Substrate and energy costs of the production of exocellular enzymes by Bacillus licheniformis
โ Scribed by J. Frankena; H. W. Van Verseveld; A. H. Stouthamer
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 945 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
โฆ Synopsis
Substrate and energy costs of the production of exocellular enzymes from glucose and citrate by B. licheniformis S1684 as well as molar growth yields corrected for these costs of product formation were calculated using data from chemostat experiments. The calculations showed that 1.46-1.73 mol glucose and 2.31-2.77 mol citrate are needed for formation and excretion of 1 mol protein. Consequently, t h e values o f t h e m a x i m a l p r o d u c t y i e l d f r o m s u b s t r a t e CY,,,, g / m o l ) a r e 80 < Y,,, < 95 when product is formed from glucose and 50 < Y,,, < 60 when product is formed from citrate. The higher substrate costs for product formation from citrate are due to a higher level of C 0 2 production during protein formation and a higher substrate requirement for the energy supply of product formation and excretion than when product is formed from glucose.
The theoretical ATP requirement for protein synthesis could be determined reasonably well, but the energy costs of protein excretion could not be determined exactly. The energy costs of protein formation are higher than those of biomass formation or protein excretion. Molar growth yields corrected for the substrate costs of product formation were high, indicating a high efficiency of growth.
Growth and production parameters were determined as well from experimental data of recycling fermentor experiments using a parameter optimization procedure based on a mathematical model describing biomass growth as a linear function of the substrate consumption rate and the rate of product formation as a linear function of biomass growth rate. The fitting procedure yielded two growth and production domains during glucose limitation. In the first domain the values for the maximal growth yield and maintenance coefficient were in agreement with those found i n chemostat experiments at corresponding values of Y,,,. Domain 2 could be described best w i t h linear g r o w t h and product formation. In domain 2 the rate of product formation decreased and more substrate became available for biomass formation. As a consequence the specific growth rate increased in the shift from domain 1 to 2. Domain 2 behavior most probably is caused by the relstatus of 8. licheniformis S1684.
๐ SIMILAR VOLUMES
## Abstract The simultaneous production of ฮฑโamylase, ฮฒโglucanase and proteolytic enzymes by __Bacillus subtilis__ has been studied. The effect of culturing conditions on the simultaneous production of these enzymes has also been investigated. Two known strains were used as standards, the other str
Current methods for reengineering enzyme substrate specificities rely heavily on the use of static x-ray crystallographic models. In this article we detail the use of a molecular mechanics approach for suggesting regions of Bacillus stearothermophilus Llactate dehydrogenase (EC 1.1.1.27) involved in
## Abstract Lipopeptide biosurfactants produced by the __Bacillus licheniformis__ V9T14 strain showed an interesting antiโadhesion activity against biofilm formation of human pathogenic bacterial strains. The chemical characterisation of the crude extract of V9T14 strain was first developed through