Enhanced production of glutaminase free L-asparaginase II by Bacillus subtilis WB800N through media optimization

2017 ◽  
Vol 34 (11) ◽  
pp. 2901-2915 ◽  
Author(s):  
Chityala Sushma ◽  
Ashish Prabhu Anand ◽  
Venkata Dasu Veeranki
Keyword(s):  
Bacillus Subtilis ◽  
Media Optimization ◽  
Enhanced Production ◽  
Bacillus Subtilis Wb800n

Deciphering characteristics of the designer cellulosome from Bacillus subtilis WB800N via enzymatic analysis

2017 ◽  
Vol 117 ◽  
pp. 147-155 ◽  
Author(s):  
Chia-Chi Lin ◽  
Cally Joe San Yap ◽  
Shu-Chen Kan ◽  
Nai-Chi Hsueh ◽  
Liang-Yu Yang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Analysis ◽  
Bacillus Subtilis Wb800n ◽  
Designer Cellulosome

scholarly journals Comparative Evaluation of Agroindustrial Byproducts for the Production of Alkaline Protease by Wild and Mutant Strains ofBacillus subtilisin Submerged and Solid State Fermentation

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Hamid Mukhtar ◽  
Ikramul Haq
Keyword(s):  
Bacillus Subtilis ◽  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Soybean Meal ◽  
Alkaline Protease ◽  
Enzyme Production ◽  
Enhanced Production ◽  
Industrial Byproducts ◽  
Agroindustrial Byproducts

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.

scholarly journals Enhanced Secretory Production of a Single-Chain Antibody Fragment from Bacillus subtilis by Coproduction of Molecular Chaperones

1998 ◽  
Vol 180 (11) ◽  
pp. 2830-2835 ◽  
Author(s):  
Sau-Ching Wu ◽  
Ruiqiong Ye ◽  
Xu-Chu Wu ◽  
Shi-Chung Ng ◽  
Sui-Lam Wong
Keyword(s):  
Bacillus Subtilis ◽  
Molecular Chaperones ◽  
Total Yield ◽  
Antibody Fragment ◽  
Biologically Active ◽  
Production Yield ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Enhanced Production ◽  
Secretory Production

ABSTRACT Formation of inclusion bodies is a major limiting factor for secretory production of an antidigoxin single-chain antibody (SCA) fragment from Bacillus subtilis. To address this problem, three new strains with enhanced production of molecular chaperones were constructed. WB600BHM constitutively produces the major intracellular molecular chaperones in an appropriate ratio without any heat shock treatment. This strain reduced the formation of insoluble SCA by 45% and increased the secretory production yield by 60%. The second strain, WB600B[pEPP], overproduces an extracytoplasmic molecular chaperone, PrsA. An increase in the total yield of SCA was observed. The third strain, WB600BHM[pEPP], coproduces both intracellular and extracytoplasmic molecular chaperones. This led to a further reduction in inclusion body formation and a 2.5-fold increase in the secretory production yield. SCA fragments secreted by this strain were biologically active and showed affinity to digoxin comparable to the affinity of those secreted by strains without overproduction of molecular chaperones. Interestingly, accumulation of a pool of periplasmic SCA was observed in the PrsA-overproducing strains. This pool is suggested to represent the secreted folding intermediates in the process of achieving their final configuration.

Sign in / Sign up

Export Citation Format

Share Document