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• W1982712927 abstract "Abstract The potential applications of glycosyltransferases in glycoconjugate synthesis have attracted considerable interest from the biotechnology community in recent years. In this work, we present a novel glucosyltransferase from Catharanthus roseus cell cultures. The enzyme was purified to one spot in SDS-polyacrylamide gel electrophoresis, and its molecular weight was about 51 kDa. The optimum temperature was 35 °C, and the optimum pH was 7.6. Sodium ion has weak effect on enzyme activity, whereas divalent ions inhibit enzyme activity strongly. The K m values were 0.112, 0.077, 0.064 and 1.0 mM for scopoletin, 5,7-dihydroxyflavone, 5,7-dihydroxyflavanone and UDPG, respectively. Substrate screening with the purified enzyme was performed against a range of phenolic compounds using UDPG as sugar donor. The enzyme showed activity towards a number of coumarins including umbelliferone, scopoletin, isoscopoletin and esculetin, and flavonoids including a flavone, a flavanone and chalcones. No activity was detected with compounds characterized by a single aromatic ring, i.e. simple and acidic phenols. The substrate specificity and the regioselectivity suggest enzyme structural features that are different from those of other glucosyltransferases." @default.
• W1982712927 created "2016-06-24" @default.
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• W1982712927 date "2010-05-01" @default.
• W1982712927 modified "2023-09-26" @default.
• W1982712927 title "A novel glucosyltransferase from Catharanthus roseus cell suspensions" @default.
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• W1982712927 doi "https://doi.org/10.1016/j.procbio.2009.12.014" @default.
• W1982712927 hasPublicationYear "2010" @default.
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