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Screening of commercial enzymes for transfructosylation of tyrosol: Effect of process conditions and reaction network.

08:00 EDT 30th March 2019 | BioPortfolio

Summary of "Screening of commercial enzymes for transfructosylation of tyrosol: Effect of process conditions and reaction network."

Enzymatic fructosylation of organic acceptors other than saccharides brings new possibilities to synthesize molecules that do not exist in nature. The introduction of fructosyl moiety may lead to glycosides possessing enhanced physico-chemical and bioactive properties which could be useful in the pharmaceutical and cosmetic industry. In this work, the regioselective synthesis of tyrosol β-D-fructofuranoside catalyzed by β-fructofuranosidase is investigated. In the first step, thirty-two commercial enzyme preparations were screened for fructoside-hydrolysing activity. The most active preparations were subsequently examined for fructofuranosyl transfer from sucrose to tyrosol. The best candidate, Novozym 188, was chosen to study the effect of reaction conditions on the product formation in a batch reactor. The effects of substrates concentrations, temperature, pH, time, and enzyme dosage on the concentration of tyrosol β-D-fructofuranoside produced were studied using the design of experiments methodology. The maximal product concentration of 3.8 g/L was achieved for the sucrose concentration of 1.5 M, tyrosol concentration of 29 g/L, temperature of 41°C and pH 5.1. Besides the main transfructosylation reaction between sucrose and tyrosol, several side reactions took place. A reaction network included also the formation of fructooligosaccharides and the hydrolysis of sucrose and all reaction products. This article is protected by copyright. All rights reserved.

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This article was published in the following journal.

Name: Biotechnology journal
ISSN: 1860-7314
Pages: e1800571

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