scholarly journals Thermotolerant Extracellular Proteases Produced by Bacillus subtilis Isolated from Local Soil that Representing Industrial Applications

2017 ◽  
Vol 11 (2) ◽  
pp. 733-741 ◽  
Author(s):  
M. E Uddin ◽  
T Ahmad ◽  
MM Ajam ◽  
M Moniruzzaman ◽  
D Mandol ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Industrial Applications ◽  
Extracellular Proteases ◽  
Local Soil

scholarly journals Complete Genome Sequence of Bacillus subtilis Strain WB800N, an Extracellular Protease-Deficient Derivative of Strain 168

2018 ◽  
Vol 7 (18) ◽  
Author(s):  
Haeyoung Jeong ◽  
Da-Eun Jeong ◽  
Seung-Hwan Park ◽  
Seong Joo Kim ◽  
Soo-Keun Choi
Keyword(s):  
Bacillus Subtilis ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Genetically Engineered ◽  
Subtilis Strain ◽  
Secretory Proteins ◽  
Extracellular Proteases ◽  
Content Type ◽  
Protease Deficient

Bacillus subtilis WB800N is a genetically engineered variant of B. subtilis 168, such that all extracellular proteases are disrupted, which enables WB800N to be widely used for the expression of secretory proteins. Here, we report the 4.2-Mb complete genome sequence of WB800N and present all of the disrupted gene structure.

Production and characterisation of thermostable alkaline protease from Bacillus subtilis isolated from LA hot spring, Terengganu

2021 ◽  
Vol 16 (7) ◽  
pp. 84-91
Author(s):  
Maslinda Alias ◽  
Hakim Che Harun Mohammad ◽  
Ashraf Razali Nurul ◽  
Jasnizat Saidin ◽  
Nazaitulshila Rasit ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Hot Spring ◽  
Skim Milk ◽  
Industrial Applications ◽  
Protease Production ◽  
Significant Activity ◽  
Original Activity ◽  
Optimum Ph

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.

scholarly journals Applications of Bacillus subtilis Spores in Biotechnology and Advanced Materials

2020 ◽  
Vol 86 (17) ◽  
Author(s):  
Xiaopei Zhang ◽  
Amal Al-Dossary ◽  
Myer Hussain ◽  
Peter Setlow ◽  
Jiahe Li
Keyword(s):  
Bacillus Subtilis ◽  
Large Scale ◽  
Genetic Manipulation ◽  
Industrial Applications ◽  
Advanced Materials ◽  
Content Type ◽  
Interdisciplinary Approaches ◽  
Food Shortages ◽  
Material Sciences ◽  
Basic Studies

ABSTRACT The bacterium Bacillus subtilis has long been an important subject for basic studies. However, this organism has also had industrial applications due to its easy genetic manipulation, favorable culturing characteristics for large‐scale fermentation, superior capacity for protein secretion, and generally recognized as safe (GRAS) status. In addition, as the metabolically dormant form of B. subtilis, its spores have attracted great interest due to their extreme resistance to many environmental stresses, which makes spores a novel platform for a variety of applications. In this review, we summarize both conventional and emerging applications of B. subtilis spores, with a focus on how their unique characteristics have led to innovative applications in many areas of technology, including generation of stable and recyclable enzymes, synthetic biology, drug delivery, and material sciences. Ultimately, this review hopes to inspire the scientific community to leverage interdisciplinary approaches using spores to address global concerns about food shortages, environmental protection, and health care.

scholarly journals Genes Involved in SkfA Killing Factor Production Protect a Bacillus subtilis Lipase against Proteolysis

2005 ◽  
Vol 71 (4) ◽  
pp. 1899-1908 ◽  
Author(s):  
Helga Westers ◽  
Peter G. Braun ◽  
Lidia Westers ◽  
Haike Antelmann ◽  
Michael Hecker ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Protease Inhibitor ◽  
Bactericidal Activity ◽  
Industrial Applications ◽  
High Potential ◽  
Proteolytic Degradation ◽  
Wild Type ◽  
Factor Production ◽  
Protease Deficient ◽  
High Level

ABSTRACT Small lipases of Bacillus species, such as LipA from Bacillus subtilis, have a high potential for industrial applications. Recent studies showed that deletion of six AT-rich islands from the B. subtilis genome results in reduced amounts of extracellular LipA. Here we demonstrate that the reduced LipA levels are due to the absence of four genes, skfABCD, located in the prophage 1 region. Intact skfABCD genes are required not only for LipA production at wild-type levels by B. subtilis 168 but also under conditions of LipA overproduction. Notably, SkfA has bactericidal activity and, probably, requires the SkfB to SkfD proteins for its production. The present results show that LipA is more prone to proteolytic degradation in the absence of SkfA and that high-level LipA production can be improved significantly by employing multiple protease-deficient B. subtilis strains. In conclusion, our findings imply that SkfA protects LipA, directly or indirectly, against proteolytic degradation. Conceivably, SkfA could act as a modulator in LipA folding or as a protease inhibitor.

