Loading...
Please wait, while we are loading the content...
Purification and properties of an amylopullulanase, a glucoamylase, and an alpha-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Ganghofner, D. Kellermann, Joseph Bronnenmeier, Karin |
| Copyright Year | 1998 |
| Abstract | Thermoanaerobic bacteria are of considerable interest as producers of thermostable amylolytic enzymes. The soluble amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum DSM 571 was fractionated into a pullulanase, a glucoamylase, and an alpha-glucosidase. The enzymes were purified to homogeneity and their physical and catalytic properties were studied. The pullulanase, which cleaved both alpha-1,4- and alpha-1,6-glucosidic bonds, was an amylopullulanase closely related to similar enzymes from other thermoanaerobic bacteria. Partial amino acid sequences of the glucoamylase were identical with the corresponding sequences deduced from the cga gene encoding the glucoamylase from Clostridium sp. strain G0005. The alpha-glucosidase was identified as an isomaltase belonging to a group of structurally related exo-alpha-1,4-glucosidases and oligo-1,6-glucosidases from bacilli. Comparison of enzyme activities indicated that the glucoamylase had the major amylolytic activity of T. thermosaccharolyticum, with amylopullulanase and alpha-glucosidase assisting in the cleavage of alpha-1,6-glucosidic bonds. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://ci.nii.ac.jp/els/contents110002678967.pdf?id=ART0002951418 |
| PubMed reference number | 9532787v1 |
| Volume Number | 62 |
| Issue Number | 2 |
| Journal | Bioscience, biotechnology, and biochemistry |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Alpha-glucosidase Amino Acid Sequence Amino Acids Bacillus |
| Content Type | Text |
| Resource Type | Article |