Aßmann, MiriamMiriamAßmannMügge, CarolinCarolinMüggeGaßmeyer, Sarah KatharinaSarah KatharinaGaßmeyerEnoki, JunichiJunichiEnokiHilterhaus, LutzLutzHilterhausKourist, RobertRobertKouristLiese, AndreasAndreasLieseKara, SelinSelinKara2018-02-092018-02-092017-03-16Frontiers in microbiology (8): 448- (2017)http://tubdok.tub.tuhh.de/handle/11420/1524The enzyme arylmalonate decarboxylase (AMDase) enables the selective synthesis of enantiopure (S)-arylpropinates in a simple single-step decarboxylation of dicarboxylic acid precursors. However, the poor enzyme stability with a half-life time of about 1.2 h under process conditions is a serious limitation of the productivity, which results in a need for high catalyst loads. By immobilization on an amino C2 acrylate carrier the operational stability of the (S)-selective AMDase variant G74C/M159L/C188G/V43I/A125P/V156L was increased to a half-life of about 8.6 days, which represents a 158-fold improvement. Further optimization was achieved by simple immobilization of the cell lysate to eliminate the cost- and time intensive enzyme purification step.en1664-302X2017448Frontiers Mediahttps://creativecommons.org/licenses/by/4.0/arylmalonate decarboxylasebiocatalysisenantioselectivityimmobilizationprocess stabilityprofenBiowissenschaften, BiologieJournal Articleurn:nbn:de:gbv:830-8821840910.15480/882.152111420/152410.3389/fmicb.2017.0044810.15480/882.1521Journal Article