scholarly journals Cloning and Expression of theγ-Polyglutamic Acid Synthetase GenepgsBCA inBacillus subtilisWB600

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Biaosheng Lin ◽  
Zhijuan Li ◽  
Huixia Zhang ◽  
Jiangwen Wu ◽  
Maochun Luo
Keyword(s):  
Bacillus Subtilis ◽  
Fermentation Broth ◽  
Recombinant Expression ◽  
Product Yield ◽  
Industrial Applications ◽  
Cloning And Expression ◽  
Polyglutamic Acid ◽  
Recombinant Bacteria ◽  
Expression Product ◽  
Clone And Express

To clone and express theγ-polyglutamic acid (γ-PGA) synthetase genepgsBCA inBacillus subtilis, a pWB980 plasmid was used to construct and transfect the recombinant expression vector pWB980-pgsBCA intoBacillus subtilisWB600.PgsBCAwas expressed under the action of a P43 promoter in the pWB980 plasmid. Our results showed that the recombinant bacteria had the capacity to synthesizeγ-PGA. The expression product was secreted extracellularly into the fermentation broth, with a product yield of 1.74 g/L or higher.γ-PGA samples from the fermentation broth were purified and characterized. Hydrolysates ofγ-PGA presented in single form, constituting simple glutamic acid only, which matched the characteristics of the infrared spectra of theγ-PGA standard, and presented as multimolecular aggregates with a molecular weight within the range of 500–600 kDa. Expressing theγ-PGA synthetase genepgsBCAinB. subtilissystem has potential industrial applications.

scholarly journals Promoter Screening from Bacillus subtilis in Various Conditions Hunting for Synthetic Biology and Industrial Applications

PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0158447 ◽  
Author(s):  
Yafeng Song ◽  
Jonas M. Nikoloff ◽  
Gang Fu ◽  
Jingqi Chen ◽  
Qinggang Li ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Synthetic Biology ◽  
Industrial Applications

scholarly journals Biochemical Characterization of Cellulase From Bacillus subtilis Strain and its Effect on Digestibility and Structural Modifications of Lignocellulose Rich Biomass

2021 ◽  
Vol 9 ◽  
Author(s):  
Waseem Ayoub Malik ◽  
Saleem Javed
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Biomass Conversion ◽  
Industrial Applications ◽  
Partial Purification ◽  
Subtilis Strain ◽  
Complex Nature ◽  
Structural Modifications ◽  
Optimum Activity

Microbial cellulases have become the mainstream biocatalysts due to their complex nature and widespread industrial applications. The present study reports the partial purification and characterization of cellulase from Bacillus subtilis CD001 and its application in biomass saccharification. Out of four different substrates, carboxymethyl cellulose, when amended as fermentation substrate, induced the highest cellulase production from B. subtilis CD001. The optimum activity of CMCase, FPase, and amylase was 2.4 U/ml, 1.5 U/ml, and 1.45 U/ml, respectively. The enzyme was partially purified by (NH4)2SO4 precipitation and sequenced through LC-MS/MS. The cellulase was found to be approximately 55 kDa by SDS-PAGE and capable of hydrolyzing cellulose, as confirmed by zymogram analysis. The enzyme was assigned an accession number AOR98335.1 and displayed 46% sequence homology with 14 peptide-spectrum matches having 12 unique peptide sequences. Characterization of the enzyme revealed it to be an acidothermophilic cellulase, having an optimum activity at pH 5 and a temperature of 60°C. Kinetic analysis of partially purified enzyme showed the Km and Vmax values of 0.996 mM and 1.647 U/ml, respectively. The enzyme activity was accelerated by ZnSO4, MnSO4, and MgSO4, whereas inhibited significantly by EDTA and moderately by β-mercaptoethanol and urea. Further, characterization of the enzyme saccharified sugarcane bagasse, wheat straw, and filter paper by SEM, ATR-FTIR, and XRD revealed efficient hydrolysis and structural modifications of cellulosic materials, indicating the potential industrial application of the B. subtilis CD001 cellulase. The findings demonstrated the potential suitability of cellulase from B. subtilis CD001 for use in current mainstream biomass conversion into fuels and other industrial processes.

Toxicity of zinc oxide and iron oxide engineered nanoparticles to Bacillus subtilis in river water systems

2020 ◽  
Vol 7 (1) ◽  
pp. 172-185 ◽  
Author(s):  
Samuel K. Leareng ◽  
Eunice Ubomba-Jaswa ◽  
Ndeke Musee
Keyword(s):  
Zinc Oxide ◽  
Bacillus Subtilis ◽  
Iron Oxide ◽  
River Water ◽  
Water Systems ◽  
Industrial Applications ◽  
Consumer Products ◽  
Engineered Nanoparticles

Zinc oxide (nZnO) and iron oxide (nFeOx) engineered nanoparticles (ENPs) are widely used in consumer products and industrial applications, and consequently, are continuously being released into the environment.

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