Cinnamic acid production using Streptomyces lividans expressing phenylalanine ammonia lyase

Noda, Shinshi; Miyazaki, Takaya; Miyoshi, Takanori; Miyake, Michiru; Okai, Naoko; Tanaka, Tsutomu; Ogino, Chiaki; Kondo, Akihiko

doi:10.1007/s10295-011-0955-2

Cited by 47 publications

(43 citation statements)

References 27 publications

(46 reference statements)

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“…To date, there are a few reports concerning this method. However, although t-CA production has been reported previously, the level of t-CA productivity was very low and still needs to be improved [37,38].…”

Section: Introductionmentioning

confidence: 83%

Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from l-Phenylalanine

Zang

Jiang

Cong

et al. 2015

Appl Biochem Biotechnol

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Phenylalanine ammonia-lyase (PAL) is one of the most extensively studied enzymes with its crucial role in secondary phenylpropanoid metabolism of plants. Recently, its demand has been increased for aromatic chemical production, but its applications in trans-cinnamic acid production were not much explored. In the present study, a putative PAL gene from Zea mays designated as ZmPAL2 was expressed and characterized in Escherichia coli BL21 (DE3). The recombinant ZmPAL2 exhibited a high PAL activity (7.14 U/mg) and a weak tyrosine ammonia-lyase activity. The optimal temperature of ZmPAL2 was 55 °C, and the thermal stability results showed that about 50 % of enzyme activity remained after a treatment at 60 °C for 6 h. The recombinant ZmPAL2 is a good candidate for the production of trans-cinnamic acid. The vitro conversion indicated that the recombinant ZmPAL2 could effectively catalyze the L-phenylalanine to trans-cinnamic acid, and the trans-cinnamic acid concentration can reach up to 5 g/l.

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Section: Introductionmentioning

confidence: 83%

Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from l-Phenylalanine

Zang

Jiang

Cong

et al. 2015

Appl Biochem Biotechnol

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“…Although trans-cinnamate is produced in nature by plants and fungal species (Cochrane et al, 2004;Nijkamp et al, 2005), its current bulk production is via chemical synthesis (Burt, 2004;Miyamoto et al, 2004;Nijkamp et al, 2005;Noda et al, 2011). Biological approaches have also been performed by using phenylalanine ammonia lyase (PAL) enzyme genes from different microorganisms (Nijkamp et al, 2005;Noda et al, 2011). The pal genes encode enzymes that catalyze nonoxidative deamination of phenylalanine to cinnamic acid.…”

Section: Introductionmentioning

confidence: 99%

“…L-Phenylalanine is a precursor for the synthesis of a number of aromatic compounds, including trans-cinnamate and 2-phenylethanol (2-PE) (Achmon et al, 2014;Dueñas-S anchez et al, 2014;Noda et al, 2011). Trans-cinnamic acid is an aromatic compound that is used in the manufacture of flavours (as precursor of methyl, ethyl and benzyl esters for perfumes), dyes and pharmaceuticals, as well as a precursor of the sweetener aspartame.…”

Section: Introductionmentioning

confidence: 99%

Pseudomonas putida as a platform for the synthesis of aromatic compounds

et al. 2016

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Aromatic compounds such as L-phenylalanine, 2-phenylethanol and trans-cinnamate are aromatic compounds of industrial interest. Current trends support replacement of chemical synthesis of these compounds by 'green' alternatives produced in microbial cell factories. The solvent-tolerant Pseudomonas putida DOT-T1E strain was genetically modified to produce up to 1 g l À1 of L-phenylalanine. In order to engineer this strain, we carried out the following stepwise process: (1) we selected random mutants that are resistant to toxic phenylalanine analogues; (2) we then deleted up to five genes belonging to phenylalanine metabolism pathways, which greatly diminished the internal metabolism of phenylalanine; and (3) in these mutants, we overexpressed the pheA fbr gene, which encodes a recombinant variant of PheA that is insensitive to feedback inhibition by phenylalanine. Furthermore, by introducing new genes, we were able to further extend the diversity of compounds produced. Introduction of histidinol phosphate transferase (PP_0967), phenylpyruvate decarboxylase (kdc) and an alcohol dehydrogenase (adh) enabled the strain to produce up to 180 mg l À1 2-phenylethanol. When phenylalanine ammonia lyase (pal) was introduced, the resulting strain produced up to 200 mg l À1 of trans-cinnamate. These results demonstrate that P. putida can serve as a promising microbial cell factory for the production of L-phenylalanine and related compounds.

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“…The membrane was rinsed twice with double distilled H 2 O for 2 min and dried. The chromogenic band was visualized with UVP BioSpectrum 410 (Upland, CA, USA) imaging system (24,25).…”

Section: Electrophoresis and Western Blott Ingmentioning

confidence: 99%

Biochemical Evaluation of Phenylalanine Ammonia Lyase (PAL) from Endemic Cyathobasis fruticulosa (Bunge) Aellen. for the Dietary Treatment of Phenylketonuria (PKU)

Şirin¹,

Aydaş²,

Aslım³

2016

Food Technol. Biotechnol.

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SummaryEnzyme substitution therapy with the phenylalanine ammonia lyase (PAL) is a new approach to the treatment of patients with phenylketonuria (PKU). This enzyme is responsible for the conversion of phenylalanine to trans-cinnamic acid. We assessed the PAL enzyme of the endemic plant Cyathobasis fruticulosa (Bunge) Aellen. for its possible role in the dietary treatment of PKU. The enzyme was found to have a high activity of (64.9±0.1) U/ mg, with the optimum pH, temperature and buff er (Tris-HCl and l-phenylalanine) concentration levels of pH=8.8, 37 °C and 100 mM, respectively. Optimum enzyme activity was achieved at pH=4.0 and 7.5, corresponding to pH levels of gastric and intestinal juice, and NaCl concentration of 200 mM. The purifi cation of the enzyme by 1.87-fold yielded an activity of 98.6 U/mg. PAL activities determined by HPLC analyses before and aft er purification were similar. Two protein bands, one at 70 and the other at 23 kDa, were determined by Western blot analysis of the enzyme. This enzyme is a potential candidate for serial production of dietary food and biotechnological products.

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Cinnamic acid production using Streptomyces lividans expressing phenylalanine ammonia lyase

Cited by 47 publications

References 27 publications

Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from l-Phenylalanine

Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from l-Phenylalanine

Pseudomonas putida as a platform for the synthesis of aromatic compounds

Biochemical Evaluation of Phenylalanine Ammonia Lyase (PAL) from Endemic Cyathobasis fruticulosa (Bunge) Aellen. for the Dietary Treatment of Phenylketonuria (PKU)

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