Overexpression of a serine alkaline protease gene in Bacillus licheniformis and its impact on the metabolic reaction network

2003 ◽  
Vol 32 (6) ◽  
pp. 706-720 ◽  
Author(s):  
Pınar Çalik ◽  
Gregory C. Tomlin ◽  
Stephen G. Oliver ◽  
Tunçer H. Özdamar
2015 ◽  
Vol 3 (2) ◽  
pp. 347-351
Author(s):  
Rajnish Prakash Singh ◽  
Prabhat Nath Jha

Halophilic microorganisms are recognized as potential source of secondary metabolites including enzymes and drugs with wide agricultural and industrial applications. In the present study protease producing halotolerant bacterium Bacillus licheniformis HSW-16 was isolated from hypersaline Sambhar lake, Rajasthan India. Protease production was performed by using azocasein as substrate. Confirmation of protease production was also done by amplification of alkaline protease gene and sequencing. The various nutritional factors such as carbon and nitrogen source and other physiological parameters like pH, temperature, incubation time and agitation speed were optimized for optimum protease production. The enzyme was active in pH range 7-10, temperature 25 °C-40 °C and salt concentration of 1.5M. The characteristics demonstrated by this isolate showed that it could be used as a potential source of enzyme.Int J Appl Sci Biotechnol, Vol 3(2): 347-351 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12757 


2014 ◽  
Vol 886 ◽  
pp. 349-354
Author(s):  
Qing Shan Mo ◽  
Yao Tian ◽  
Hui Tu Zhang ◽  
Ling Jun Bu ◽  
Fu Ping Lu

Bacillus alcalophilusisolated was used for the production of alkaline protease. The enzyme encoded by alkaline protease gene (apr4) gene. To further improve the production of the strain for industrial requirement, a genetic manipulation system forBacillus alcalophiluswas developed. Additional copies of theapr4 gene were transferred into the strainBacillus alcalophilusand integrated into the 16S rDNA sites, yielding a series of recombinant strains. One of these recombinant strains, designated K23, exhibited superior properties for production of alkaline protease. the protease activity of K23 achieved by (6.19 ± 0.34) × 104U/ml, which is approximately 111.3% higher than that of the wild-type ones for 50-h fermentation. In addition, the new strain was genetically stable for more than 100 generations. These superior characteristics make it to be more suitable than the wild-type strain for alkaline protease production.


1991 ◽  
Vol 57 (4) ◽  
pp. 901-909 ◽  
Author(s):  
J C van der Laan ◽  
G Gerritse ◽  
L J Mulleners ◽  
R A van der Hoek ◽  
W J Quax

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