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Puri ® cation and characterization of thermostable b-amylase and pullulanase from high-yielding Clostridium thermosulfurogenes SV 2
| Content Provider | Semantic Scholar |
|---|---|
| Author | Reddy, P. Rama Mohan Swamy, M. V. Seenayya, Gunda |
| Copyright Year | 1998 |
| Abstract | Thermostable b-amylase and pullulanase, secreted by the thermophilic anaerobic bacterium Clostridium thermosulfurogenes strain SV2, were puri®ed by salting out with ammonium sulphate, DEAE-cellulose column chromatography, and gel ®ltration using Sephadex G-200. Maltose was identi®ed as a major hydrolysis product of starch by b-amylase, and maltotriose was identi®ed as a major hydrolysis product of pullulan by pullulanase. The molecular masses of native b-amylase and pullulanase were determined to be 180 and 100 kDa by gel ®ltration, and 210 and 80 kDa by SDS±PAGE, respectively. The temperature optima of puri®ed b-amylase and pullulanase were 70 and 75 °C, respectively, and both enzymes were completely stable at 70 °C for 2 h. The presence of starch further increased the stability of both the enzymes to 80 °C and both displayed a pH activity optimum of 6.0. The starch hydrolysis products formed by b-amylase action had b-anomeric form. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.aarnavi.com/paduru/papers/wjmb.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
