scholarly journals Cow Dung Substrate for the Potential Production of Alkaline Proteases by Pseudomonas putida Strain AT in Solid-State Fermentation

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Ponnuswamy Vijayaraghavan ◽  
Sreekumar Saranya ◽  
Samuel Gnana Prakash Vincent

Cow dung and agroresidues were used as the substrates for the production of alkaline proteases by Pseudomonas putida strain AT in solid-state fermentation. Among the various substrates evaluated, cow dung supported maximum (1351±217 U/g) protease production. The optimum conditions for the production of alkaline proteases were a fermentation period of 48 h, 120% (v/w) moisture, pH 9, and the addition of 6% (v/w) inoculum, 1.5% (w/w) trehalose, and 2.0% (w/w) yeast extract to the cow dung substrate. The enzyme was active over a range of temperatures (50–70°C) and pHs (8–10), with maximum activity at 60°C and pH 9. These enzymes showed stability towards surfactants, detergents, and solvent and digested various natural proteins.

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Abdilbar Usman ◽  
Said Mohammed ◽  
Jermen Mamo

Acid proteases represent an important group of enzymes, extensively used in food and beverage industries. There is an increased demand for acid proteases adapting to the industrial extreme environment, especially lower pH. Thus, this necessitates the search for a better acid protease from fungi that best performs in industrial conditions. The fungal isolates were isolated from grape and dairy farm soil using potato dextrose agar and further screened for protease production based on the hydrolysis of clear zone on skim milk agar. The potential fungi were then subjected to secondary screening under solid-state fermentation (SSF). After the secondary screening, the potential fungus was identified to the genus level by the macroscopic and microscopic methods. The growth conditions and media composition for the potential fungus were further optimized under SSF. The crude enzyme produced by the potential isolate was characterized after partial purification by acetone and ammonium sulfate precipitation. A total of 9 fungal isolates showed protease production in primary and secondary screening; however, one potential isolate (Z1BL1) was selected for further study based on its protease activity. The isolate was identified to the genus Aspergillus based on their morphological features. The maximum acid protease from the isolate Z1BL1 was obtained using fermentation media containing wheat bran as a solid substrate, 1 mL of 3.2 × 106 inoculum size, 50% moisture content, and pH 4.5 upon 120-h incubation at 30°C. The acetone-precipitated enzyme exhibited the maximum activity at 50°C and pH 5 with stability at pH 4–6 and temperature 40–60°C. Thus, the acid protease produced from Aspergillus showed suitable enzyme characteristics required in the industry and could be a candidate for application in the food industry after further purification.


BioResources ◽  
2019 ◽  
Vol 15 (1) ◽  
pp. 429-443
Author(s):  
Jing Bai ◽  
Fengli Liu ◽  
Siqi Li ◽  
Pan Li ◽  
Chun Chang ◽  
...  

Solid-state fermentation was carried out for production of gibberellin via the addition of enzymatic hydrolysate from steam-exploded corn stalks during the culture period. The enzymatic hydrolysate from the steam-exploded corn stalks was added to the culture medium during the solid-state fermentation period, which improved gibberellin production. When the enzymatic hydrolysate was added into the 400 mL/kg dry basis substrate in the solid-state fermentation after 60 h, the temperature was 30 °C, the pH was 7.00, the mass ratio of solid to liquid was 1:1.1, and the fermentation period was 168 h. This led to the largest gibberellin yield (9.48 g/kg dry basis), and when compared with pre-optimization, the gibberellin yield increased by 135%. The optimum conditions to maximize the biomass for the fermentation process were obtained; the temperature was 32 °C for a gibberellin yield of 9.20 g/kg dry basis, the pH was 6.00 and the mass ratio of solid to liquid was 1:1.1 for a gibberellin yield of 9.48 g/kg dry basis, and the fermentation period was 96 h for a gibberellin yield of 6.94 g/kg dry basis. Therefore, a new alternative way for gibberellin production via solid-state fermentation has been demonstrated.


