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10.3762/bjoc.13.173 http://scihub22266oqcxt.onion/10.3762/bjoc.13.173 C5588541!5588541!28904622     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Beilstein+J+Org+Chem 2017 ; 13 (ä): 1788-95 Nephropedia Template TP {{tp|p=28904622|t=2017. Selective enzymatic esterification of lignin model compounds in the ball mill |pdf=|usr=}}{{28904622}} gab.com Text Selective enzymatic esterification of lignin model compounds in the ball mill JO: Beilstein J Org Chem http://www.kidney.de/pget.php?&tw=1&pmid=28904622 #FOAvip A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to afford monoesterified products. Amongst the tested lipases, CALB proved to be the most effective biocatalyst for these transformations. Noteworthy, various acyl donors of different chain lengths were tolerated under the mechanochemical conditions. Twit Text FOAVip Selective enzymatic esterification of lignin model compounds in the ball mill ????Beilstein J Org Chem http://www.kidney.de/pget.php?&tw=1&pmid=28904622 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28904622 #FOAvip English Wikipedia <ref>{{Cite pmid|28904622}}</ref> Selective enzymatic esterification of lignin model compounds in the ball mill #MMPMID28904622 Weißbach U; Dabral S; Konnert L; Bolm C; Hernández JG Beilstein J Org Chem 2017[]; 13 (ä): 1788-95 PMID28904622show ga A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to afford monoesterified products. Amongst the tested lipases, CALB proved to be the most effective biocatalyst for these transformations. Noteworthy, various acyl donors of different chain lengths were tolerated under the mechanochemical conditions. äSelective enzymatic esterification of lignin model compounds in the ba(epmc).pdf DeepDyve Pubget Overpricing