A soil isolate of Bacillus stearothermophilus was found to synthesize thermostable alpha-amylase. The enzyme was purified to homogeneity by ammonium sulfate fractionation and IECC on DEAE-cellulose column. The purified enzyme was considered to be a monomeric protein with a molar mass of 64 kDa, as determined by SDS-PAGE. The enzyme showed a wide range of pH tolerance and maximum activity at pH 7.0. The temperature tolerance was up to 100 degrees C with more than 90% catalytic activity; the maximum activity was observed at 50 degrees C. Divalent metal ions exhibited inhibitory effect on the enzyme activity. However, proteinase inhibitor did not react positively.
- MeSH
- alfa-amylasy chemie izolace a purifikace metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- Geobacillus stearothermophilus enzymologie izolace a purifikace MeSH
- koncentrace vodíkových iontů MeSH
- půdní mikrobiologie MeSH
- teplota MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- alfa-amylasy MeSH
To improve the yield of lysine by the isolate, auxotrophic mutants were isolated. Among the mutants, only one auxotrophic mutant required vitamin B12. This mutant produced alpha-alanine. About 200 mutants resistant to the lysine analog S-(2-aminoethyl)-L-cysteine were isolated and some of them produced well above the wild type.
- MeSH
- alanin biosyntéza MeSH
- antibiotická rezistence genetika MeSH
- Arthrobacter genetika izolace a purifikace metabolismus MeSH
- bakteriologické techniky MeSH
- cystein analogy a deriváty farmakologie MeSH
- lysin biosyntéza MeSH
- methylnitronitrosoguanidin MeSH
- mutace MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- alanin MeSH
- cystein MeSH
- lysin MeSH
- methylnitronitrosoguanidin MeSH
- S-2-aminoethyl cysteine MeSH Prohlížeč
