Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues

0534585 - MBÚ 2021 RIV CH eng J - Journal Article
Martínková, Ludmila - Příhodová, Romana - Kulik, Natalia - Pelantová, Helena - Křístková, Barbora - Petrásková, Lucie - Biedermann, David
Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues.
Catalysts. Roč. 10, č. 9 (2020), č. článku 1077. E-ISSN 2073-4344
R&D Projects: GA MŠMT(CZ) LTC18080; GA MŠMT(CZ) LTC19037
Institutional support: RVO:61388971
Keywords : biocatalyzed reaction * tyrosinase * alkylphenol
OECD category: Bioprocessing technologies (industrial processes relying on biological agents to drive the process) biocatalysis, fermentation
Impact factor: 4.146, year: 2020
Method of publishing: Open access
https://www.mdpi.com/2073-4344/10/9/1077

Catechols are antioxidants and radical scavengers with a broad medical potential. 4-Methylcatechol (1b) and 4-ethylcatechol (2b) (occurring in some traditional fermented and smoked foods) activate the cell defense against oxidative stress. We examined the biocatalyzed reactions towards 4-n-alkylcatechols with different side chains length, which is a factor important for the biological activities of catechols. 4-n-Alkylcatechols with methyl through heptyl side chains (1b-7b) were obtained in one pot by (i) oxidation of phenols 1a-7a with tyrosinase from Agaricus bisporus followed by (ii) reduction of ortho-quinones (intermediates) with L-ascorbic acid sodium salt. The conversions decreased with increasing side chain length. The preparative reactions were carried out with substrates 1a-5a. The isolated yields of the purified products decreased from 59% in 2b to 10% in 5b in correlation with logP of the substrates. Homology modeling indicated that the affinities of two tyrosinase isoforms (PPO3 and PPO4) to the substrates with side chains longer than C2 decreased with increasing side chain length. This was probably due to steric limitations and to missing interactions of the extended side chains in the active sites. We envisage using the model to predict further substrates of tyrosinase and testing the products, catechols, for radical-scavenging and biological activities.
Permanent Link: http://hdl.handle.net/11104/0312756