scholarly journals Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis.

1994 ◽  
Vol 176 (18) ◽  
pp. 5673-5680 ◽  
Author(s):  
M Ogura ◽  
M Kawata-Mukai ◽  
M Itaya ◽  
K Takio ◽  
T Tanaka
1984 ◽  
Vol 160 (1) ◽  
pp. 438-441 ◽  
Author(s):  
J H Hageman ◽  
G W Shankweiler ◽  
P R Wall ◽  
K Franich ◽  
G W McCowan ◽  
...  

2008 ◽  
Vol 4 (1) ◽  
pp. 184 ◽  
Author(s):  
Jan‐Willem Veening ◽  
Oleg A Igoshin ◽  
Robyn T Eijlander ◽  
Reindert Nijland ◽  
Leendert W Hamoen ◽  
...  

1988 ◽  
Vol 28 (4-5) ◽  
pp. 404-408 ◽  
Author(s):  
Manoj M. Kole ◽  
Indira Draper ◽  
Donald F. Gerson

Author(s):  
Cheong, J.Y. ◽  
Mustafa, M. ◽  
Abd. Aziz, N.A. ◽  
Go, R. ◽  
Ahmad Adli, A.

2009 ◽  
Vol 26 (6) ◽  
pp. 1047-1052 ◽  
Author(s):  
Inés Infante ◽  
Maria A. Morel ◽  
Martha C. Ubalde ◽  
Cecilia Martínez-Rosales ◽  
Silvia Belvisi ◽  
...  

2021 ◽  
Vol 16 (7) ◽  
pp. 84-91
Author(s):  
Maslinda Alias ◽  
Hakim Che Harun Mohammad ◽  
Ashraf Razali Nurul ◽  
Jasnizat Saidin ◽  
Nazaitulshila Rasit ◽  
...  

This research aims to produce thermostable alkaline protease from Bacillus subtilis isolated from La Hot Spring, Terengganu, Malaysia. The study was also conducted to determine the optimum conditions for protease production and stability by considering several parameters including pH, temperature and salt concentration. All seven bacteria were screened on skim milk agar overnight at 37 °C. Three strains with the highest proteolytic activity were identified in protease specific medium. The thermostable alkaline protease had an optimum temperature of 60 °C which achieved 85.73, 82.90 and 83.05 U/mL of protease activity for the three strains respectively. Furthermore, the strains exhibited significant activity of more than 90% from their original activity. Meanwhile, the optimum pH for protease production was pH 9 with the protease activity of 76.76, 79.71 and 88.39 U/mL for TB4, TB6 and TB9 strains, respectively. Proteases were found stable at pH 9 where the loss did not exceed 30% of its original activity. Collectively, all of the data emphasised that proteases from B. subtilis were alkaline thermostable proteases in accordance with a recent report. The finding highlights the viability of the proteases for biotechnological and industrial applications.


2011 ◽  
Vol 17 (2) ◽  
pp. 215-222 ◽  
Author(s):  
P. Rathakrishnan ◽  
P. Nagarajan ◽  
Rajesh Kannan

Optimization of the growth condition for maximum growth rate and protease production was carried out using Bacillus subtilis. The optimization of protease production using agro industrial waste product such as cassava waste as substrate was performed with statistical methodology based on experimental designs. The screening of twelve nutrients for their influence on protease production was achieved using a Plackett-Burman design. MgSO4.7H2O, casein and glucose were selected based on their positive influence on protease production. The selected components were optimized using Response Surface Methodology (RSM). The optimum conditions are (% w/w): MgsO4.7H2O- 0.14, casein- 1.4 and glucose- 2.64. These conditions were validated experimentally which revealed an enhanced protease yield of 202.048 U/gds.


Molecules ◽  
2019 ◽  
Vol 24 (3) ◽  
pp. 592 ◽  
Author(s):  
Xian Zhang ◽  
Zhaoyang Xu ◽  
Song Liu ◽  
Kai Qian ◽  
Meijuan Xu ◽  
...  

In this study, the Micrococcus luteus K-3 glutaminase was successfully over-expressed in the GRAS (Generally Recognized as Safe) Bacillus subtilis strain 168 by integration of the Mglu gene in the 16S rDNA locus. This was done in order to screen a strain producing high levels of recombinant glutaminase from the selected candidates. The transcription of the glutaminase genes in the B. subtilis 168 chromosome and the expression of glutaminase protein was further assessed by qPCR, SDS-PAGE analysis and an enzyme activity assay. To further increase the production of glutaminase, the nprB and nprE genes, which encode specific proteases, were disrupted by integration of the Mglu gene. After continuous cell culturing without the addition of antibiotics, the integrated recombinant strains showed excellent genetic stability, demonstrating favorable industrialization potential. After the fermentation temperature was optimized, a 5-L bioreactor was used for fed-batch fermentation of the recombinant glutaminase producing strain at 24 °C, and the highest enzyme activity achieved was approximately 357.6 U/mL.


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