2008 ◽  
Vol 83 (7) ◽  
pp. 1012-1018 ◽  
Author(s):  
Jarun Chutmanop ◽  
Sinsupha Chuichulcherm ◽  
Yusuf Chisti ◽  
Penjit Srinophakun

2016 ◽  
Vol 29 (1) ◽  
pp. 222-233 ◽  
Author(s):  
TAMIRES CARVALHO DOS SANTOS ◽  
GEORGE ABREU FILHO ◽  
AILA RIANY DE BRITO ◽  
AURELIANO JOSÉ VIEIRA PIRES ◽  
RENATA CRISTINA FERREIRA BONOMO ◽  
...  

ABSTRACT: Prickly palm cactus husk was used as a solid-state fermentation support substrate for the production of cellulolytic enzymes using Aspergillus niger and Rhizopus sp. A Box-Behnken design was used to evaluate the effects of water activity, fermentation time and temperature on endoglucanase and total cellulase production. Response Surface Methodology showed that optimum conditions for endoglucanase production were achieved at after 70.35 h of fermentation at 29.56°C and a water activity of 0.875 for Aspergillus niger and after 68.12 h at 30.41°C for Rhizopus sp. Optimum conditions for total cellulase production were achieved after 74.27 h of fermentation at 31.22°C for Aspergillus niger and after 72.48 h and 27.86°C for Rhizopus sp. Water activity had a significant effect on Aspergillus niger endoglucanase production only. In industrial applications, enzymatic characterization is important for optimizing variables such as temperature and pH. In this study we showed that endoglucanase and total cellulase had a high level of thermostability and pH stability in all the enzymatic extracts. Enzymatic deactivation kinetic experiments indicated that the enzymes remained active after the freezing of the crude extract. Based on the results, bioconversion of cactus is an excellent alternative for the production of thermostable enzymes.


2021 ◽  
Vol 320 ◽  
pp. 124222
Author(s):  
Ibrahim M. Banat ◽  
Quentin Carboué ◽  
Gerardo Saucedo-Castañeda ◽  
José de Jesús Cázares-Marinero

2019 ◽  
Vol 42 (8) ◽  
pp. 1325-1332 ◽  
Author(s):  
Tania Maria Costa ◽  
Vander Kaufmann ◽  
Camila Jeriane Paganelli ◽  
Diogo Alexandre Siebert ◽  
Gustavo Amadeu Micke ◽  
...  

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Ponnuswamy Vijayaraghavan ◽  
P. Rajendran ◽  
Samuel Gnana Prakash Vincent ◽  
Arumugaperumal Arun ◽  
Naif Abdullah Al-Dhabi ◽  
...  

Fibrinolytic enzymes have wide applications in clinical and waste treatment. Bacterial isolates were screened for fibrinolytic enzyme producing ability by skimmed milk agar plate using bromocresol green dye, fibrin plate method, zymography analysis, and goat blood clot lysis. After these sequential screenings,Bacillussp. IND12 was selected for fibrinolytic enzyme production.Bacillussp. IND12 effectively used cow dung for its growth and enzyme production (687±6.5 U/g substrate). Further, the optimum bioprocess parameters were found out for maximum fibrinolytic enzyme production using cow dung as a low cost substrate under solid-state fermentation. Two-level full-factorial experiments revealed that moisture, pH, sucrose, peptone, and MgSO4were the vital parameters with statistical significance (p<0.001). Three factors (moisture, sucrose, and MgSO4) were further studied through experiments of central composite rotational design and response surface methodology. Enzyme production of optimized medium showed4143±12.31 U/g material, which was more than fourfold the initial enzyme production (978±36.4 U/g). The analysis of variance showed that the developed response surface model was highly significant (p<0.001). The fibrinolytic enzyme digested goat blood clot (100%), chicken skin (83±3.6%), egg white (100%), and bovine serum albumin (29±4.9%).


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