-cyclodextrin glucosyltransferase was purified from alkalophilic Bacilhs sp. No. 562 over 64-fold with a yield of 32%. Its molecular size was estimated to be 170 kDa by gel &ration and 82 kDa by SDS-PAGE, with a pI of 7.2. The enzyme showed optimum activity at 65ยฐC and pH 7.0. It was stable from
Partial purification and some properties of an alkaline cellulase from an alkalophilicBacillussp.
โ Scribed by H. Khyami-Horani
- Publisher
- Springer
- Year
- 1996
- Tongue
- English
- Weight
- 532 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1573-0972
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โฆ Synopsis
A newly isolated Bacillus species, which grew optimally at 30ยฐC and pH 10, produced a carboxymethylcellulase in a medium containing 10 g CM-cellulose/l. The enzyme, when partially purified by gel filtration, had a mass of about 29 kDa as determined by both SDS-PAGE and gel filtration chromatography. It was optimally active at pH 9.5 and 40ยฐC, and was stable from pH 7 to 11 at 4ยฐC for 24 h. The enzyme was stimulated by Ca(2+) (1mM) but was completely inhibited by Hg(2+) (1MM). Neither EDTA nor EGTA (10MM) affected the activity.
๐ SIMILAR VOLUMES
To obtain a new serine protease from alkalophilic Bacillus sp. NKS-21, shotgun cloning was carried out. As a result, a new protease gene was obtained. It encoded an intracellular serine protease (ISP-1) in which there was no signal sequence. The molecular weight was 34,624. The protease showed about