scholarly journals Improved Rifamycin B Production byNocardia mediterraneiMTCC 14 under Solid-State Fermentation through Process Optimization

2014 ◽  
Vol 2014 ◽  
pp. 1-13 ◽  
Author(s):  
Basavaraj M. Vastrad ◽  
Shivayogeshwar E. Neelagund ◽  
Sudhir R. Iiger ◽  
Ajeet M. Godbole ◽  
Venkatrao Kulkarni

Optimization of various production parameters using response surface methodology (RSM) was performed to assess maximum yield of rifamycin B fromNocardia mediterraneiMTCC 14. Plackett-Burman design test was applied to determine the significant effects of various production parameters such as glucose, maltose, ribose, galactose, beef extract, peanut meal, ammonium chloride, ammonium sulphate, barbital, pH, and moisture content on production of rifamycin B. Among the eleven variables tested, galactose, ribose, glucose, and pH were found to have significant effect on rifamycin B production. Optimum levels of the significant variables were decided by using a central composite design. The most appropriate condition for production of rifamycin B was found to be a single step production at galactose (8% w/w), ribose (3% w/w), glucose (9% w/w), and pH (7.0). At these optimum production parameters, the maximum yield of rifamycin B obtained experimentally (9.87 g/kgds dry sunflower oil cake) was found to be very close to its predicted value of 10.35 g/kgds dry sunflower oil cake. The mathematical model developed was found to fit greatly with the experimental data of rifamycin B production.

2010 ◽  
Vol 22 (2) ◽  
pp. 281-296 ◽  
Author(s):  
M. Mašković ◽  
B. Jančić-Stojanović ◽  
A. Malenović ◽  
D. Ivanović ◽  
M. Medenica

2021 ◽  
Vol 166 ◽  
pp. 113488
Author(s):  
Agnese Spadi ◽  
Giulia Angeloni ◽  
Lorenzo Guerrini ◽  
Ferdinando Corti ◽  
Marco Michelozzi ◽  
...  

2021 ◽  
Vol 19 (1) ◽  
pp. 326-332
Author(s):  
Ana Paula Ferreirade Souza ◽  
Mateus Henrique Petrarca ◽  
Patrícia Aparecida de Campos Braga ◽  
Nadia Regina Rodrigues ◽  
Felix Guillermo Reyes Reyes

2013 ◽  
Vol 31 (No. 6) ◽  
pp. 627-632 ◽  
Author(s):  
O.G. Nagel ◽  
M.P. Molina ◽  
R.L. Althaus

We proposed an experimental design of a microbial bioassay of dichotomous response (positive or negative) using Bacillus subtilis BGA for the detection of sulfonamide residues. In the first stage, the bioassay response time was reduced to 6 h by increasing the spore concentration of B. subtilis. Then, the effects of spore, indicator, trimethoprim (TMP) concentration, and volume of the culture medium were examined with a Plackett Burman design (2<sup>4-1</sup>). Finally, the effect of TMP concentration on the method detection capabilities and specificity was analysed using a logistic model with interaction. The detection capabilities of sulfonamides in milk are close to the MRLs when using 500 mg/l of TMP in the culture medium of the bioassay. It is concluded that the experimental design techniques and a logistic regression model can be used to design successfully a dichotomous response bioassay.


2020 ◽  
Vol 45 (1-2) ◽  
pp. 25-38
Author(s):  
RENU KAUL ◽  
◽  
SANJOY ROY CHOWDHURY ◽  

Author(s):  
Graciella da Silva Campello ◽  
Renata Aguirre Trindade ◽  
Tatiane Vieira Rêgo ◽  
Janaína Fernandes de Medeiros Burkert ◽  
Carlos André Veiga Burkert

Abstract The main goal of this study was to investigate the immobilization of commercial ß-galactosidase from Kluyveromyces lactis (Lactozym®) on Eupergit® C. A Plackett-Burman design was proposed. The ionic strength and pH were the variables that presented significant effect (p<0.1) on immobilization. The increase in the ionic strength from 0.1 to 1.5 M and the increase in pH from 6.6 to 7.4 represented an increase of 28.56% and a reduction of 18.19% in the immobilization yield, respectively. At 25°C, pH 6.6, ionic strength of 1.5 M, immobilization for 8 h, 1 mM of divalent magnesium ion and 0.4 mL of enzyme added, reached 85% immobilization yield. The free and immobilized enzymes were characterized. pH and temperature profiles showed maximum activity at pH 6.6 and 45°C, for both free and immobilized enzymes. There was a gain in thermal stability with enzyme immobilization and there was an increase of about four times in the half-life of the immobilized derivative at 45°C (from 0.43 h to 1.78 h). This greater thermal stability was also made clear through the calculation of thermodynamic parameters (ΔH, ΔG and ΔS). Km values, 30.33 mM and 104.00 mM for free and immobilized enzymes, respectively, represented a reduction in substrate affinity after immobilization, possibly owing to stereo-conformational factors. In a batch reactor for lactose hydrolysis from cheese whey, an increase in lactose conversion with immobilization was observed at 40°C and 45°C (90.43% and 65.36%, respectively) in relation to the free enzyme (84.17% and 39.58%, respectively).


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