An organic solvent-tolerant phenolic acid decarboxylase from Bacillus licheniformis for the efficient bioconversion of hydroxycinnamic acids to vinyl phenol derivatives

2014 ◽  
Vol 99 (12) ◽  
pp. 5071-5081 ◽  
Author(s):  
Hongfei Hu ◽  
Lulu Li ◽  
Shaojun Ding
Keyword(s):  
Organic Solvent ◽  
Bacillus Licheniformis ◽  
Phenolic Acid ◽  
Hydroxycinnamic Acids ◽  
Acid Decarboxylase ◽  
Phenol Derivatives ◽  
Organic Solvent Tolerant ◽  
Phenolic Acid Decarboxylase ◽  
Solvent Tolerant ◽  
Vinyl Phenol

An organic solvent-, detergent-, and thermostable alkaline protease from the mesophilic, organic solvent-tolerant Bacillus licheniformis 3C5

Microbiology ◽  
2010 ◽  
Vol 79 (5) ◽  
pp. 620-629 ◽  
Author(s):  
W. Rachadech ◽  
A. Navacharoen ◽  
W. Ruangsit ◽  
T. Pongtharangkul ◽  
A. S. Vangnai
Keyword(s):  
Organic Solvent ◽  
Bacillus Licheniformis ◽  
Alkaline Protease ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

scholarly journals Functional Autodisplay of Phenolic Acid Decarboxylase using a GDSL Autotransporter on Escherichia coli for Efficient Catalysis of 4-Hydroxycinnamic Acids to Vinylphenol Derivatives

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 634 ◽  
Author(s):  
Lulu Li ◽  
Xiang Wu ◽  
Liangkun Long ◽  
Shaojun Ding
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Signal Peptide ◽  
Phenolic Acid ◽  
Residual Activity ◽  
Hydroxycinnamic Acids ◽  
Acid Decarboxylase ◽  
Buffer System ◽  
E Coli ◽  
Phenolic Acid Decarboxylase

Bioproduction of vinylphenol derivatives, such as 4-vinylguaiacol (4-VG) and 4-vinylphenol (4-VP), from 4-hydroxycinnamic acids, such as ferulic acid (FA) and p-coumaric acid (pCA), employing whole cells expressing phenolic acid decarboxylases (PAD) as a biocatalyst has attracted much attention in recent years. However, the accumulation of 4-VG or 4-VP in the cell may cause high cytotoxicity to Escherichia coli (E. coli) and consequently cell death during the process. In this study, we firstly report the functional display of a phenolic acid decarboxylase (BLPAD) from Bacillus licheniformis using a GDSL autotransporter from Pseudomonas putida on the cell surface of E. coli. Expression and localization of BLPAD on E. coli were verified by SDS-PAGE and protease accessibility. The PelB signal peptide is more effective in guiding the translocation of BLPAD on the cell surface than the native signal peptide of GDSL, and the cell surface displaying BLPAD activity reached 19.72 U/OD600. The cell surface displaying BLPAD showed good reusability and retained 63% of residual activity after 7 cycles of repeated use. In contrast, the residual activity of the intracellular expressing cells was approximately 11% after 3 cycles of reuse. The molar bioconversion yields of 72.6% and 80.4% were achieved at the concentration of 300 mM of FA and pCA in a biphasic toluene/Na2HPO4–citric acid buffer system, respectively. Its good reusability and efficient catalysis suggested that the cell surface displaying BLPAD can be used as a whole-cell biocatalyst for efficient production of 4-VG and 4-VP.

An organic-solvent-tolerant esterase from thermophilic Bacillus licheniformis S-86

2009 ◽  
Vol 100 (2) ◽  
pp. 896-902 ◽  
Author(s):  
Sebastián Torres ◽  
M. Alejandra Martínez ◽  
Ashok Pandey ◽  
Guillermo R. Castro
Keyword(s):  
Organic Solvent ◽  
Bacillus Licheniformis ◽  
Thermophilic Bacillus ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant
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