Direct Affinity-Immobilized Phenolic Acid Decarboxylase by a Linker Peptide on Zeolite for Efficient Bioconversion of Ferulic Acid into 4-Vinylguaiacol

2020 ◽  
Vol 8 (39) ◽  
pp. 14732-14742
Author(s):  
Lulu Li ◽  
Liangkun Long ◽  
Shaojun Ding
Keyword(s):  
Ferulic Acid ◽  
Phenolic Acid ◽  
Acid Decarboxylase ◽  
Linker Peptide ◽  
Phenolic Acid Decarboxylase

scholarly journals An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii

AMB Express ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 4 ◽  
Author(s):  
Hui-Kai Huang ◽  
Li-Fan Chen ◽  
Masamichi Tokashiki ◽  
Tadahiro Ozawa ◽  
Toki Taira ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Phenolic Acid ◽  
Candida Guilliermondii ◽  
Acid Decarboxylase ◽  
Endogenous Factor ◽  
Phenolic Acid Decarboxylase

scholarly journals Improving the catalytic characteristics of phenolic acid decarboxylase from Bacillus amyloliquefaciens by the engineering of N-terminus and C-terminus

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Qin Li ◽  
Ying Xia ◽  
Ting Zhao ◽  
Yuanyuan Gong ◽  
Shangling Fang ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Phenolic Acid ◽  
Bacillus Amyloliquefaciens ◽  
Sinapic Acid ◽  
Alkali Resistance ◽  
Acid Decarboxylase ◽  
Coumaric Acid ◽  
C Terminus ◽  
N Terminus ◽  
Phenolic Acid Decarboxylase

Abstract Background 4-vinylphenols produced by phenolic acid degradation catalyzed by phenolic acid decarboxylase can be used in food additives as well as flavor and fragrance industry. Improving the catalytic characters of phenolic acid decarboxylase is of great significance to enhance its practical application. Results A phenolic acid decarboxylase (P-WT) was created from Bacillus amyloliquefaciens ZJH-01. Mutants such as P-C, P-N, P-m1, P-m2, P-Nm1, and P-Nm2 were constructed by site-directed mutagenesis of P-WT. P-C showed better substrate affinities and higher turnover rates than P-WT for p-coumaric acid, ferulic acid, and sinapic acid; however, P-N had reduced affinity toward p-coumaric acid. The extension of the C-terminus increased its acid resistance, whereas the extension of the N-terminus contributed to the alkali resistance and heat resistance. The affinity of P-m1 to four substrates and that of P-m2 to p-coumaric acid and ferulic acid were greatly improved. However, the affinity of P-Nm2 to four phenolic acids was greatly reduced. The residual enzyme activities of P-Nm1 and P-Nm2 considerably improved compared with those of P-m1 and P-m2 after incubation at 50 °C for 60 min. Conclusions The extension of the N-terminus may be more conducive to the combination of the binding cavity with the substrate in an alkaline environment and may make its structure more stable.

scholarly journals Improving the catalytic characteristics of phenolic acid decarboxylase from Bacillus amyloliquefaciens by the engineering of N-terminus and C-terminus

2020 ◽  
Author(s):  
Qin Li ◽  
Ying Xia ◽  
Ting Zhao ◽  
Yuanyuan Gong ◽  
Shangling Fang ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Phenolic Acid ◽  
Food Additives ◽  
Sinapic Acid ◽  
Alkali Resistance ◽  
Acid Decarboxylase ◽  
Coumaric Acid ◽  
C Terminus ◽  
N Terminus ◽  
Phenolic Acid Decarboxylase

Abstract Background: 4-vinylphenols produced by phenolic acid degradation catalyzed by phenolic acid decarboxylase can be used in food additives as well as flavor and fragrance industry. Improving the catalytic characters of phenolic acid decarboxylase is of great significance to enhance its practical application. Results: Mutants such as P-C, P-N, P-m1, P-m2, P-Nm1, and P-Nm2 were constructed by site-directed mutagenesis of P-WT. P-C showed better substrate affinities and higher turnover rates than P-WT for p-coumaric acid, ferulic acid, and sinapic acid; however, P-N had reduced affinity toward p-coumaric acid. The extension of the C-terminus increased its acid resistance, whereas the extension of the N-terminus contributed to the alkali resistance and heat resistance. The affinity of P-m1 to four substrates and that of P-m2 to p-coumaric acid and ferulic acid were greatly improved. However, the affinity of P-Nm2 to four phenolic acids was greatly reduced. The residual enzyme activities of P-Nm1 and P-Nm2 considerably improved compared with those of P-m1 and P-m2 after incubation at 50°C for 60 min.Conclusions: The extension of the N-terminus may be more conducive to the combination of the binding cavity with the substrate in an alkaline environment and may make its structure more stable.

Enhancing Volatile Phenol Concentrations in Wine by Expressing Various Phenolic Acid Decarboxylase Genes inSaccharomyces cerevisiae

2003 ◽  
Vol 51 (17) ◽  
pp. 4909-4915 ◽  
Author(s):  
Annél Smit ◽  
Ricardo R. Cordero Otero ◽  
Marius G. Lambrechts ◽  
Isak S. Pretorius ◽  
Pierre van Rensburg
Keyword(s):  
Phenolic Acid ◽  
Acid Decarboxylase ◽  
Volatile Phenol ◽  
Phenolic Acid Decarboxylase
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