Cloning, Expression, and Identification of a Novel Extracellular Cold-Adapted Alkaline Protease Gene of the Marine Bacterium Strain YS-80-122

2010 ◽  
Vol 162 (5) ◽  
pp. 1497-1505 ◽  
Author(s):  
Fang Wang ◽  
Jianhua Hao ◽  
Chengye Yang ◽  
Mi Sun
Keyword(s):  
Alkaline Protease ◽  
Marine Bacterium ◽  
Protease Gene ◽  
Cold Adapted ◽  
Bacterium Strain ◽  
Alkaline Protease Gene

Using 16S rDNA as Target Site for Homologous Recombination to Improve the Alkaline Protease Production of Bacillus alcalophilus

2014 ◽  
Vol 886 ◽  
pp. 349-354
Author(s):  
Qing Shan Mo ◽  
Yao Tian ◽  
Hui Tu Zhang ◽  
Ling Jun Bu ◽  
Fu Ping Lu
Keyword(s):  
16S Rdna ◽  
Alkaline Protease ◽  
Genetic Manipulation ◽  
Protease Production ◽  
Protease Gene ◽  
Wild Type ◽  
Recombinant Strains ◽  
Manipulation System ◽  
Rdna Sites ◽  
Alkaline Protease Gene

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.

scholarly journals Cloning, characterization, and multiple chromosomal integration of a Bacillus alkaline protease gene.

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
Keyword(s):  
Alkaline Protease ◽  
Protease Gene ◽  
Chromosomal Integration ◽  
Alkaline Protease Gene

Random Mutation of Alkaline Protease Gene in Bacillus pumilus*

2010 ◽  
Vol 16 (1) ◽  
pp. 96-99
Author(s):  
Jin YANG ◽  
Hong FENG ◽  
Mingyuan WAN ◽  
Huike JIAO ◽  
Xiaolu ZHANG ◽  
...  
Keyword(s):  
Alkaline Protease ◽  
Bacillus Pumilus ◽  
Protease Gene ◽  
Random Mutation ◽  
Alkaline Protease Gene

scholarly journals Involvement of Stringent Factor RelA in Expression of the Alkaline Protease Gene aprE in Bacillus subtilis

2001 ◽  
Vol 183 (15) ◽  
pp. 4648-4651 ◽  
Author(s):  
Michihiro Hata ◽  
Mitsuo Ogura ◽  
Teruo Tanaka
Keyword(s):  
Bacillus Subtilis ◽  
Alkaline Protease ◽  
Double Mutant ◽  
Regulatory System ◽  
Protease Gene ◽  
Wild Type ◽  
Double Mutation ◽  
Two Component ◽  
In The Wild ◽  
Alkaline Protease Gene

ABSTRACT Expression of Bacillus subtilis aprE, encoding an extracellular alkaline protease, is positively regulated by phosphorylated DegU, the regulator of a two-component regulatory system, DegS-DegU. We found that the expression of anaprE′-′lacZ fusion was greatly reduced in a disruption mutant with a mutation of relA, which encodes the stringent factor RelA. The level of DegU in the relA mutant was similar to that in the wild-type cell. A relA degU double mutation did not result in a further decrease of theaprE′-′lacZ level found in a degU single mutant. The expression of the aprE′-′lacZ fusion in therelA mutant was stimulated by multicopy degR or the degU32(Hy) and degS200(Hy) mutations that cause the stabilization of phosphorylated DegU. Furthermore, the expression of sacB′-′lacZ, which is also dependent on phosphorylated DegU, was stimulated by the relA mutation, and this stimulation was not seen in the relA degU double mutant. These results show that RelA (or its product guanosine-3′,5′-bisdiphosphate [pp Gpp]) does not affect the phosphorylation of DegU and suggest that it participates in the expression of aprE and sacB through the regulation of DegU-dependent transcription.

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