Biotransformation of eugenol to ferulic acid by a recombinant strain of Ralstonia eutropha H16.

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http://www.wikidata.org/entity/Q39640592

description

2002 nî lūn-bûn

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2002年の論文

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2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

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2002年论文

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2002年论文

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name

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@en

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

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type

Item

label

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@en

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@nl

prefLabel

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@en

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@nl

P1476

Biotransformation of eugenol t ...... ain of Ralstonia eutropha H16.

@en

P2093

Alexander Steinbüchel

http://www.w3.org/2001/XMLSchema#string

Horst Priefert

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Jörg Overhage

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P2860

Protein measurement with the Folin phenol reagent

Purification and characterization of the coniferyl aldehyde dehydrogenase from Pseudomonas sp. Strain HR199 and molecular characterization of the gene

Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate

Biotechnological production of vanillin

Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes

Molecular characterization of the genes pcaG and pcaH, encoding protocatechuate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR199.

Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. Strain HR199.

Identification and molecular characterization of the eugenol hydroxylase genes (ehyA/ehyB) of Pseudomonas sp. strain HR199.

Characterization of the eugenol hydroxylase genes (ehyA/ehyB) from the new eugenol-degrading Pseudomonas sp. strain OPS1.

A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex.

P304

4315-4321

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scholarly article

P356

10.1128/AEM.68.9.4315-4321.2002

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P407

English

P433

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P478

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P577

2002-09-01T00:00:00Z

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P5875

11188709

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P698

12200281

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P932

124108

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