Analyses of the efficiency of a recombinant vanillyl alcohol oxidase in producing vanillin in the hydrothermal liquefaction aqueous phase-Reference-Cited by-同舟云学术

Analyses of the efficiency of a recombinant vanillyl alcohol oxidase in producing vanillin in the hydrothermal liquefaction aqueous phase

Published:2022-12-20 Issue: Volume: Page:1-7
ISSN:1759-7269
Container-title:Biofuels
language:en
Short-container-title:Biofuels

Author:

Chimbazaza Edson¹^ORCID,van der Sluis Rencia²,Marx Sanette¹

Affiliation:

1. Department of Mineral and Chemical Engineering (Biofuels Research Group), North-West University, Potchefstroom, South Africa

2. Focus Area for Human Metabolomics, North-West University, Potchefstroom, South Africa

Funder

the National Research Foundation of South Africa through the DSI/NRF Research Chair in Biofuels

Publisher

Informa UK Limited

Subject

Waste Management and Disposal,Renewable Energy, Sustainability and the Environment

Link

https://www.tandfonline.com/doi/pdf/10.1080/17597269.2022.2156050

Reference34 articles.

1. The VAO/PCMH flavoprotein family

2. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD

3. Van Rooyen N. 2012. Identification, cloning andHeterologous expression of fungal vanillyl-alcohol oxidases [doctoral dissertation]. Bloemfontein: University of the Free State.

4. Molecular Cloning, Sequencing, and Heterologous Expression of the vaoA Gene from Penicillium simplicissimum CBS 170.90 Encoding Vanillyl-Alcohol Oxidase

5. Highly Efficient Biotransformation of Eugenol to Ferulic Acid and Further Conversion to Vanillin in Recombinant Strains of Escherichia coli

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