TY - JOUR
T1 - Vanillin dehydrogenase (VhdA) from Aspergillus niger is active on depolymerized lignin
AU - Lubbers, Ronnie J.M.
AU - Martínez-Reyes, Natalia
AU - Rhanama, Nooshin
AU - Nair, Rakesh
AU - Prieto, Isabel
AU - Ihalainen, Petri
AU - Heikkilä, Matti
AU - de Vries, Ronald P.
N1 - Publisher Copyright:
© 2024 The Authors
PY - 2024/12
Y1 - 2024/12
N2 - Vanillin dehydrogenases are important enzymes involved in the conversion of lignin-derived aromatic aldehydes such as vanillin and p-hydroxybenzaldehyde into its acid form. In a previous study we identified the first fungal vanillin dehydrogenase (VdhA) from the filamentous fungus Aspergillus niger. In this study we heterologous produced VdhA in a bioreactor to obtain sufficient enzyme for a more details analysis of its biochemical properties. This demonstrated that VdhA has a high optimal temperature (50 °C), neutral optimum pH and a broad substrate specificity for aromatic aldehydes. Deletion of vdhA in A. niger resulted in reduced growth on several aromatic aldehydes, largely collating with the in vitro substrate specificity of the enzyme. In addition, we demonstrated that VdhA can convert multiple aromatic aldehydes present in depolymerized lignin, indicating that VdhA can be applied in industrial conversion of lignin fractions to either simplify the composition of the fraction or to reduce the aldehydes that can undergo undesired repolymerization reactions within the mixture.
AB - Vanillin dehydrogenases are important enzymes involved in the conversion of lignin-derived aromatic aldehydes such as vanillin and p-hydroxybenzaldehyde into its acid form. In a previous study we identified the first fungal vanillin dehydrogenase (VdhA) from the filamentous fungus Aspergillus niger. In this study we heterologous produced VdhA in a bioreactor to obtain sufficient enzyme for a more details analysis of its biochemical properties. This demonstrated that VdhA has a high optimal temperature (50 °C), neutral optimum pH and a broad substrate specificity for aromatic aldehydes. Deletion of vdhA in A. niger resulted in reduced growth on several aromatic aldehydes, largely collating with the in vitro substrate specificity of the enzyme. In addition, we demonstrated that VdhA can convert multiple aromatic aldehydes present in depolymerized lignin, indicating that VdhA can be applied in industrial conversion of lignin fractions to either simplify the composition of the fraction or to reduce the aldehydes that can undergo undesired repolymerization reactions within the mixture.
KW - Aspergillus niger
KW - Lignin conversion
KW - Substrate specificity
KW - Vanillin conversion
KW - Vanillin dehydrogenase
UR - http://www.scopus.com/inward/record.url?scp=85207366737&partnerID=8YFLogxK
U2 - 10.1016/j.scenv.2024.100179
DO - 10.1016/j.scenv.2024.100179
M3 - Article
AN - SCOPUS:85207366737
SN - 2949-8392
VL - 8
JO - Sustainable Chemistry for the Environment
JF - Sustainable Chemistry for the Environment
M1 - 100179
ER -