scholarly journals Isolation and Optimal Fermentation Condition of the Bacillus subtilis Subsp. natto Strain WTC016 for Nattokinase Production

Fermentation ◽  
2019 ◽  
Vol 5 (4) ◽  
pp. 92 ◽  
Author(s):  
Shouyong Ju ◽  
Zhilin Cao ◽  
Christina Wong ◽  
Yangyang Liu ◽  
Mohamed F. Foda ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Bacillus Subtilis ◽  
Fibrinolytic Activity ◽  
Inoculum Size ◽  
Orthogonal Test ◽  
Fermentation Condition ◽  
Fermentation Conditions ◽  
Optimal Tests ◽  
Physiological Tests ◽  
Subtilis Subsp

Nattokinase is a serine protease in the subtilisin family which is produced by Bacillus subtilis subsp. natto and exhibits vigorous fibrinolytic activity that has been suggested to be able to prevent and treat thromboembolic diseases. In this study, WTC016, a spore-forming and rod-shaped bacterium with fibrinolytic activity was successfully isolated from soil, which was identified as Bacillus subtilis subsp. natto based on morphological and physiological tests, and phylogenetic analysis of 16S rRNA and gyrA. According to the growth curve of WTC016, the nattokinase production reached the highest amount in the stationary phase. To optimize the liquid fermentation condition for nattokinase yield of WTC016, further optimal tests of four factors, including the temperature, pH, inoculum size, and loading volume, followed by orthogonal test of all these factors, was performed. The optimal fermentation conditions were determined as 30 °C, 7.0 pH, 2% inoculum size, and 60 mL of loading volume in 250 mL conical flask, which indicates the highest nattokinase production of 3284 ± 58 IU/mL while fermented for 26 h. This work laid the foundation for producing nattokinase using Bacillus subtilis subsp. natto WTC016.

Study on Combination and Bioremediation of Chlorimuron-Ethyl-Degrading Strains

2011 ◽  
Vol 340 ◽  
pp. 215-221 ◽  
Author(s):  
Chun Hong Xu ◽  
Chun Yan Li ◽  
Ming Hua Xiong ◽  
Jun Bo Pan ◽  
Xue Song Li ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Stenotrophomonas Maltophilia ◽  
Removal Rate ◽  
Inoculum Size ◽  
Orthogonal Test ◽  
Cucumber Seedling ◽  
Rhodotorula Mucilaginosa ◽  
Culture Experiment ◽  
Chlorimuron Ethyl ◽  
Pot Culture

The degradation capacity of the four chlorimuron-ethyl-degrading strains, D310-1, LCY-2, LCY-3 and LCY-4, which identified asRhodococcussp.,Stenotrophomonas maltophilia sp,Bacillus subtilis sp., andRhodotorula mucilaginosasp., respectively, combined in different ways was examined in this study. Then the optimal degradation conditions and mitigation phytotoxicity of chlorimuron-ethyl on sensitive crop were investigated by both orthogonal test and pot culture experiment. The experimental results showed that the combination of four strains was adopted, and the removal rate of chlorimuron-ethyl reached the maximum of 90% in 30 days. Then the optimal degradation conditions were inoculum size 2.5%, temperature 28°C, pH 7.0 and the soil moisture 35%, and the mixed strains could eradicate 92.57% of chlorimuron-ethyl within 30 days. Furthermore pot culture experiment indicated that inoculation of mixed strains could also mitigate the phytotoxic effects of chlorimuron-ethyl on the growth of cucumber seedling.

Optimization of Process Parameters for Production of Pectinase using Bacillus Subtilis MF447840.1

2019 ◽  
Vol 13 (1) ◽  
pp. 69-73 ◽  
Author(s):  
Ram Balak Mahto ◽  
Mukesh Yadav ◽  
Soumya Sasmal ◽  
Biswnath Bhunia
Keyword(s):  
Bacillus Subtilis ◽  
Process Parameters ◽  
Volume Ratio ◽  
Optimum Process ◽  
Agitation Rate ◽  
Fermentation Condition ◽  
Optimization Of Process Parameters ◽  
Food And Beverage ◽  
Pectinase Production ◽  
Sterile Product

Background: Pectinase enzyme has immense industrial prospects in the food and beverage industries. </P><P> Objective: In our investigation, we find out the optimum process parameters suitable for better pectinase generation by Bacillus subtilis MF447840.1 using submerged fermentation. </P><P> Method: 2% (OD600 nm = 0.2) of pure Bacillus subtilis MF447840.1 bacterial culture was inoculated in sterile product production media. The production media components used for this study were 1 g/l of pectin, 2 g/l of (NH4)2SO4, 1 g/l of NaCl, 0.25 g/l of K2HPO4, 0.25 g/l of KH2PO4 and 1 g/l of MgSO4 for pectinase generation. We reviewed all recent patents on pectinase production and utilization. The various process parameters were observed by changing one variable time method. </P><P> Results: The optimum fermentation condition of different parameters was noticed to be 5% inoculums, 25% volume ratio, temperature (37°C), pH (7.4) and agitation rate (120 rpm) following 4 days incubation. </P><P> Conclusion: Maximum pectinase generation was noticed as 345 ± 12.35 U following 4 days incubation.

