Most cited article - PubMed ID 3131218
Formation of some extracellular enzymes during the exponential growth of Bacillus subtilis
Bacillus subtilis 115 grew in a medium with amino acids and glucose with the maximum specific growth rates mu of 1.20-1.10/h in the temperature range of 45-48 degrees C. Activity of the extracellular neutral proteinase excreted by 1.3 mg/mL dry mass during 8 h of the postexponential and stationary growth phases decreased from its maximum value of 0.23 TU/mL at 40 degrees C to 0.13 and 0.06 TU/mL at 45 and 48 degrees C, respectively. Formation of the extracellular serine proteinase decreased even more - from 0.18 TU/mL at 40 degrees C to 0.06 and 0.03 TU/mL at 45 and 48 degrees C, respectively. Sporulation, expressed as the portion of sporangia with refractile spores at the 6th h of the stationary phase decreased from 46% at 40 degrees C to 17 and 3% at 45 and 48 degrees C, respectively.
- MeSH
- Bacillus subtilis physiology MeSH
- Cell Division MeSH
- Endopeptidases biosynthesis MeSH
- Metalloendopeptidases biosynthesis MeSH
- Spores, Bacterial physiology MeSH
- Subtilisins biosynthesis MeSH
- Hot Temperature MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Endopeptidases MeSH
- Metalloendopeptidases MeSH
- Subtilisins MeSH
Growth, differential rate of alpha-amylase synthesis and production characteristics of Bacillus subtilis DP 1 (isolate from starch materials) in comparison with 10 Bacillus strains were examined in batch fermentation. The effect of the carbon and nitrogen source was evaluated with regard to cell growth and enzyme production. The pH optimum of enzyme activity was 6.5 and temperature optimum of 60 degrees C.
- MeSH
- alpha-Amylases biosynthesis MeSH
- Bacillus subtilis enzymology growth & development MeSH
- Cell Division physiology MeSH
- Nitrogen physiology MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Culture Media pharmacology MeSH
- Temperature MeSH
- Carbon physiology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- alpha-Amylases MeSH
- Nitrogen MeSH
- Culture Media MeSH
- Carbon MeSH