Screening of Bacillus subtilis Bs-W5 Medium and Optimization of Culture Conditions

2019 ◽  
Vol 08 (02) ◽  
pp. 93-101
Author(s):  
琳 王
Keyword(s):  
Bacillus Subtilis ◽  
Culture Conditions ◽  
Optimization Of Culture Conditions

Optimization of Culture Conditions for Biosynthesis of Lipopeptide by Bacillus Subtilis with Starch

2013 ◽  
Vol 291-294 ◽  
pp. 225-229 ◽  
Author(s):  
Zong Ming Zheng ◽  
Ti Peng Wang ◽  
Qin Wu
Keyword(s):  
Bacillus Subtilis ◽  
Culture Conditions ◽  
Culture Temperature ◽  
Ph Optimum ◽  
Linear Effect ◽  
Initial Ph ◽  
Culture Cycle ◽  
Optimization Of Culture Conditions ◽  
Fermentation Parameters ◽  
Main Effects

Optimization of culture conditions for lipopeptide production of lipopeptide by Bacillus subtilis NEL-01 was carried out in shaker flask batch fermentations using composite central design of response surface methodology (RSM). A five-level three-factor central composite design was employed to determine the maximum lipopeptide production at optimum levels for culture temperature, initial pH and culture cycle. Culture temperature and culture cycle showed the significant linear main effects, while pH had no significant linear effect. The production was also significantly affected by quadratic effect of culture temperature and initial pH. Optimum fermentation parameters were predicted at temperature, initial pH, and culture cycle of 34.81 °C, 7.33g/l, 49.26 h, respectively. The prediction lipopeptide yield was 1879.56 mg/l. The subsequent experiments confirmed the prediction.

scholarly journals Isolation and Optimization of Culture Conditions of Thraustochytrium kinnei for Biomass Production, Nanoparticle Synthesis, Antioxidant and Antimicrobial Activities

2021 ◽  
Vol 9 (6) ◽  
pp. 678
Author(s):  
Kaliyamoorthy Kalidasan ◽  
Nabikhan Asmathunisha ◽  
Venugopal Gomathi ◽  
Laurent Dufossé ◽  
Kandasamy Kathiresan
Keyword(s):  
Antimicrobial Activity ◽  
Gold Nanoparticles ◽  
Silver Nanoparticles ◽  
Biomass Production ◽  
Petroleum Ether Extract ◽  
Antimicrobial Activities ◽  
Culture Conditions ◽  
Gold And Silver Nanoparticles ◽  
Optimization Of Culture Conditions ◽  
Antioxidant And Antimicrobial Activities

This work deals with the identification of a predominant thraustochytrid strain, the optimization of culture conditions, the synthesis of nanoparticles, and the evaluation of antioxidant and antimicrobial activities in biomass extracts and nanoparticles. Thraustochytrium kinnei was identified as a predominant strain from decomposing mangrove leaves, and its culture conditions were optimized for maximum biomass production of 13.53 g·L−1, with total lipids of 41.33% and DHA of 39.16% of total fatty acids. Furthermore, the strain was shown to synthesize gold and silver nanoparticles in the size ranges of 10–85 nm and 5–90 nm, respectively. Silver nanoparticles exhibited higher total antioxidant and DPPH activities than gold nanoparticles and methanol extract of the strain. The silver nanoparticles showed higher antimicrobial activity than gold nanoparticles and petroleum ether extract of the strain. Thus, Thraustochytrium kinnei is proven to be promising for synthesis of silver nanoparticles with high antioxidant and antimicrobial activity.

scholarly journals 4-Aminobutyrate (GABA) transporters from the amine-polyamine-choline superfamily: substrate specificity and ligand recognition profile of the 4-aminobutyrate permease from Bacillus subtilis

1998 ◽  
Vol 333 (3) ◽  
pp. 565-571 ◽  
Author(s):  
Casey E. BRECHTEL ◽  
Steven C. KING
Keyword(s):  
Bacillus Subtilis ◽  
Culture Conditions ◽  
Ligand Recognition ◽  
Open Chain ◽  
Conformationally Constrained ◽  
E Coli ◽  
Gaba Transporters ◽  
Transport Defect ◽  
Gaba Analogues ◽  
Limited Culture

A previous study [Ferson, Wray and Fisher (1996) Mol. Microbiol. 22, 693–701] has shown that transposon-mediated disruption of a protein 47% identical to the Escherichia coli GABA (4-aminobutyrate) transporter abolishes the ability of nitrogen-limited culture conditions to induce expression of a GABA transport activity in Bacillus subtilis. Here it is demonstrated directly that the B. subtilis GABA permease (gabP) gene can complement the transport defect in the gabP-negative E. colistrain. Unexpectedly, the ligand-recognition profile of the B. subtilis GabP was found to differ substantially from that of the highly homologous E. coli GabP. Unlike the E. coli GabP, the B. subtilis GabP: (i) exhibits approx. equal preference for the 3-carbon (β-alanine, Km = 9.6 µM) and the 4-carbon (GABA, Km = 37 µM) amino acids, and (ii) resists inhibition by bulky, conformationally constrained compounds (e.g. nipecotic acid, guvacine), which are active against GABA transporters from brain. The present study shows additionally that the B. subtilis GabP can translocate several open-chain GABA analogues (3-aminobutyrate, 3-aminopropanoate, cis-4-aminobutenoate) across the membrane via counterflow against [3H]GABA. Thus, consistent with the idea that the ligand-recognition domain of the B. subtilis GabP is less spacious than that of the close homologue from E. coli, the former exhibits more stringent requirements than the latter for substrate recognition and translocation. These distinct functional characteristics of the E. coli and B. subtilis GABA transporters provide a basis by which to identify ligand-recognition domains within the amine-polyamine-choline transporter superfamily.

Effect of temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37

2021 ◽  
Vol 66 (1) ◽  
pp. 72-79
Author(s):  
Thuoc Doan Van ◽  
Hung Nguyen Phuc
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Animal Feed ◽  
Culture Conditions ◽  
Effect Of Temperature ◽  
Physical Parameters ◽  
Original Activity ◽  
Optimum Ph ◽  
Production Activity ◽  
Ph Range

The effect of physical parameters such as temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37 was investigated. The results indicated that the optimum culture conditions for enzyme activity were pH 7.0 and 35 oC. The optimum pH and temperature for enzyme activity were 6.0 and 70 oC. The crude enzyme was found to be stable in the pH range of 5.0 to 7.0. The enzyme was stable for 1 h at a temperature from 30 to 80 oC; nearly 100% of enzyme activity remained at temperatures of 30 - 40 oC, and about 34% of original activity remained at a temperature of 80 oC. These features demonstrated that α-amylase from B. subtilis V37 can be applied in many areas such as the food, fermentation, and animal feed industries.

Sign in / Sign up

Export Citation Format

Share Document