Optimization of Fermentation Conditions for Blue Pigment Production by Bacterial Strain T2013

2014 ◽  
Vol 1073-1076 ◽  
pp. 286-291
Author(s):  
Yong Zuo ◽  
Peng Jiang ◽  
Xiao Long Wang ◽  
Bin Fu ◽  
Xiao Long Yang ◽  
...  
Keyword(s):  
Bacterial Strain ◽  
Orthogonal Test ◽  
Blue Pigment ◽  
Liquid Volume ◽  
Initial Value ◽  
Fermentation Time ◽  
Fermentation Conditions ◽  
Inoculum Volume ◽  
Optimization Of Fermentation ◽  
Single Factor Experiment

The fermentation conditions of Bacterial Strain T2013 were studied. The fermentation conditions of T2013 were investigated with single-factor experiment. In addition to, the fermentation conditions were optimized through the orthogonal test. The results showed the highest production of blue pigment was obtained on condition that fermentation time was 2d, the liquid volume was 50ml in the 250ml shake-flask, the inoculum volume was 2%, the initial value of pH was 7.6, fermentation temperature was 37°C and the speed was 150r/min.The fermentation conditions of Bacterial Strain T2013 were preliminarily determined,whichprovides a theoretical basis for the industrial production of blue pigment.

scholarly journals Phylogenetic analysis and secondary structure of the Bacillus subtilis bacteriophage RNA required for DNA packaging.

1990 ◽  
Vol 265 (36) ◽  
pp. 22365-22370
Author(s):  
S Bailey ◽  
J Wichitwechkarn ◽  
D Johnson ◽  
B E Reilly ◽  
D L Anderson ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Bacillus Subtilis ◽  
Secondary Structure ◽  
Dna Packaging ◽  
Subtilis Bacteriophage

scholarly journals Complete Genome Sequence of Bacillus subtilis subsp. subtilis Strain ∆6

2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Daniel R. Reuß ◽  
Andrea Thürmer ◽  
Rolf Daniel ◽  
Wim J. Quax ◽  
Jörg Stülke
Keyword(s):  
Bacillus Subtilis ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Full Genome Sequence ◽  
Subtilis Strain ◽  
Full Genome ◽  
Biotechnological Applications ◽  
A Genome ◽  
Subtilis Subsp

Bacillus subtilis ∆6 is a genome-reduced strain that was cured from six prophages and AT-rich islands. This strain is of great interest for biotechnological applications. Here, we announce the full-genome sequence of this strain. Interestingly, the conjugative element ICE Bs 1 has most likely undergone self-excision in B. subtilis ∆6.

Anionic polymers of the cell wall of Bacillus subtilis subsp. subtilis VKM B-501T

2009 ◽  
Vol 74 (5) ◽  
pp. 543-548 ◽  
Author(s):  
A. S. Shashkov ◽  
N. V. Potekhina ◽  
S. N. Senchenkova ◽  
E. B. Kudryashova
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Anionic Polymers ◽  
Subtilis Subsp

The Bacillus subtilis ywkA gene encodes a malic enzyme and its transcription is activated by the YufL/YufM two-component system in response to malate

Microbiology ◽  
2003 ◽  
Vol 149 (9) ◽  
pp. 2331-2343 ◽  
Author(s):  
Thierry Doan ◽  
Pascale Servant ◽  
Shigeo Tojo ◽  
Hirotake Yamaguchi ◽  
Guillaume Lerondel ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Malic Enzyme ◽  
Northern Analysis ◽  
Two Component System ◽  
Extracellular Medium ◽  
Component System ◽  
Two Component ◽  
Transcriptome Comparison ◽  
Physiological Tests

A transcriptome comparison of a wild-type Bacillus subtilis strain growing under glycolytic or gluconeogenic conditions was performed. In particular, it revealed that the ywkA gene, one of the four paralogues putatively encoding a malic enzyme, was more transcribed during gluconeogenesis. Using a lacZ reporter fusion to the ywkA promoter, it was shown that ywkA was specifically induced by external malate and not subject to glucose catabolite repression. Northern analysis confirmed this expression pattern and demonstrated that ywkA is cotranscribed with the downstream ywkB gene. The ywkA gene product was purified and biochemical studies demonstrated its malic enzyme activity, which was 10-fold higher with NAD than with NADP (k cat/K m 102 and 10 s−1 mM−1, respectively). However, physiological tests with single and multiple mutant strains affected in ywkA and/or in ywkA paralogues showed that ywkA does not contribute to efficient utilization of malate for growth. Transposon mutagenesis allowed the identification of the uncharacterized YufL/YufM two-component system as being responsible for the control of ywkA expression. Genetic analysis and in vitro studies with purified YufM protein showed that YufM binds just upstream of ywkA promoter and activates ywkA transcription in response to the presence of malate in the extracellular medium, transmitted by YufL. ywkA and yufL/yufM could thus be renamed maeA for malic enzyme and malK/malR for malate kinase sensor/malate response regulator, respectively.

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