Enhanced production of violacein by Chromobacterium violaceum using agro‐industrial waste soybean meal

Author(s):  
Nisarg Gohil ◽  
Gargi Bhattacharjee ◽  
Manoj Gayke ◽  
Hanuman Narode ◽  
Khalid J. Alzahrani ◽  
...  
2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Hamid Mukhtar ◽  
Ikramul Haq

The present study describes the screening of different agroindustrial byproducts for enhanced production of alkaline protease by a wild and EMS induced mutant strain ofBacillus subtilisIH-72EMS8. During submerged fermentation, different agro-industrial byproducts were tested which include defatted seed meals of rape, guar, sunflower, gluten, cotton, soybean, and gram. In addition to these meals, rice bran, wheat bran, and wheat flour were also evaluated for protease production. Of all the byproducts tested, soybean meal at a concentration of 20 g/L gave maximum production of the enzyme, that is, 5.74  ±  0.26 U/mL from wild and 11.28  ±  0.45 U/mL from mutant strain, during submerged fermentation. Different mesh sizes (coarse, medium, and fine) of the soybean meal were also evaluated, and a finely ground soybean meal (fine mesh) was found to be the best. In addition to the defatted seed meals, their alkali extracts were also tested for the production of alkaline protease byBacillus subtilis, but these were proved nonsignificant for enhanced production of the enzyme. The production of the enzyme was also studied in solid state fermentation, and different agro-industrial byproducts were also evaluated for enzyme production. Wheat bran partially replaced with guar meal was found as the best substrate for maximum enzyme production under solid state fermentation conditions.


1996 ◽  
Vol 76 (1) ◽  
pp. 105-112 ◽  
Author(s):  
P. H. Robinson

Primiparous dairy cows were utilized in two experiments to evaluate the productive benefits of modifying the strategy of within-day feeding of soybean meal (SBM) as a supplement to a basal mixed ration fed twice daily. The design of the two experiments was the same, although one was completed with early-lactation cows and the other with late-lactation cows. The evaluation of protein status of all treatments, after the experiments were complete, indicated that cows were limited by supplies of digestible undegraded intake protein (DUIP) on all treatments of both experiments. However, benefits of feeding 800 g d−1 of supplemental SBM versus none were primarily restricted to enhanced production of milk protein, and it is suggested that this was primarily the result of the contribution of DUIP from SBM to intestinal protein supply. Feeding SBM in two versus four daily meals either 1 or 1 and 5 h, respectively, after offer of the mixed ration had no influence on animal performance at either stage of lactation. However, feeding SBM in two daily meals 1 h prior to the mixed ration versus in two daily meals 1 h after offer of the mixed ration enhanced milk, milk energy, and milk lactose output in late lactation, but not in early lactation. These apparently inconsistent production responses between stages of lactation are consistent with a hypothesis that microbial growth is progressively restricted as supplies of degraded intake protein (DIP), relative to requirements, decline. Under these conditions, which applied to the late-lactation cows, feeding DIP at times of the day when rumen-soluble N levels would be lowest (i.e., pre-feeding) would be beneficial for stimulating microbial growth prior to ingestion of the mixed ration. Key words: Management, strategy, sequence, dairy cattle


Author(s):  
Nisarg Gohil ◽  
Gargi Bhattacharjee ◽  
Ravi Kalariya ◽  
Vikrant Pandya ◽  
Khushal Khambhati ◽  
...  

2004 ◽  
Vol 71 ◽  
pp. 97-106 ◽  
Author(s):  
Mark Burkitt ◽  
Clare Jones ◽  
Andrew Lawrence ◽  
Peter Wardman

The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. We have been concerned with the role of cytochrome c/H2O2 in the induction of oxidative stress during apoptosis. Our initial studies showed that cytochrome c is a potent catalyst of 2′,7′-dichlorofluorescin oxidation, thereby explaining the increased rate of production of the fluorophore 2′,7′-dichlorofluorescein in apoptotic cells. Although it has been speculated that the oxidizing species may be a ferryl-haem intermediate, no definitive evidence for the formation of such a species has been reported. Alternatively, it is possible that the hydroxyl radical may be generated, as seen in the reaction of certain iron chelates with H2O2. By examining the effects of radical scavengers on 2′,7′-dichlorofluorescin oxidation by cytochrome c/H2O2, together with complementary EPR studies, we have demonstrated that the hydroxyl radical is not generated. Our findings point, instead, to the formation of a peroxidase compound I species, with one oxidizing equivalent present as an oxo-ferryl haem intermediate and the other as the tyrosyl radical identified by Barr and colleagues [Barr, Gunther, Deterding, Tomer and Mason (1996) J. Biol. Chem. 271, 15498-15503]. Studies with spin traps indicated that the oxo-ferryl haem is the active oxidant. These findings provide a physico-chemical basis for the redox changes that occur during apoptosis. Excessive changes (possibly catalysed by cytochrome c) may have implications for the redox regulation of cell death, including the sensitivity of tumour cells to chemotherapeutic agents.


2019 ◽  
Vol 81 (1) ◽  
pp. 34-48
Author(s):  
T.P. Pirog ◽  
◽  
А.Yu. Gershtman ◽  
T.A. Shevchuk ◽  
◽  
...  
Keyword(s):  

2020 ◽  
Vol 11 (5) ◽  
pp. 214
Author(s):  
Sajjad Ali Mangi ◽  
Zubair Ahmed Memon ◽  
Shabir Hussain Khahro ◽  
Rizwan Ali Memon ◽  
Arshad Hussain Memon

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