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Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues
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SYSNO ASEP 0534585 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues Author(s) Martínková, Ludmila (MBU-M) RID, ORCID
Příhodová, Romana (MBU-M)
Kulik, Natalia (MBU-M) ORCID
Pelantová, Helena (MBU-M) ORCID, RID
Křístková, Barbora (MBU-M)
Petrásková, Lucie (MBU-M) ORCID
Biedermann, David (MBU-M) RID, ORCIDArticle number 1077 Source Title Catalysts. - : MDPI
Roč. 10, č. 9 (2020)Number of pages 14 s. Language eng - English Country CH - Switzerland Keywords biocatalyzed reaction ; tyrosinase ; alkylphenol Subject RIV EI - Biotechnology ; Bionics OECD category Bioprocessing technologies (industrial processes relying on biological agents to drive the process) biocatalysis, fermentation R&D Projects LTC18080 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC19037 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000581343700001 EID SCOPUS 85091110004 DOI 10.3390/catal10091077 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2021 Electronic address https://www.mdpi.com/2073-4344/10/9/1077
Number of the records: 1